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1. Apoptotic cell death in disease—Current understanding of the NCCD 2023

Author: Vitale, Ilio, Pietrocola, Federico, Guilbaud, Emma, Aaronson, Stuart A, Abrams, John M, Adam, Dieter, Agostini, Massimiliano, Agostinis, Patrizia, Alnemri, Emad S, Altucci, Lucia, Amelio, Ivano, Andrews, David W, Aqeilan, Rami I, Arama, Eli, Baehrecke, Eric H, Balachandran, Siddharth, Bano, Daniele, Barlev, Nickolai A, Bartek, Jiri, Bazan, Nicolas G, Becker, Christoph, Bernassola, Francesca, Bertrand, Mathieu JM, Bianchi, Marco E, Blagosklonny, Mikhail V, Blander, J Magarian, Blandino, Giovanni, Blomgren, Klas, Borner, Christoph, Bortner, Carl D, Bove, Pierluigi, Boya, Patricia, Brenner, Catherine, Broz, Petr, Brunner, Thomas, Damgaard, Rune Busk, Calin, George A, Campanella, Michelangelo, Candi, Eleonora, Carbone, Michele, Carmona-Gutierrez, Didac, Cecconi, Francesco, Chan, Francis K-M, Chen, Guo-Qiang, Chen, Quan, Chen, Youhai H, Cheng, Emily H, Chipuk, Jerry E, Cidlowski, John A, Ciechanover, Aaron, Ciliberto, Gennaro, Conrad, Marcus, Cubillos-Ruiz, Juan R, Czabotar, Peter E, D’Angiolella, Vincenzo, Daugaard, Mads, Dawson, Ted M, Dawson, Valina L, De Maria, Ruggero, De Strooper, Bart, Debatin, Klaus-Michael, Deberardinis, Ralph J, Degterev, Alexei, Del Sal, Giannino, Deshmukh, Mohanish, Di Virgilio, Francesco, Diederich, Marc, Dixon, Scott J, Dynlacht, Brian D, El-Deiry, Wafik S, Elrod, John W, Engeland, Kurt, Fimia, Gian Maria, Galassi, Claudia, Ganini, Carlo, Garcia-Saez, Ana J, Garg, Abhishek D, Garrido, Carmen, Gavathiotis, Evripidis, Gerlic, Motti, Ghosh, Sourav, Green, Douglas R, Greene, Lloyd A, Gronemeyer, Hinrich, Häcker, Georg, Hajnóczky, György, Hardwick, J Marie, Haupt, Ygal, He, Sudan, Heery, David M, Hengartner, Michael O, Hetz, Claudio, Hildeman, David A, Ichijo, Hidenori, Inoue, Satoshi, Jäättelä, Marja, Janic, Ana, Joseph, Bertrand, Jost, Philipp J, and Kanneganti, Thirumala-Devi
Subjects: Biochemistry and Cell Biology, Biological Sciences, 1.1 Normal biological development and functioning, 2.1 Biological and endogenous factors, Generic health relevance, Good Health and Well Being, Animals, Humans, Apoptosis, Cell Death, Caspases, Carcinogenesis, Mammals, Medical and Health Sciences, Biochemistry & Molecular Biology, Biological sciences, Biomedical and clinical sciences, Health sciences
Abstract: Apoptosis is a form of regulated cell death (RCD) that involves proteases of the caspase family. Pharmacological and genetic strategies that experimentally inhibit or delay apoptosis in mammalian systems have elucidated the key contribution of this process not only to (post-)embryonic development and adult tissue homeostasis, but also to the etiology of multiple human disorders. Consistent with this notion, while defects in the molecular machinery for apoptotic cell death impair organismal development and promote oncogenesis, the unwarranted activation of apoptosis promotes cell loss and tissue damage in the context of various neurological, cardiovascular, renal, hepatic, infectious, neoplastic and inflammatory conditions. Here, the Nomenclature Committee on Cell Death (NCCD) gathered to critically summarize an abundant pre-clinical literature mechanistically linking the core apoptotic apparatus to organismal homeostasis in the context of disease.
Published: 2023

2. Mitochondrial Stress-Initiated Aberrant Activation of the NLRP3 Inflammasome Regulates the Functional Deterioration of Hematopoietic Stem Cell Aging

Author: Luo, Hanzhi, Mu, Wei-Chieh, Karki, Rajendra, Chiang, Hou-Hsien, Mohrin, Mary, Shin, Jiyung J, Ohkubo, Rika, Ito, Keisuke, Kanneganti, Thirumala-Devi, and Chen, Danica
Subjects: Biochemistry and Cell Biology, Biological Sciences, Aging, Regenerative Medicine, Stem Cell Research, Stem Cell Research - Nonembryonic - Non-Human, Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, Inflammatory and immune system, Animals, Cellular Senescence, Hematopoietic Stem Cells, Inflammasomes, Mice, Mice, Knockout, Mitochondria, NLR Family, Pyrin Domain-Containing 3 Protein, Sirtuin 2, Stress, Physiological, NLRP3, SIRT2, SIRT3, SIRT7, aging, clonal hematopoiesis, hematopoietic stem cell, inflammasome, mitochondrial UPR, oxidative stress, Medical Physiology, Biological sciences
Abstract: Aging-associated defects in hematopoietic stem cells (HSCs) can manifest in their progeny, leading to aberrant activation of the NLRP3 inflammasome in macrophages and affecting distant tissues and organismal health span. Whether the NLRP3 inflammasome is aberrantly activated in HSCs during physiological aging is unknown. We show here that SIRT2, a cytosolic NAD+-dependent deacetylase, is required for HSC maintenance and regenerative capacity at an old age by repressing the activation of the NLRP3 inflammasome in HSCs cell autonomously. With age, reduced SIRT2 expression and increased mitochondrial stress lead to aberrant activation of the NLRP3 inflammasome in HSCs. SIRT2 overexpression, NLRP3 inactivation, or caspase 1 inactivation improves the maintenance and regenerative capacity of aged HSCs. These results suggest that mitochondrial stress-initiated aberrant activation of the NLRP3 inflammasome is a reversible driver of the functional decline of HSC aging and highlight the importance of inflammatory signaling in regulating HSC aging.
Published: 2019

3. The ketone metabolite β-hydroxybutyrate blocks NLRP3 inflammasome–mediated inflammatory disease

Author: Youm, Yun-Hee, Nguyen, Kim Y, Grant, Ryan W, Goldberg, Emily L, Bodogai, Monica, Kim, Dongin, D'Agostino, Dominic, Planavsky, Noah, Lupfer, Christopher, Kanneganti, Thirumala D, Kang, Seokwon, Horvath, Tamas L, Fahmy, Tarek M, Crawford, Peter A, Biragyn, Arya, Alnemri, Emad, and Dixit, Vishwa Deep
Subjects: Nutrition, 3-Hydroxybutyric Acid, Adult, Aged, Animals, Carrier Proteins, Caspase 1, Cryopyrin-Associated Periodic Syndromes, Diet, Ketogenic, Disease Models, Animal, Female, Humans, Inflammasomes, Inflammation, Interleukin-18, Interleukin-1beta, Male, Mice, Monocytes, NLR Family, Pyrin Domain-Containing 3 Protein, Potassium, Cryopyrin-associated Periodic Syndromes, Medical and Health Sciences, Immunology
Abstract: The ketone bodies β-hydroxybutyrate (BHB) and acetoacetate (AcAc) support mammalian survival during states of energy deficit by serving as alternative sources of ATP. BHB levels are elevated by starvation, caloric restriction, high-intensity exercise, or the low-carbohydrate ketogenic diet. Prolonged fasting reduces inflammation; however, the impact that ketones and other alternative metabolic fuels produced during energy deficits have on the innate immune response is unknown. We report that BHB, but neither AcAc nor the structurally related short-chain fatty acids butyrate and acetate, suppresses activation of the NLRP3 inflammasome in response to urate crystals, ATP and lipotoxic fatty acids. BHB did not inhibit caspase-1 activation in response to pathogens that activate the NLR family, CARD domain containing 4 (NLRC4) or absent in melanoma 2 (AIM2) inflammasome and did not affect non-canonical caspase-11, inflammasome activation. Mechanistically, BHB inhibits the NLRP3 inflammasome by preventing K(+) efflux and reducing ASC oligomerization and speck formation. The inhibitory effects of BHB on NLRP3 are not dependent on chirality or starvation-regulated mechanisms like AMP-activated protein kinase (AMPK), reactive oxygen species (ROS), autophagy or glycolytic inhibition. BHB blocks the NLRP3 inflammasome without undergoing oxidation in the TCA cycle, and independently of uncoupling protein-2 (UCP2), sirtuin-2 (SIRT2), the G protein-coupled receptor GPR109A or hydrocaboxylic acid receptor 2 (HCAR2). BHB reduces NLRP3 inflammasome-mediated interleukin (IL)-1β and IL-18 production in human monocytes. In vivo, BHB or a ketogenic diet attenuates caspase-1 activation and IL-1β secretion in mouse models of NLRP3-mediated diseases such as Muckle-Wells syndrome, familial cold autoinflammatory syndrome and urate crystal-induced peritonitis. Our findings suggest that the anti-inflammatory effects of caloric restriction or ketogenic diets may be linked to BHB-mediated inhibition of the NLRP3 inflammasome.
Published: 2015

4. It's just a phase: NLRP6 phase separations drive signaling

Author: Rebecca E. Tweedell and Thirumala-Devi Kanneganti
Subjects: Lipopolysaccharides, Inflammasomes, Receptors, Cell Surface, Cell Biology, Biology, Research Highlight, Article, CARD Signaling Adaptor Proteins, Intestines, Intrinsically Disordered Proteins, Teichoic Acids, Mice, Liver, Chemical physics, Phase (matter), Hepatocytes, Animals, RNA Viruses, Polylysine, Amino Acid Sequence, Molecular Biology, Protein Binding, RNA, Double-Stranded, Signal Transduction
Abstract: NLRP6 is important in host defense by inducing functional outcomes including inflammasome activation and interferon production. Here we show that NLRP6 undergoes liquid-liquid phase separation (LLPS) upon interaction with dsRNA in vitro and in cells, and that an intrinsically disordered poly-lysine sequence (K350–354) of NLRP6 is important for multivalent interactions, phase separation and inflammasome activation. Nlrp6-deficient or Nlrp6(K350−354A) mutant mice show reduced inflammasome activation upon mouse hepatitis virus or rotavirus infection, and in steady state stimulated by intestinal microbiota, implicating NLRP6 LLPS in anti-microbial immunity. Recruitment of ASC via helical assembly solidifies NLRP6 condensates, and ASC further recruits and activates caspase-1. Lipoteichoic acid, a known NLRP6 ligand, also promotes NLRP6 LLPS, and DHX15, a helicase in NLRP6-induced interferon signaling, co-forms condensates with NLRP6 and dsRNA. Thus, LLPS of NLRP6 is a common response to ligand stimulation, which serves to direct NLRP6 to distinct functional outcomes depending on the cellular context.
Published: 2023

5. AIM2 sensors mediate immunity to

Author: Camila, Marques-da-Silva, Barun, Poudel, Rodrigo P, Baptista, Kristen, Peissig, Lisa S, Hancox, Justine C, Shiau, Lecia L, Pewe, Melanie J, Shears, Thirumala-Devi, Kanneganti, Photini, Sinnis, Dennis E, Kyle, Prajwal, Gurung, John T, Harty, and Samarchith P, Kurup
Subjects: DNA-Binding Proteins, Plasmodium, Liver, Caspases, Hepatocytes, Animals, Humans, Parasites, Malaria
Abstract: Malaria, caused by
Published: 2023

6. Inflammasome-mediated GSDMD activation facilitates escape of Candida albicans from macrophages

Author: Hongbo Yu, Fei Liu, Hiroto Kambara, Xuemei Xie, Maikel Acosta-Zaldívar, Cunling Zhang, Julia R. Köhler, Jiajia Li, Hongbo R. Luo, Rongxia Guo, Ning-Ning Liu, Ting Bei, Fengxia Ma, Li Zhao, Xionghui Ding, Wenli Han, Xiaoyu Zhang, Wanjun Qi, and Apurva Kanneganti
Subjects: Programmed cell death, Inflammasomes, Science, Interleukin-1beta, General Physics and Astronomy, Kaplan-Meier Estimate, Kidney, Article, General Biochemistry, Genetics and Molecular Biology, Microbiology, Sepsis, Mediator, Candida albicans, medicine, Animals, Humans, Cells, Cultured, Mice, Knockout, Multidisciplinary, biology, Immune cell death, Macrophages, Caspase 1, Candidiasis, Intracellular Signaling Peptides and Proteins, Pyroptosis, Inflammasome, General Chemistry, Phosphate-Binding Proteins, medicine.disease, biology.organism_classification, Corpus albicans, Mice, Inbred C57BL, Host-Pathogen Interactions, Female, Infection, Candidalysin, medicine.drug
Abstract: Candida albicans is the most common cause of fungal sepsis. Inhibition of inflammasome activity confers resistance to polymicrobial and LPS-induced sepsis; however, inflammasome signaling appears to protect against C. albicans infection, so inflammasome inhibitors are not clinically useful for candidiasis. Here we show disruption of GSDMD, a known inflammasome target and key pyroptotic cell death mediator, paradoxically alleviates candidiasis, improving outcomes and survival of Candida-infected mice. Mechanistically, C. albicans hijacked the canonical inflammasome-GSDMD axis-mediated pyroptosis to promote their escape from macrophages, deploying hyphae and candidalysin, a pore-forming toxin expressed by hyphae. GSDMD inhibition alleviated candidiasis by preventing C. albicans escape from macrophages while maintaining inflammasome-dependent but GSDMD-independent IL-1β production for anti-fungal host defenses. This study demonstrates key functions for GSDMD in Candida’s escape from host immunity in vitro and in vivo and suggests that GSDMD may be a potential therapeutic target in C. albicans-induced sepsis., Inflammasome signalling has been shown to protect Candida albicans during infection and as such limits inflammasome inhibitors in this context. Here the authors implicate Gasdermin D in C.ablicans immune evasion and suggests its targeting therapeutically.
Published: 2021

7. Determining distinct roles of IL-1α through generation of an IL-1α knockout mouse with no defect in IL-1β expression

Author: R.K. Subbarao Malireddi, Ratnakar Bynigeri, Balabhaskararao Kancharana, Bhesh Raj Sharma, Amanda R. Burton, Stephane Pelletier, and Thirumala-Devi Kanneganti
Subjects: Mice, Knockout, Mice, Inflammasomes, Interleukin-1alpha, Macrophages, Interleukin-8, Immunology, Animals, Immunology and Allergy
Abstract: Interleukin 1α (IL-1α) and IL-1β are the founding members of the IL-1 cytokine family, and these innate immune inflammatory mediators are critically important in health and disease. Early studies on these molecules suggested that their expression was interdependent, with an initial genetic model of IL-1α depletion, the IL-1α KO mouse (Il1a-KOline1), showing reduced IL-1β expression. However, studies using this line in models of infection and inflammation resulted in contrasting observations. To overcome the limitations of this genetic model, we have generated and characterized a new line of IL-1α KO mice (Il1a-KOline2) using CRISPR-Cas9 technology. In contrast to cells from theIl1a-KOline1, where IL-1β expression was drastically reduced, bone marrow-derived macrophages (BMDMs) fromIl1a-KOline2mice showed normal induction and activation of IL-1β. Additionally,Il1a-KOline2BMDMs showed normal inflammasome activation and IL-1β expression in response to multiple innate immune triggers, including both pathogen-associated molecular patterns and pathogens. Moreover, usingIl1a-KOline2cells, we confirmed that IL-1α, independent of IL-1β, is critical for the expression of the neutrophil chemoattractant KC/CXCL1. Overall, we report the generation of a new line of IL-1α KO mice and confirm functions for IL-1α independent of IL-1β. Future studies on the unique functions of IL-1α and IL-1β using these mice will be critical to identify new roles for these molecules in health and disease and develop therapeutic strategies.
Published: 2022
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8. AIM2 forms a complex with pyrin and ZBP1 to drive PANoptosis and host defence

Author: Ravi C. Kalathur, SangJoon Lee, Thirumala-Devi Kanneganti, Lam Nhat Nguyen, Rajendra Karki, and Yaqiu Wang
Subjects: Male, Damp, THP-1 Cells, Apoptosis, Herpesvirus 1, Human, medicine.disease_cause, Pyrin domain, Mice, RIPK1, AIM2, Pyroptosis, medicine, Animals, Humans, FADD, Francisella novicida, Francisella, Cells, Cultured, Multidisciplinary, Innate immune system, biology, Caspase 1, RNA-Binding Proteins, Inflammasome, Pyrin, Cell biology, DNA-Binding Proteins, Mice, Inbred C57BL, Necroptosis, biology.protein, Cytokines, Female, medicine.drug
Abstract: Inflammasomes are important sentinels of innate immune defence, sensing pathogens and inducing cell death in infected cells1. There are several inflammasome sensors that each detect and respond to a specific pathogen- or damage-associated molecular pattern (PAMP or DAMP, respectively)1. During infection, live pathogens can induce the release of multiple PAMPs and DAMPs, which can simultaneously engage multiple inflammasome sensors2–5. Here we found that AIM2 regulates the innate immune sensors pyrin and ZBP1 to drive inflammatory signalling and a form of inflammatory cell death known as PANoptosis, and provide host protection during infections with herpes simplex virus 1 and Francisella novicida. We also observed that AIM2, pyrin and ZBP1 were members of a large multi-protein complex along with ASC, caspase-1, caspase-8, RIPK3, RIPK1 and FADD, that drove inflammatory cell death (PANoptosis). Collectively, our findings define a previously unknown regulatory and molecular interaction between AIM2, pyrin and ZBP1 that drives assembly of an AIM2-mediated multi-protein complex that we term the AIM2 PANoptosome and comprising multiple inflammasome sensors and cell death regulators. These results advance the understanding of the functions of these molecules in innate immunity and inflammatory cell death, suggesting new therapeutic targets for AIM2-, ZBP1- and pyrin-mediated diseases. AIM2 responds to infection with herpes simplex virus 1 or Francisella novicida by driving assembly of a large multi-protein complex containing multiple inflammasome sensors and cell death regulators.
Published: 2021

9. Humans pIKK-up NLRP3 to skip NEK7

Author: R.K. Subbarao Malireddi and Thirumala-Devi Kanneganti
Subjects: Mice, Inbred C57BL, Mice, Inflammasomes, Immunology, NLR Family, Pyrin Domain-Containing 3 Protein, Immunology and Allergy, Humans, Animals, NIMA-Related Kinases, Protein Serine-Threonine Kinases
Abstract: NLRP3 inflammasome regulation is essential for controlling cell death and inflammation. Mechanistic studies in murine cells suggest a two-step model of priming and activation with an indispensable role for NEK7. However, in a recent article in Immunity, Schmacke et al. report that, in humans, transcription-independent NLRP3 activation occurs by circumventing NEK7 via IKKβ.
Published: 2022

10. Single cell analysis of PANoptosome cell death complexes through an expansion microscopy method

Author: Yaqiu Wang, Nagakannan Pandian, Joo-Hui Han, Balamurugan Sundaram, SangJoon Lee, Rajendra Karki, Clifford S. Guy, and Thirumala-Devi Kanneganti
Subjects: Pharmacology, Caspase 8, Mice, Microscopy, Cellular and Molecular Neuroscience, Inflammasomes, Pyroptosis, Animals, Molecular Medicine, Apoptosis, Cell Biology, Single-Cell Analysis, Molecular Biology
Abstract: In response to infection or sterile insults, inflammatory programmed cell death is an essential component of the innate immune response to remove infected or damaged cells. PANoptosis is a unique innate immune inflammatory cell death pathway regulated by multifaceted macromolecular complexes called PANoptosomes, which integrate components from other cell death pathways. Growing evidence shows that PANoptosis can be triggered in many physiological conditions, including viral and bacterial infections, cytokine storms, and cancers. However, PANoptosomes at the single cell level have not yet been fully characterized. Initial investigations have suggested that key pyroptotic, apoptotic, and necroptotic molecules including the inflammasome adaptor protein ASC, apoptotic caspase-8 (CASP8), and necroptotic RIPK3 are conserved components of PANoptosomes. Here, we optimized an immunofluorescence procedure to probe the highly dynamic multiprotein PANoptosome complexes across various innate immune cell death-inducing conditions. We first identified and validated antibodies to stain endogenous mouse ASC, CASP8, and RIPK3, without residual staining in the respective knockout cells. We then assessed the formation of PANoptosomes across innate immune cell death-inducing conditions by monitoring the colocalization of ASC with CASP8 and/or RIPK3. Finally, we established an expansion microscopy procedure using these validated antibodies to image the organization of ASC, CASP8, and RIPK3 within the PANoptosome. This optimized protocol, which can be easily adapted to study other multiprotein complexes and other cell death triggers, provides confirmation of PANoptosome assembly in individual cells and forms the foundation for a deeper molecular understanding of the PANoptosome complex and PANoptosis to facilitate therapeutic targeting.
Published: 2022

11. TLR and IKK Complex–Mediated Innate Immune Signaling Inhibits Stress Granule Assembly

Author: Parimal Samir, David E. Place, R. K. Subbarao Malireddi, and Thirumala-Devi Kanneganti
Subjects: Mice, Knockout, Innate immune system, Chemistry, Endoplasmic reticulum, p38 mitogen-activated protein kinases, Toll-Like Receptors, Immunology, Pattern recognition receptor, IRAK1, Immunity, Innate, Stress Granules, I-kappa B Kinase, Cell biology, Mice, 03 medical and health sciences, 0302 clinical medicine, Stress granule, Animals, Immunology and Allergy, Stress granule assembly, Kinase activity, Cells, Cultured, Signal Transduction, 030215 immunology
Abstract: Cellular stress can induce cytoplasmic ribonucleoprotein complexes called stress granules that allow the cells to survive. Stress granules are also central to cellular responses to infections, in which they can act as platforms for viral sensing or modulate innate immune signaling through pattern recognition receptors. However, the effect of innate immune signaling on stress granules is poorly understood. In this study, we report that prior induction of innate immune signaling through TLRs inhibited stress granule assembly in a TLR ligand dose-dependent manner in murine bone marrow–derived macrophages. Time course analysis suggests that TLR stimulation can reverse stress granule assembly even after it has begun. Additionally, both MYD88- and TRIF-mediated TLR signaling inhibited stress granule assembly in response to endoplasmic reticulum stress in bone marrow–derived macrophages and the chemotherapeutic drug oxaliplatin in murine B16 melanoma cells. This inhibition was not due to a decrease in expression of the critical stress granule proteins G3BP1 and DDX3X and was independent of IRAK1/4, JNK, ERK and P38 kinase activity but dependent on IKK complex kinase activity. Overall, we have identified the TLR–IKK complex signaling axis as a regulator of stress granule assembly–disassembly dynamics, highlighting cross-talk between processes that are critical in health and disease.
Published: 2021

12. Inflammatory Cell Death, PANoptosis, Mediated by Cytokines in Diverse Cancer Lineages Inhibits Tumor Growth

Author: R. K. Subbarao Malireddi, Parimal Samir, Balabhaskararao Kancharana, Thirumala-Devi Kanneganti, SangJoon Lee, Balamurugan Sundaram, and Rajendra Karki
Subjects: Programmed cell death, Necroptosis, medicine.medical_treatment, Immunology, Immunogenic Cell Death, Article, Interferon-gamma, Mice, Cell Line, Tumor, Neoplasms, Animals, Humans, Immunology and Allergy, Medicine, Cytotoxic T cell, Tumor Necrosis Factor-alpha, business.industry, Pyroptosis, Cancer, General Medicine, Immunotherapy, medicine.disease, Xenograft Model Antitumor Assays, Apoptosis, Cancer cell, Cancer research, business, Signal Transduction
Abstract: Resistance to cell death is a hallmark of cancer. Immunotherapy, particularly immune checkpoint blockade therapy, drives immune-mediated cell death and has greatly improved treatment outcomes for some patients with cancer, but it often fails clinically. Its success relies on the cytokines and cytotoxic functions of effector immune cells to bypass the resistance to cell death and eliminate cancer cells. However, the specific cytokines capable of inducing cell death in tumors and the mechanisms that connect cytokines to cell death across cancer cell types remain unknown. In this study, we analyzed expression of several cytokines that are modulated in tumors and found correlations between cytokine expression and mortality. Of several cytokines tested for their ability to kill cancer cells, only TNF-α and IFN-γ together were able to induce cell death in 13 distinct human cancer cell lines derived from colon and lung cancer, melanoma, and leukemia. Further evaluation of the specific programmed cell death pathways activated by TNF-α and IFN-γ in these cancer lines identified PANoptosis, a form of inflammatory cell death that was previously shown to be activated by contemporaneous engagement of components from pyroptosis, apoptosis, and/or necroptosis. Specifically, TNF-α and IFN-γ triggered activation of gasdermin D, gasdermin E, caspase-8, caspase-3, caspase-7, and MLKL. Furthermore, the intratumoral administration of TNF-α and IFN-γ suppressed the growth of transplanted xenograft tumors in an NSG mouse model. Overall, this study shows that PANoptosis, induced by synergism of TNF-α and IFN-γ, is an important mechanism to kill cancer cells and suppress tumor growth that could be therapeutically targeted.
Published: 2021

13. ZBP1-dependent inflammatory cell death, PANoptosis, and cytokine storm disrupt IFN therapeutic efficacy during coronavirus infection

Author: Rajendra Karki, SangJoon Lee, Raghvendra Mall, Nagakannan Pandian, Yaqiu Wang, Bhesh Raj Sharma, RK Subbarao Malireddi, Dong Yang, Sanja Trifkovic, Jacob A. Steele, Jon P. Connelly, Gella Vishwanath, Mitnala Sasikala, Duvvur Nageshwar Reddy, Peter Vogel, Shondra M. Pruett-Miller, Richard Webby, Colleen Beth Jonsson, and Thirumala-Devi Kanneganti
Subjects: Mice, Cell Death, SARS-CoV-2, Immunology, Animals, Humans, RNA-Binding Proteins, General Medicine, Interferons, Cytokine Release Syndrome, Pandemics, COVID-19 Drug Treatment
Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the virus responsible for coronavirus disease 2019 (COVID-19), continues to cause substantial morbidity and mortality in the ongoing global pandemic. Understanding the fundamental mechanisms that govern innate immune and inflammatory responses during SARS-CoV-2 infection is critical for developing effective therapeutic strategies. Whereas interferon (IFN)–based therapies are generally expected to be beneficial during viral infection, clinical trials in COVID-19 have shown limited efficacy and potential detrimental effects of IFN treatment during SARS-CoV-2 infection. However, the underlying mechanisms responsible for this failure remain unknown. In this study, we found that IFN induced Z-DNA-binding protein 1 (ZBP1)–mediated inflammatory cell death, PANoptosis, in human and murine macrophages and in the lungs of mice infected with β-coronaviruses, including SARS-CoV-2 and mouse hepatitis virus (MHV). In patients with COVID-19, expression of the innate immune sensor ZBP1 was increased in immune cells from those who succumbed to the disease compared with those who recovered, further suggesting a link between ZBP1 and pathology. In mice, IFN-β treatment after β-coronavirus infection increased lethality, and genetic deletion of Zbp1 or its Zα domain suppressed cell death and protected the mice from IFN-mediated lethality during β-coronavirus infection. Overall, our results identify that ZBP1 induced during coronavirus infection limits the efficacy of IFN therapy by driving inflammatory cell death and lethality. Therefore, inhibiting ZBP1 activity may improve the efficacy of IFN therapy, paving the way for the development of new and critically needed therapeutics for COVID-19 as well as other infections and inflammatory conditions where IFN-mediated cell death and pathology occur.
Published: 2022

14. The innate immune system and cell death in autoinflammatory and autoimmune disease

Author: David E. Place and Thirumala-Devi Kanneganti
Subjects: 0301 basic medicine, Programmed cell death, Necroptosis, Immunology, Inflammation, Autoimmune Diseases, 03 medical and health sciences, 0302 clinical medicine, Immune system, Immunity, medicine, Animals, Humans, Immunology and Allergy, Autoimmune disease, Innate immune system, business.industry, Pyroptosis, biochemical phenomena, metabolism, and nutrition, medicine.disease, Immunity, Innate, 030104 developmental biology, Immune System, medicine.symptom, business, 030215 immunology
Abstract: The innate immune system, the first line of defense against pathogens and host tissue damage, initiates pro-inflammatory responses which, when dysregulated, promote inflammation to drive a broad range of autoimmune diseases. Immunomodulatory therapies have been developed to successfully treat several autoimmune diseases, but still many others lack effective treatments. Here, we explore recent advances in how the innate immune system contributes to autoinflammation, from the innate immune sensors that initiate immune responses to how this system regulates the activation of programmed cell death pathways including pyroptosis, apoptosis, necroptosis, and PANoptosis, which involves machinery from the pyroptotic, apoptotic, and necroptotic pathways. Recent advances in our understanding of innate immunity raise important considerations for developing new inflammatory disease treatments that target innate immune signaling and programmed cell death pathways.
Published: 2020

15. DEAD/H-Box Helicases in Immunity, Inflammation, Cell Differentiation, and Cell Death and Disease

Author: Parimal Samir and Thirumala-Devi Kanneganti
Subjects: DEAD-box RNA Helicases, Inflammation, Mammals, Cell Death, DNA Helicases, Animals, Humans, RNA, Cell Differentiation, General Medicine
Abstract: DEAD/H-box proteins are the largest family of RNA helicases in mammalian genomes, and they are present in all kingdoms of life. Since their discovery in the late 1980s, DEAD/H-box family proteins have been a major focus of study. They have been found to play central roles in RNA metabolism, gene expression, signal transduction, programmed cell death, and the immune response to bacterial and viral infections. Aberrant functions of DEAD/H-box proteins have been implicated in a wide range of human diseases that include cancer, neurodegeneration, and inherited genetic disorders. In this review, we provide a historical context and discuss the molecular functions of DEAD/H-box proteins, highlighting the recent discoveries linking their dysregulation to human diseases. We will also discuss the state of knowledge regarding two specific DEAD/H-box proteins that have critical roles in immune responses and programmed cell death, DDX3X and DDX58, also known as RIG-I. Given their importance in homeostasis and disease, an improved understanding of DEAD/H-box protein biology and protein–protein interactions will be critical for informing strategies to counteract the pathogenesis associated with several human diseases.
Published: 2022

16. NLRC4 Deficiency Leads to Enhanced Phosphorylation of MLKL and Necroptosis

Author: Rajendra Karki, Balamurugan Sundaram, and Thirumala-Devi Kanneganti
Subjects: Mice, Inflammasomes, Caspases, Macrophages, Immunology, Necroptosis, Immunology and Allergy, Animals, General Medicine, Phosphorylation, Protein Kinases, Article, Neuronal Apoptosis-Inhibitory Protein
Abstract: Hosts rely on the innate immune system to clear pathogens in response to infection. Pathogen-associated molecular patterns bind to innate immune receptors and engage activation of downstream signaling to initiate a host immune response to fight infection. A key component of this innate response is programmed cell death. Recent work has highlighted significant cross-talk and functional redundancy between cell death pathways, leading to the discovery of PANoptosis, an inflammatory programmed cell death pathway dependent on PANoptosomes, which are innate immune danger-sensing complexes that activate inflammatory cell death and contain caspases with or without inflammasome components and receptor interacting protein homotypic interaction motif–containing proteins. Although PANoptosis has been characterized in response to a growing number of pathogens, inflammatory diseases, and cancer, its role and the functional consequences of PANoptotic component modulation during NLR family CARD domain-containing protein 4 (NLRC4) activation by Pseudomonas aeruginosa infection remain unknown. In this study, we show that P. aeruginosa can induce PANoptosis in mouse bone marrow–derived macrophages (BMDMs). Only the combined deletion of caspase-1, -11, -8, and RIPK3 protected mouse BMDMs from cell death. Moreover, we showed that PANoptotic components act in a compensatory manner; in the absence of NAIP5 and NLRC4 during P. aeruginosa challenge, activation of caspase-1, -3, -7, and -8 was reduced, whereas alternative cell death molecules such as RIPK1 and MLKL were activated in mouse BMDMs. Taken together, these data highlight the extensive cross-talk between cell death signaling molecules and showcase the plasticity of the system.
Published: 2022

17. Innate immunity: the first line of defense against SARS-CoV-2

Author: Michael S. Diamond and Thirumala-Devi Kanneganti
Subjects: Inflammasomes, SARS-CoV-2, Immunology, Toll-Like Receptors, COVID-19, NLR Proteins, Virus Internalization, Article, Immunity, Innate, Receptors, Pattern Recognition, Immunology and Allergy, Animals, Cytokines, Humans, Immune Evasion, Signal Transduction
Abstract: The coronavirus disease 2019 (COVID-19) pandemic, caused by SARS-CoV-2, continues to cause substantial morbidity and mortality. While most infections are mild, some patients experience severe and potentially fatal systemic inflammation, tissue damage, cytokine storm and acute respiratory distress syndrome. The innate immune system acts as the first line of defense, sensing the virus through pattern recognition receptors and activating inflammatory pathways that promote viral clearance. Here, we discuss the innate immune processes involved in virus recognition and the resultant inflammation, and how this insight has enabled the development of therapeutic interventions against COVID-19. An improved understanding of how the innate immune system detects and responds to SARS-CoV-2 will help identify targeted therapeutic modalities that mitigate severe disease and improve patient outcomes.
Published: 2022

18. A comprehensive guide to studying inflammasome activation and cell death

Author: Rebecca E. Tweedell, R. K. Subbarao Malireddi, and Thirumala-Devi Kanneganti
Subjects: Male, Programmed cell death, Inflammasomes, Interleukin-1beta, Cell, Apoptosis, Article, General Biochemistry, Genetics and Molecular Biology, Mice, 03 medical and health sciences, 0302 clinical medicine, In vivo, Image Processing, Computer-Assisted, medicine, Animals, 030304 developmental biology, 0303 health sciences, Innate immune system, Cell Death, L-Lactate Dehydrogenase, Chemistry, Macrophages, Caspase 1, Interleukin-18, Pattern recognition receptor, Inflammasome, Immunity, Innate, Neoplasm Proteins, Cell biology, Mice, Inbred C57BL, medicine.anatomical_structure, Female, Inflammasome complex, 030217 neurology & neurosurgery, medicine.drug
Abstract: Inflammasomes are multimeric heterogeneous mega-Dalton protein complexes that play key roles in the host innate immune response to infection and sterile insults. Assembly of the inflammasome complex following infection or injury begins with the oligomerization of the upstream inflammasome-forming sensor and proceeds through a multistep process of well-coordinated events and downstream effector functions. Together, these steps enable elegant experimental readouts with which to reliably assess the successful activation of the inflammasome complex and cell death. Here, we describe a comprehensive protocol that details several in vitro (in bone marrow–derived macrophages) and in vivo (in mice) strategies for activating the inflammasome and explain how to subsequently assess multiple downstream effects in parallel to unequivocally establish the activation status of the inflammasome and cell death pathways. Our workflow assesses inflammasome activation via the formation of the apoptosis-associated speck-like protein containing a CARD (ASC) speck; cleavage of caspase-1 and gasdermin D; release of IL-1β, IL-18, caspase-1, and lactate dehydrogenase from the cell; and real-time analysis of cell death by imaging. Analyses take up to ~24 h to complete. Overall, our multifaceted approach provides a comprehensive and consistent protocol for assessing inflammasome activation and cell death. This protocol describes a toolbox for comprehensive characterization of inflammasome activation and cell death in response to both in vivo (in mice) and in vitro (using bone marrow–derived macrophages) models of infection, sterile insults, and cancer.
Published: 2020

19. Acute IL-4 Governs Pathogenic T Cell Responses during Leishmania major Infection

Author: Barun Poudel, Scott A. Brown, Prajwal Gurung, Lalita Mazgaeen, Matthew S. Yorek, and Thirumala-Devi Kanneganti
Subjects: CD4-Positive T-Lymphocytes, T cell, Immunology, Leishmaniasis, Cutaneous, CD8-Positive T-Lymphocytes, Neutralization, Article, Interferon-gamma, Mice, Immune system, Th2 Cells, Cutaneous leishmaniasis, medicine, Immunology and Allergy, Animals, Humans, Leishmania major, Interleukin 4, Mice, Inbred BALB C, biology, General Medicine, Th1 Cells, Leishmania, biology.organism_classification, medicine.disease, medicine.anatomical_structure, Interleukin-4, CD8
Abstract: Leishmania spp. infection is a global health problem affecting more than 2 million people every year with 300 million at risk worldwide. It is well established that a dominant Th1 response (IFN-γ, a hallmark Th1 cytokine) provides resistance, whereas a dominant Th2 response (IL-4, a hallmark Th2 cytokine) confers susceptibility during infection. Given the important role of IL-4 during L. major infection, we used IL-4–neutralizing Abs to investigate the cellular and molecular events regulated by IL-4 signaling. As previously published, neutralization of IL-4 in L. major–infected BALB/c mice (a Leishmania susceptible strain) provided protection when compared with control L. major–infected BALB/c mice. Despite this protection, IFN-γ production by T cells was dramatically reduced. Temporal neutralization of IL-4 revealed that acute IL-4 produced within the first days of infection is critical for not only programming IL-4–producing Th2 CD4+ T cells, but for promoting IFN-γ produced by CD8+ T cells. Mechanistically, IL-4 signaling enhances anti-CD3–induced Tbet and IFN-γ expression in both CD4+ and CD8+ T cells. Given the pathogenic role of IFN-γ–producing CD8+ T cells, our data suggest that IL-4 promotes cutaneous leishmaniasis pathology by not only promoting Th2 immune responses but also pathogenic CD8+ T cell responses. Our studies open new research grounds to investigate the unsuspected role of IL-4 in regulating both Th1 and Th2 responses.
Published: 2020

20. DDX3X Sits at the Crossroads of Liquid–Liquid and Prionoid Phase Transitions Arbitrating Life and Death Cell Fate Decisions in Stressed Cells

Author: Parimal Samir and Thirumala-Devi Kanneganti
Subjects: 0301 basic medicine, Cell, Cell fate determination, Biology, DNACB Bit, DEAD-box RNA Helicases, 03 medical and health sciences, 0302 clinical medicine, Stress granule, Genetics, medicine, Animals, Humans, Stress granule assembly, Molecular Biology, Innate immune system, Cell Death, integumentary system, Inflammasome, Receptor Cross-Talk, Cell Biology, General Medicine, Cell biology, Crosstalk (biology), 030104 developmental biology, medicine.anatomical_structure, 030220 oncology & carcinogenesis, Signal transduction, Signal Transduction, medicine.drug
Abstract: The crosstalk between cellular stress responses and innate immune signaling pathways remains poorly understood. Cells can respond to stressors by assembling stress granules that store 40S ribosomes, translation initiation factors, and mRNAs, and allow the cell to survive. Some stressors can activate the NLRP3 inflammasome, which leads to pyroptotic cell death. Stress granules and the NLRP3 inflammasome provide distinct cell fate choices to the cell. These complexes also involve distinct types of phase transitions-liquid-liquid phase separation for stress granules and prionoid phase transition for the NLRP3 inflammasome. We recently reported that DDX3X modulates this crosstalk by acting as a common essential factor for NLRP3 inflammasome activation and stress granule assembly. Here, we discuss the role of DDX3X in modulating the liquid-liquid phase separation and prionoid phase transition required for making cell fate decisions under stress conditions.
Published: 2020

21. Caspases in Cell Death, Inflammation, and Pyroptosis

Author: Sannula Kesavardhana, R. K. Subbarao Malireddi, and Thirumala-Devi Kanneganti
Subjects: 0301 basic medicine, Proteases, Programmed cell death, Immunology, Apoptosis, Inflammation, Article, 03 medical and health sciences, 0302 clinical medicine, Pyroptosis, medicine, Animals, Humans, Immunology and Allergy, Caspase, Innate immune system, Cell Death, biology, Inflammasome, Neoplasm Proteins, Cell biology, Enzyme Activation, Multicellular organism, 030104 developmental biology, Caspases, 030220 oncology & carcinogenesis, biology.protein, Disease Susceptibility, medicine.symptom, Biomarkers, Signal Transduction, medicine.drug
Abstract: Caspases are a family of conserved cysteine proteases that play key roles in programmed cell death and inflammation. In multicellular organisms, caspases are activated via macromolecular signaling complexes that bring inactive procaspases together and promote their proximity-induced autoactivation and proteolytic processing. Activation of caspases ultimately results in programmed execution of cell death, and the nature of this cell death is determined by the specific caspases involved. Pioneering new research has unraveled distinct roles and cross talk of caspases in the regulation of programmed cell death, inflammation, and innate immune responses. In-depth understanding of these mechanisms is essential to foster the development of precise therapeutic targets to treat autoinflammatory disorders, infectious diseases, and cancer. This review focuses on mechanisms governing caspase activation and programmed cell death with special emphasis on the recent progress in caspase cross talk and caspase-driven gasdermin D–induced pyroptosis.
Published: 2020

22. The nonreceptor tyrosine kinase SYK drives caspase-8/NLRP3 inflammasome-mediated autoinflammatory osteomyelitis

Author: Thirumala-Devi Kanneganti, Balaji Banoth, Tejasvi Krishna Dasari, Bhesh Raj Sharma, Amanda R. Burton, Rechel Geiger, Prajwal Gurung, and Rajendra Karki
Subjects: 0301 basic medicine, Inflammasomes, Interleukin-1beta, Syk, Biology, Caspase 8, Biochemistry, 03 medical and health sciences, AIM2, NLR Family, Pyrin Domain-Containing 3 Protein, medicine, Animals, Syk Kinase, Protein kinase A, Molecular Biology, Inflammation, 030102 biochemistry & molecular biology, Chronic recurrent multifocal osteomyelitis, NF-kappa B, Osteomyelitis, Inflammasome, Cell Biology, medicine.disease, Cell biology, CARD Signaling Adaptor Proteins, DNA-Binding Proteins, Mice, Inbred C57BL, 030104 developmental biology, Receptor-Interacting Protein Serine-Threonine Kinases, Disease Progression, Editors' Picks Highlights, Signal transduction, Tyrosine kinase, Signal Transduction, medicine.drug
Abstract: Chronic recurrent multifocal osteomyelitis (CRMO) in humans can be modeled in Pstpip2cmo mice, which carry a missense mutation in the proline–serine–threonine phosphatase–interacting protein 2 (Pstpip2) gene. As cmo disease in mice, the experimental model analogous to human CRMO, is mediated specifically by IL-1β and not by IL-1α, delineating the molecular pathways contributing to pathogenic IL-1β production is crucial to developing targeted therapies. In particular, our earlier findings support redundant roles of NLR family pyrin domain-containing 3 (NLRP3) and caspase-1 with caspase-8 in instigating cmo. However, the signaling components upstream of caspase-8 and pro-IL-1β cleavage in Pstpip2cmo mice are not well-understood. Therefore, here we investigated the signaling pathways in these mice and discovered a central role of a nonreceptor tyrosine kinase, spleen tyrosine kinase (SYK), in mediating osteomyelitis. Using several mutant mouse strains, immunoblotting, and microcomputed tomography, we demonstrate that absent in melanoma 2 (AIM2), receptor-interacting serine/ threonine protein kinase 3 (RIPK3), and caspase recruitment domain–containing protein 9 (CARD9) are each dispensable for osteomyelitis induction in Pstpip2cmo mice, whereas genetic deletion of Syk completely abrogates the disease phenotype. We further show that SYK centrally mediates signaling upstream of caspase-1 and caspase-8 activation and principally up-regulates NF-κB and IL-1β signaling in Pstpip2cmo mice, thereby inducing cmo. These results provide a rationale for directly targeting SYK and its downstream signaling components in CRMO.
Published: 2020

23. Inflammasomes and the fine line between defense and disease

Author: Shelbi Christgen and Thirumala-Devi Kanneganti
Subjects: 0301 basic medicine, NLRP6, Inflammasomes, Extramural, Immunology, Inflammasome, Disease, Biology, Fine line, Article, Cell biology, 03 medical and health sciences, 030104 developmental biology, 0302 clinical medicine, medicine, Animals, Humans, Immunology and Allergy, 030215 immunology, medicine.drug, Interferon regulatory factors
Abstract: Recognition of invading pathogens and execution of defensive responses are crucial steps in successfully combating infectious diseases. Inflammasomes are a group of diverse, signal-transducing complexes with key roles in both processes. While the responses mediated by inflammasomes are vital to host defense, aberrations in inflammasome regulation or activity can lead to the development of autoimmune and sterile inflammatory diseases, including cancer. The field of inflammasome research has rapidly expanded to identify novel regulatory pathways, new inflammasome components, and the mechanistic details of the activation of these complexes. In this review, we discuss recent insights into the regulation of inflammasomes by interferon regulatory factor proteins, newly discovered mechanisms of activation for the NLRP1b and NLRP6 inflammasomes, and recent studies exploring the viability of inflammasome-modulating immunotherapies.
Published: 2020

24. Deletion of haematopoietic Dectin-2 or CARD9 does not protect from atherosclerosis development under hyperglycaemic conditions

Author: Janna A. van Diepen, Jimmy F.P. Berbée, Geerte Hoeke, Thirumala D. Kanneganti, Patrick C.N. Rensen, Tom Houben, Anneke Hijmans, Kathrin Thiem, Mariëtte R. Boon, Isabel M. Mol, Rinke Stienstra, Esther Lutgens, Margien G.S. Boels, Cees J. Tack, Ronit Shiri-Sverdlov, Enchen Zhou, Mihai G. Netea, Johan Bussink, Medical Biochemistry, ACS - Atherosclerosis & ischemic syndromes, AII - Inflammatory diseases, Moleculaire Genetica, and RS: NUTRIM - R2 - Liver and digestive health
Subjects: Blood Glucose, Male, Endocrinology, Diabetes and Metabolism, lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], 030204 cardiovascular system & hematology, LECTIN RECEPTORS, RAGE (receptor), Voeding, Metabolisme en Genomica, 0302 clinical medicine, Antigens, Ly, Receptor, Aorta, Cells, Cultured, Bone Marrow Transplantation, Mice, Knockout, RISK, 0303 health sciences, biology, CHOLESTEROL, Pattern recognition receptor, Metabolic Disorders Radboud Institute for Molecular Life Sciences [Radboudumc 6], Plaque, Atherosclerotic, RAGE, Metabolism and Genomics, macrophages, Haematopoiesis, CARDIOVASCULAR-DISEASE, monocytes/macrophages, Metabolisme en Genomica, Cytokines, Nutrition, Metabolism and Genomics, Original Article, LIGANDS, Collagen, medicine.symptom, Cardiology and Cardiovascular Medicine, monocytes, Rare cancers Radboud Institute for Health Sciences [Radboudumc 9], Dectin-2, EXPRESSION, Aortic Diseases, Inflammation, Diabetes Mellitus, Experimental, 03 medical and health sciences, Voeding, TLR, Internal Medicine, medicine, Monocytes macrophages, Animals, Genetic Predisposition to Disease, Lectins, C-Type, 030304 developmental biology, VLAG, Nutrition, business.industry, Lectin, Hematopoietic Stem Cells, Atherosclerosis, CARD Signaling Adaptor Proteins, Mice, Inbred C57BL, MICE, Receptors, LDL, Diet, Western, inflammation, Immunology, biology.protein, Macrophages, Peritoneal, business, C-type lectin receptors, CARD9, Biomarkers, Gene Deletion, hyperglycaemia
Abstract: Background: C-type lectin receptors, including Dectin-2, are pattern recognition receptors on monocytes and macrophages that mainly recognize sugars and sugar-like structures present on fungi. Activation of C-type lectin receptors induces downstream CARD9 signalling, leading to the production of cytokines. We hypothesized that under hyperglycaemic conditions, as is the case in diabetes mellitus, glycosylated protein (sugar-like) structures activate C-type lectin receptors, leading to immune cell activation and increased atherosclerosis development. Methods: Low-density lipoprotein receptor-deficient mice were lethally irradiated and transplanted with bone marrow from control wild-type, Dectin-2−/− or Card9−/− mice. After 6 weeks of recovery, mice received streptozotocin injections (50 mg/g BW; 5 days) to induce hyperglycaemia. After an additional 2 weeks, mice were fed a Western-type diet (0.1% cholesterol) for 10 weeks. Results and Conclusion: Deletion of haematopoietic Dectin-2 reduced the number of circulating Ly6Chi monocytes, increased pro-inflammatory cytokine production, but did not affect atherosclerosis development. Deletion of haematopoietic CARD9 tended to reduce macrophage and collagen content in atherosclerotic lesions, again without influencing the lesion size. Deletion of haematopoietic Dectin-2 did not influence atherosclerosis development under hyperglycaemic conditions, despite some minor effects on inflammation. Deletion of haematopoietic CARD9 induced minor alterations in plaque composition under hyperglycaemic conditions, without affecting lesion size.
Published: 2020

25. Hidden Aspects of Valency in Immune System Regulation

Author: Parimal Samir and Thirumala-Devi Kanneganti
Subjects: 0301 basic medicine, Immunology, Computational biology, Article, Immunomodulation, 03 medical and health sciences, 0302 clinical medicine, Immune system, NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Humans, Immunology and Allergy, RNA Processing, Post-Transcriptional, Biological Variation, Individual, Innate immune system, Chemistry, fungi, Models, Immunological, Valency, food and beverages, Immunity, Innate, 030104 developmental biology, Gene Expression Regulation, Immune System, Inflammation Mediators, Whole cell, Protein Processing, Post-Translational, Function (biology), 030215 immunology
Abstract: Valency can be defined as the number of discrete interactions a biomolecule can engage in. Valency can be critical for function, such as determining whether a molecule acts as a scaffold for assembling large supramolecular complexes or it forms a functional dimer. Here, we highlight the importance of the role of valency in regulating immune responses with a focus on innate immunity. We discuss some of the ways in which valency itself is regulated through transcriptional, post-transcriptional, and post-translational modifications. Finally, we propose that the valency model can be applied at the whole cell level to study differences in individual cell responses with relevance to putative therapeutic applications.
Published: 2019

26. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1

Author: Klionsky, Daniel, Abdel-Aziz, Amal Kamal, Abdelfatah, Sara, Abdellatif, Mahmoud, Abdoli, Asghar, Abel, Steffen, Abeliovich, Hagai, Abildgaard, Marie, Abudu, Yakubu Princely, Acevedo-Arozena, Abraham, Adamopoulos, Iannis, Adeli, Khosrow, Adolph, Timon, Adornetto, Annagrazia, Aflaki, Elma, Agam, Galila, Agarwal, Anupam, Aggarwal, Bharat, Agnello, Maria, Agostinis, Patrizia, Agrewala, Javed, Agrotis, Alexander, Aguilar, Patricia, Ahmad, S Tariq, Ahmed, Zubair, Ahumada-Castro, Ulises, Aits, Sonja, Aizawa, Shu, Akkoc, Yunus, Akoumianaki, Tonia, Akpinar, Hafize Aysin, Al-Abd, Ahmed, Al-Akra, Lina, Al-Gharaibeh, Abeer, Alaoui-Jamali, Moulay, Alberti, Simon, Alcocer-Gómez, Elísabet, Alessandri, Cristiano, Ali, Muhammad, Alim Al-Bari, M Abdul, Aliwaini, Saeb, Alizadeh, Javad, Almacellas, Eugènia, Almasan, Alexandru, Alonso, Alicia, Alonso, Guillermo, Altan-Bonnet, Nihal, Altieri, Dario, Álvarez, Élida, Alves, Sara, Alves Da Costa, Cristine, Alzaharna, Mazen, Amadio, Marialaura, Amantini, Consuelo, Amaral, Cristina, Ambrosio, Susanna, Amer, Amal, Ammanathan, Veena, An, Zhenyi, Andersen, Stig, Andrabi, Shaida, Andrade-Silva, Magaiver, Andres, Allen, Angelini, Sabrina, Ann, David, Anozie, Uche, Ansari, Mohammad, Antas, Pedro, Antebi, Adam, Antón, Zuriñe, Anwar, Tahira, Apetoh, Lionel, Apostolova, Nadezda, Araki, Toshiyuki, Araki, Yasuhiro, Arasaki, Kohei, Araújo, Wagner, Araya, Jun, Arden, Catherine, Arévalo, Maria-Angeles, Arguelles, Sandro, Arias, Esperanza, Arikkath, Jyothi, Arimoto, Hirokazu, Ariosa, Aileen, Armstrong-James, Darius, Arnauné-Pelloquin, Laetitia, Aroca, Angeles, Arroyo, Daniela, Arsov, Ivica, Artero, Rubén, Asaro, Dalia Maria Lucia, Aschner, Michael, Ashrafizadeh, Milad, Ashur-Fabian, Osnat, Atanasov, Atanas, Au, Alicia, Auberger, Patrick, Auner, Holger, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Ávalos, Yenniffer, Aveic, Sanja, Aveleira, Célia Alexandra, Avin-Wittenberg, Tamar, Aydin, Yucel, Ayton, Scott, Ayyadevara, Srinivas, Azzopardi, Maria, Baba, Misuzu, Backer, Jonathan, Backues, Steven, Bae, Dong-Hun, Bae, Ok-Nam, Bae, Soo Han, Baehrecke, Eric, Baek, Ahruem, Baek, Seung-Hoon, Baek, Sung Hee, Bagetta, Giacinto, Bagniewska-Zadworna, Agnieszka, Bai, Hua, Bai, Jie, Bai, Xiyuan, Bai, Yidong, Bairagi, Nandadulal, Baksi, Shounak, Balbi, Teresa, Baldari, Cosima, Balduini, Walter, Ballabio, Andrea, Ballester, Maria, Balazadeh, Salma, Balzan, Rena, Bandopadhyay, Rina, Banerjee, Sreeparna, Banerjee, Sulagna, Bánréti, Ágnes, Bao, Yan, Baptista, Mauricio, Baracca, Alessandra, Barbati, Cristiana, Bargiela, Ariadna, Barilà, Daniela, Barlow, Peter, Barmada, Sami, Barreiro, Esther, Barreto, George, Bartek, Jiri, Bartel, Bonnie, Bartolome, Alberto, Barve, Gaurav, Basagoudanavar, Suresh, Bassham, Diane, Bast, Robert, Basu, Alakananda, Batoko, Henri, Batten, Isabella, Baulieu, Etienne, Baumgarner, Bradley, Bayry, Jagadeesh, Beale, Rupert, Beau, Isabelle, Beaumatin, Florian, Bechara, Luiz, Beck, George, Beers, Michael, Begun, Jakob, Behrends, Christian, Behrens, Georg, Bei, Roberto, Bejarano, Eloy, Bel, Shai, Behl, Christian, Belaid, Amine, Belgareh-Touzé, Naïma, Bellarosa, Cristina, Belleudi, Francesca, Belló Pérez, Melissa, Bello-Morales, Raquel, Beltran, Jackeline Soares de Oliveira, Beltran, Sebastián, Benbrook, Doris Mangiaracina, Bendorius, Mykolas, Benitez, Bruno, Benito-Cuesta, Irene, Bensalem, Julien, Berchtold, Martin, Berezowska, Sabina, Bergamaschi, Daniele, Bergami, Matteo, Bergmann, Andreas, Berliocchi, Laura, Berlioz-Torrent, Clarisse, Bernard, Amélie, Berthoux, Lionel, Besirli, Cagri, Besteiro, Sebastien, Betin, Virginie, Beyaert, Rudi, Bezbradica, Jelena, Bhaskar, Kiran, Bhatia-Kissova, Ingrid, Bhattacharya, Resham, Bhattacharya, Sujoy, Bhattacharyya, Shalmoli, Bhuiyan, Md Shenuarin, Bhutia, Sujit Kumar, Bi, Lanrong, Bi, Xiaolin, Biden, Trevor, Bijian, Krikor, Billes, Viktor, Binart, Nadine, Bincoletto, Claudia, Birgisdottir, Asa, Bjorkoy, Geir, Blanco, Gonzalo, Blas-Garcia, Ana, Blasiak, Janusz, Blomgran, Robert, Blomgren, Klas, Blum, Janice, Boada-Romero, Emilio, Boban, Mirta, Boesze-Battaglia, Kathleen, Boeuf, Philippe, Boland, Barry, Bomont, Pascale, Bonaldo, Paolo, Bonam, Srinivasa Reddy, Bonfili, Laura, Bonifacino, Juan, Boone, Brian, Bootman, Martin, Bordi, Matteo, Borner, Christoph, Bornhauser, Beat, Borthakur, Gautam, Bosch, Jürgen, Bose, Santanu, botana, luis, Botas, Juan, Boulanger, Chantal, Boulton, Michael, Bourdenx, Mathieu, Bourgeois, Benjamin, Bourke, Nollaig, Bousquet, Guilhem, Boya, Patricia, Bozhkov, Peter, Bozi, Luiz, Bozkurt, Tolga, Brackney, Doug, Brandts, Christian, Braun, Ralf, Braus, Gerhard, Bravo-Sagua, Roberto, Bravo-San Pedro, José, Brest, Patrick, Bringer, Marie-Agnès, Briones-Herrera, Alfredo, Broaddus, V Courtney, Brodersen, Peter, Brodsky, Jeffrey, Brody, Steven, Bronson, Paola, Bronstein, Jeff, Brown, Carolyn, Brown, Rhoderick, Brum, Patricia, Brumell, John, Brunetti-Pierri, Nicola, Bruno, Daniele, Bryson-Richardson, Robert, Bucci, Cecilia, Buchrieser, Carmen, Bueno, Marta, Buitrago-Molina, Laura Elisa, Buraschi, Simone, Buch, Shilpa, Buchan, J Ross, Buckingham, Erin, Budak, Hikmet, Budini, Mauricio, Bultynck, Geert, Burada, Florin, Burgoyne, Joseph, Burón, M Isabel, Bustos, Victor, Büttner, Sabrina, Butturini, Elena, Byrd, Aaron, Cabas, Isabel, Cabrera-Benitez, Sandra, Cadwell, Ken, Cai, Jingjing, Cai, Lu, Cai, Qian, Cairó, Montserrat, Calbet, Jose, Caldwell, Guy, Caldwell, Kim, Call, Jarrod, Calvani, Riccardo, Calvo, Ana, Calvo-Rubio Barrera, Miguel, Camara, Niels OS, Camonis, Jacques, Camougrand, Nadine, Campanella, Michelangelo, Campbell, Edward, Campbell-Valois, François-Xavier, Campello, Silvia, Campesi, Ilaria, Campos, Juliane, Camuzard, Olivier, Cancino, Jorge, Candido de Almeida, Danilo, Canesi, Laura, Caniggia, Isabella, Canonico, Barbara, Cantí, Carles, Cao, Bin, Caraglia, Michele, Caramés, Beatriz, Carchman, Evie, Cardenal-Muñoz, Elena, Cardenas, Cesar, Cardenas, Luis, Cardoso, Sandra, Carew, Jennifer, Carle, Georges, Carleton, Gillian, Carloni, Silvia, Carmona-Gutierrez, Didac, Carneiro, Leticia, Carnevali, Oliana, Carosi, Julian, Carra, Serena, Carrier, Alice, Carrier, Lucie, Carroll, Bernadette, Carter, A Brent, Carvalho, Andreia Neves, Casanova, Magali, Casas, Caty, Casas, Josefina, Cassioli, Chiara, Castillo, Eliseo, Castillo, Karen, Castillo-Lluva, Sonia, Castoldi, Francesca, Castori, Marco, Castro, Ariel, Castro-Caldas, Margarida, Castro-Hernandez, Javier, Castro-Obregon, Susana, Catz, Sergio, Cavadas, Claudia, Cavaliere, Federica, Cavallini, Gabriella, Cavinato, Maria, Cayuela, Maria, Cebollada Rica, Paula, Cecarini, Valentina, Cecconi, Francesco, Cechowska-Pasko, Marzanna, Cenci, Simone, Ceperuelo-Mallafré, Victòria, Cerqueira, João, Cerutti, Janete, Cervia, Davide, Cetintas, Vildan Bozok, Cetrullo, Silvia, Chae, Han-Jung, Chagin, Andrei, Chai, Chee-Yin, Chakrabarti, Gopal, Chakrabarti, Oishee, Chakraborty, Tapas, Chakraborty, Trinad, Chami, mounia, Chamilos, Georgios, Chan, David, Chan, Edmond, Chan, Edward, Chan, H.Y. Edwin, Chan, Helen, Chan, Hung, Chan, Matthew, Chan, Yau Sang, Chandra, Partha, Chang, Chih-Peng, Chang, Chunmei, Chang, Hao-Chun, Chang, Kai, Chao, Jie, Chapman, Tracey, Charlet-Berguerand, Nicolas, Chatterjee, Samrat, Chaube, Shail, Chaudhary, Anu, Chauhan, Santosh, Chaum, Edward, Checler, Frédéric, Cheetham, Michael, Chen, Chang-Shi, Chen, Guang-Chao, Chen, Jian-Fu, Chen, Liam, Chen, Leilei, Chen, Lin, Chen, Mingliang, Chen, Mu-Kuan, Chen, Ning, Chen, Quan, Chen, Ruey-Hwa, Chen, Shi, Chen, Wei, Chen, Weiqiang, Chen, Xin-Ming, Chen, Xiong-Wen, Chen, Xu, Chen, Yan, Chen, Ye-Guang, Chen, Yingyu, Chen, Yongqiang, Chen, Yu-Jen, Chen, Yue-Qin, Chen, Zhefan Stephen, Chen, Zhi, Chen, Zhi-Hua, Chen, Zhijian, Chen, Zhixiang, Cheng, Hanhua, Cheng, Jun, Cheng, Shi-Yuan, Cheng, Wei, Cheng, Xiaodong, Cheng, Xiu-Tang, Cheng, Yiyun, Cheng, Zhiyong, Chen, Zhong, Cheong, Heesun, Cheong, Jit Kong, Chernyak, Boris, Cherry, Sara, Cheung, Chi Fai Randy, Cheung, Chun Hei Antonio, Cheung, King-Ho, Chevet, Eric, Chi, Richard, Chiang, Alan Kwok Shing, Chiaradonna, Ferdinando, Chiarelli, Roberto, Chiariello, Mario, Chica, Nathalia, Chiocca, Susanna, Chiong, Mario, Chiou, Shih-Hwa, Chiramel, Abhilash, Chiurchiù, Valerio, Cho, Dong-Hyung, Choe, Seong-Kyu, Choi, Augustine, Choi, Mary, Choudhury, Kamalika Roy, Chow, Norman, Chu, Charleen, Chua, Jason, Chua, John Jia En, Chung, Hyewon, Chung, Kin Pan, Chung, Seockhoon, Chung, So-Hyang, Chung, Yuen-Li, Cianfanelli, Valentina, Ciechomska, Iwona, Cifuentes, Mariana, Cinque, Laura, Cirak, Sebahattin, Cirone, Mara, Clague, Michael, Clarke, Robert, Clementi, Emilio, Coccia, Eliana, Codogno, Patrice, Cohen, Ehud, Cohen, Mickael, Colasanti, Tania, Colasuonno, Fiorella, Colbert, Robert, Colell, Anna, Čolić, Miodrag, Coll, Nuria, Collins, Mark, Colombo, María, Colón-Ramos, Daniel, Combaret, Lydie, Comincini, Sergio, Cominetti, Márcia, Consiglio, Antonella, Conte, Andrea, Conti, Fabrizio, Contu, Viorica Raluca, Cookson, Mark, Coombs, Kevin, Coppens, Isabelle, Corasaniti, Maria Tiziana, Corkery, Dale, Cordes, Nils, Cortese, Katia, Costa, Maria do Carmo, Costantino, Sarah, Costelli, Paola, Coto-Montes, Ana, Crack, Peter, Crespo, Jose, Criollo, Alfredo, Crippa, Valeria, Cristofani, Riccardo, Csizmadia, Tamas, Cuadrado, Antonio, Cui, Bing, Cui, Jun, Cui, Yixian, Cui, Yong, Culetto, Emmanuel, Cumino, Andrea, Cybulsky, Andrey, Czaja, Mark, Czuczwar, Stanislaw, D'Adamo, Stefania, D'Amelio, Marcello, D'Arcangelo, Daniela, D'Lugos, Andrew, D'Orazi, Gabriella, da Silva, James, Dafsari, Hormos Salimi, Dagda, Ruben, Dagdas, Yasin, Daglia, Maria, Dai, Xiaoxia, Dai, Yun, Dai, Yuyuan, Dal Col, Jessica, Dalhaimer, Paul, Dalla Valle, Luisa, Dallenga, Tobias, Dalmasso, Guillaume, Damme, Markus, Dando, Ilaria, Dantuma, Nico, Darling, April, Das, Hiranmoy, Dasarathy, Srinivasan, Dasari, Santosh, Dash, Srikanta, Daumke, Oliver, Dauphinee, Adrian, Davies, Jeffrey, Dávila, Valeria, Davis, Roger, Davis, Tanja, Dayalan Naidu, Sharadha, De Amicis, Francesca, De Bosscher, Karolien, De Felice, Francesca, De Franceschi, Lucia, De Leonibus, Chiara, de Mattos Barbosa, Mayara, De Meyer, Guido, De Milito, Angelo, De Nunzio, Cosimo, De Palma, Clara, De Santi, Mauro, De Virgilio, Claudio, De Zio, Daniela, Debnath, Jayanta, DeBosch, Brian, Decuypere, Jean-Paul, Deehan, Mark, Deflorian, Gianluca, DeGregori, James, Dehay, Benjamin, Del Rio, Gabriel, Delaney, Joe, Delbridge, Lea, Delorme-Axford, Elizabeth, Delpino, M Victoria, Demarchi, Francesca, Dembitz, Vilma, Demers, Nicholas, Deng, Hongbin, Deng, Zhiqiang, Dengjel, Joern, Dent, Paul, Denton, Donna, DePamphilis, Melvin, Der, Channing, Deretic, Vojo, Descoteaux, Albert, Devis, Laura, Devkota, Sushil, Devuyst, Olivier, Dewson, Grant, Dharmasivam, Mahendiran, Dhiman, Rohan, di Bernardo, Diego, Di Cristina, Manlio, Di Domenico, Fabio, Di Fazio, Pietro, Di Fonzo, Alessio, Di Guardo, Giovanni, Di Guglielmo, Gianni, Di Leo, Luca, Di Malta, Chiara, Di Nardo, Alessia, Di Rienzo, Martina, Di Sano, 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Eissa, N Tony, Eissa, Sanaa, Ejarque, Miriam, El Andaloussi, Abdeljabar, El-Hage, Nazira, El-Naggar, Shahenda, Eleuteri, Anna Maria, El-Shafey, Eman, Elgendy, Mohamed, Eliopoulos, Aristides, Elizalde, María, Elks, Philip, Elsasser, Hans-Peter, Elsherbiny, Eslam, Emerling, Brooke, Emre, N., Eng, Christina, Engedal, Nikolai, Engelbrecht, Anna-Mart, Engelsen, Agnete, Enserink, Jorrit, Escalante, Ricardo, Esclatine, Audrey, Escobar-Henriques, Mafalda, Eskelinen, Eeva-Liisa, Espert, Lucile, Eusebio, Makandjou-Ola, Fabrias, Gemma, Fabrizi, Cinzia, Facchiano, Antonio, Facchiano, Francesco, Fadeel, Bengt, Fader, Claudio, Faesen, Alex, Fairlie, W Douglas, Falcó, Alberto, Falkenburger, Bjorn, Fan, Daping, Fan, Jie, Fan, Yanbo, Fang, Evandro, Fang, Yanshan, Fang, Yognqi, Fanto, Manolis, Farfel-Becker, Tamar, Faure, Mathias, Fazeli, Gholamreza, Fedele, Anthony, Feldman, Arthur, Feng, Du, Feng, Jiachun, Feng, Lifeng, Feng, Yibin, Feng, Yuchen, Feng, Wei, Fenz Araujo, Thais, Ferguson, Thomas, Fernández, Álvaro, Fernandez-Checa, Jose, Fernández-Veledo, Sonia, Fernie, Alisdair, Ferrante, Anthony, Ferraresi, Alessandra, Ferrari, Merari, Ferreira, Julio, Ferro-Novick, Susan, Figueras, Antonio, Filadi, Riccardo, Filigheddu, Nicoletta, Filippi-Chiela, Eduardo, Filomeni, Giuseppe, Fimia, Gian Maria, Fineschi, Vittorio, Finetti, Francesca, Finkbeiner, Steven, Fisher, Edward, Fisher, Paul, Flamigni, Flavio, Fliesler, Steven, Flo, Trude, Florance, Ida, Florey, Oliver, Florio, Tullio, Fodor, Erika, Follo, Carlo, Fon, Edward, Forlino, Antonella, Fornai, Francesco, Fortini, Paola, Fracassi, Anna, Fraldi, Alessandro, Franco, Brunella, Franco, Rodrigo, Franconi, Flavia, Frankel, Lisa, Friedman, Scott, Fröhlich, Leopold, Frühbeck, Gema, Fuentes, Jose, Fujiki, Yukio, Fujita, Naonobu, Fujiwara, Yuuki, Fukuda, Mitsunori, Fulda, Simone, Furic, Luc, Furuya, Norihiko, Fusco, Carmela, Gack, Michaela, Gaffke, Lidia, Galadari, Sehamuddin, Galasso, Alessia, Galindo, Maria, Gallolu Kankanamalage, Sachith, Galluzzi, Lorenzo, Galy, Vincent, Gammoh, Noor, Gan, Boyi, Ganley, Ian, Gao, Feng, Gao, Hui, Gao, Minghui, Gao, Ping, Gao, Shou-Jiang, Gao, Wentao, Gao, Xiaobo, Garcera, Ana, Garcia, Maria Noé, Garcia, Verónica, García-del Portillo, Francisco, Garcia-Escudero, Vega, Garcia-Garcia, Aracely, Garcia-Macia, Marina, García-Moreno, Diana, Garcia-Ruiz, Carmen, García-Sanz, Patricia, Garg, Abhishek, Gargini, Ricardo, Garofalo, Tina, Garry, Robert, Gassen, Nils, Gatica, Damian, Ge, Liang, Ge, Wanzhong, Geiss-Friedlander, Ruth, Gelfi, Cecilia, Genschik, Pascal, Gentle, Ian, Gerbino, Valeria, Gerhardt, Christoph, Germain, Kyla, Germain, Marc, Gewirtz, David, Ghasemipour Afshar, Elham, Ghavami, Saeid, Ghigo, Alessandra, Ghosh, Manosij, Giamas, Georgios, Giampietri, Claudia, Giatromanolaki, Alexandra, Gibson, Gary, Gibson, Spencer, Ginet, Vanessa, Giniger, Edward, Giorgi, Carlotta, Girao, Henrique, Girardin, Stephen, Giridharan, Mridhula, Giuliano, Sandy, Giulivi, Cecilia, Giuriato, Sylvie, Giustiniani, Julien, Gluschko, Alexander, Goder, Veit, Goginashvili, Alexander, Golab, Jakub, Goldstone, David, Golebiewska, Anna, Gomes, Luciana, Gomez, Rodrigo, Gómez-Sánchez, Rubén, Gomez-Puerto, Maria Catalina, Gomez-Sintes, Raquel, Gong, Qingqiu, Goni, Felix, González-Gallego, Javier, Gonzalez-Hernandez, Tomas, Gonzalez-Polo, Rosa, Gonzalez-Reyes, Jose, González-Rodríguez, Patricia, Goping, Ing Swie, Gorbatyuk, Marina, Gorbunov, Nikolai, Görgülü, Kıvanç, Gorojod, Roxana, Gorski, Sharon, Goruppi, Sandro, Gotor, Cecilia, Gottlieb, Roberta, Gozes, Illana, Gozuacik, Devrim, Graef, Martin, Gräler, Markus, Granatiero, Veronica, Grasso, Daniel, Gray, Joshua, Green, Douglas, Greenhough, Alexander, Gregory, Stephen, Griffin, Edward, Grinstaff, Mark, Gros, Frederic, Grose, Charles, Gross, Angelina, Gruber, Florian, Grumati, Paolo, Grune, Tilman, Gu, Xueyan, Guan, Jun-Lin, Guardia, Carlos, Guda, Kishore, Guerra, Flora, Guerri, Consuelo, Guha, Prasun, Guillén, Carlos, Gujar, Shashi, 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Elena, Uchiyama, Yasuo, Ugun-Klusek, Aslihan, Uhlig, Holm, Ułamek-Kozioł, Marzena, Ulasov, Ilya, Umekawa, Midori, Ungermann, Christian, Unno, Rei, Urbe, Sylvie, Uribe-Carretero, Elisabet, Üstün, Suayib, Uversky, Vladimir, Vaccari, Thomas, Vaccaro, Maria, Vahsen, Björn, Vakifahmetoglu-Norberg, Helin, Valdor, Rut, Valente, Maria, Valko, Ayelén, Vallee, Richard, Valverde, Angela, Van Den Berghe, Greet, van der Veen, Stijn, Van Kaer, Luc, van Loosdregt, Jorg, van Wijk, Sjoerd, Vandenberghe, Wim, Vanhorebeek, Ilse, Vannier-Santos, Marcos, Vannini, Nicola, Vanrell, M Cristina, Vantaggiato, Chiara, Varano, Gabriele, Varela-Nieto, Isabel, Varga, Máté, Vasconcelos, M Helena, Vats, Somya, Vavvas, Demetrios, Vega-Naredo, Ignacio, Vega-Rubin-de-Celis, Silvia, Velasco, Guillermo, Velázquez, Ariadna, Vellai, Tibor, Vellenga, Edo, Velotti, Francesca, Verdier, Mireille, Verginis, Panayotis, Vergne, Isabelle, Verkade, Paul, Verma, Manish, Verstreken, Patrik, Vervliet, Tim, Vervoorts, Jörg, Vessoni, Alexandre, Victor, Victor, Vidal, Michel, Vidoni, Chiara, Vieira, Otilia, Vierstra, Richard, Viganó, Sonia, Vihinen, Helena, Vijayan, Vinoy, Vila, Miquel, Vilar, Marçal, Villalba, José, Villalobo, Antonio, Villarejo-Zori, Beatriz, Villarroya, Francesc, Villarroya, Joan, Vincent, Olivier, Vindis, Cecile, Viret, Christophe, Viscomi, Maria Teresa, Visnjic, Dora, Vitale, Ilio, Vocadlo, David, Voitsekhovskaja, Olga, Volonté, Cinzia, Volta, Mattia, Vomero, Marta, Von Haefen, Clarissa, Vooijs, Marc, Voos, Wolfgang, Vucicevic, Ljubica, Wade-Martins, Richard, Waguri, Satoshi, Waite, Kenrick, Wakatsuki, Shuji, Walker, David, Walker, Mark, Walker, Simon, Walter, Jochen, Wandosell, Francisco, Wang, Bo, Wang, Chao-Yung, Wang, Chen, Wang, Chenran, Wang, Chenwei, Wang, Cun-Yu, Wang, Dong, Wang, Fangyang, Wang, Feng, Wang, Fengming, Wang, Guansong, Wang, Han, Wang, Hao, Wang, Hexiang, Wang, Hong-Gang, Wang, Jianrong, Wang, Jigang, Wang, Jiou, Wang, Jundong, Wang, Kui, Wang, Lianrong, Wang, Liming, Wang, Maggie Haitian, Wang, Meiqing, Wang, Nanbu, Wang, PengWei, Wang, PeiPei, Wang, Ping, Wang, Qing Jun, Wang, Qing, Wang, Qing Kenneth, Wang, Qiong, Wang, Wen-Tao, Wang, Wuyang, Wang, Xinnan, Wang, Xuejun, Wang, Yan, Wang, Yanchang, Wang, Yanzhuang, Wang, Yen-Yun, Wang, Yihua, Wang, Yipeng, Wang, Yu, wang, yuqi, Wang, Zhe, Wang, Zhenyu, Wang, Zhouguang, Warnes, Gary, Warnsmann, Verena, Watada, Hirotaka, Watanabe, Eizo, Watchon, Maxinne, Wawrzyńska, Anna, Weaver, Timothy, Wegrzyn, Grzegorz, Wehman, Ann, Wei, Huafeng, Wei, Lei, Wei, Taotao, Wei, Yongjie, Weiergräber, Oliver, Weihl, Conrad, Weindl, Günther, Weiskirchen, Ralf, Wells, Alan, Wen, Runxia, Wen, Xin, Werner, Antonia, Weykopf, Beatrice, Wheatley, Sally, Whitton, J Lindsay, Whitworth, Alexander, Wiktorska, Katarzyna, Wildenberg, Manon, Wileman, Tom, Wilkinson, Simon, Willbold, Dieter, Williams, Brett, Williams, Robin, Williams, Roger, Williamson, Peter, Wilson, Richard, Winner, Beate, Winsor, Nathaniel, Witkin, Steven, Wodrich, Harald, Woehlbier, Ute, Wollert, Thomas, Wong, Esther, Wong, Jack Ho, Wong, Richard, Wong, Vincent Kam Wai, Wong, W Wei-Lynn, Wu, An-Guo, Wu, Chengbiao, Wu, Jian, Wu, Junfang, Wu, Kenneth, Wu, Min, Wu, Shan-Ying, Wu, Shengzhou, Wu, Shu-Yan, Wu, Shufang, Wu, William, Wu, Xiaohong, Wu, Xiaoqing, Wu, Yao-Wen, Wu, Yihua, Xavier, Ramnik, Xia, Hongguang, Xia, Lixin, Xia, Zhengyuan, Xiang, Ge, Xiang, Jin, Xiang, Mingliang, Xiang, Wei, Xiao, Bin, Xiao, Guozhi, Xiao, Hengyi, Xiao, Hong-tao, Xiao, Jian, Xiao, Lan, Xiao, Shi, Xiao, Yin, Xie, Baoming, Xie, Chuan-Ming, Xie, Min, Xie, Yuxiang, Xie, Zhiping, Xie, Zhonglin, Xilouri, Maria, Xu, Congfeng, Xu, En, Xu, Haoxing, Xu, Jing, Xu, Jinrong, Xu, Liang, Xu, Wen Wen, Xu, Xiulong, Xue, Yu, Yakhine-Diop, Sokhna, Yamaguchi, Masamitsu, Yamaguchi, Osamu, Yamamoto, Ai, Yamashina, Shunhei, Yan, Shengmin, Yan, Shian-Jang, Yan, Zhen, Yanagi, Yasuo, Yang, Chuanbin, Yang, Dun-Sheng, Yang, Huan, Yang, Huang-Tian, Yang, Hui, Yang, Jin-Ming, Yang, Jing, Yang, Jingyu, Yang, Ling, Yang, Liu, Yang, Ming, Yang, Pei-Ming, Yang, Qian, Yang, Seungwon, Yang, Shu, Yang, Shun-Fa, Yang, Wannian, Yang, Wei Yuan, Yang, Xiaoyong, Yang, Xuesong, Yang, Yi, Yang, Ying, Yao, Honghong, Yao, Shenggen, Yao, Xiaoqiang, Yao, Yong-Gang, Yao, Yong-Ming, Yasui, Takahiro, Yazdankhah, Meysam, Yen, Paul, Yi, Cong, Yin, Xiao-Ming, Yin, Yanhai, Yin, Zhangyuan, Yin, Ziyi, Ying, Meidan, Ying, Zheng, Yip, Calvin, Yiu, Stephanie Pei Tung, Yoo, Young, Yoshida, Kiyotsugu, Yoshii, Saori, Yoshimori, Tamotsu, Yousefi, Bahman, Yu, Boxuan, Yu, Haiyang, Yu, Jun, Yu, Li, Yu, Ming-Lung, Yu, Seong-Woon, Yu, Victor, Yu, W Haung, Yu, Zhengping, Yu, Zhou, Yuan, Junying, Yuan, Ling-Qing, Yuan, Shilin, Yuan, Shyng-Shiou, Yuan, Yanggang, Yuan, Zengqiang, Yue, Jianbo, Yue, Zhenyu, Yun, Jeanho, Yung, Raymond, Zacks, David, Zaffagnini, Gabriele, Zambelli, Vanessa, Zanella, Isabella, Zang, Qun, Zanivan, Sara, Zappavigna, Silvia, Zaragoza, Pilar, Zarbalis, Konstantinos, Zarebkohan, Amir, Zarrouk, Amira, Zeitlin, Scott, Zeng, Jialiu, Zeng, Ju-deng, Žerovnik, Eva, Zhan, Lixuan, Zhang, Bin, Zhang, Donna, Zhang, Hanlin, Zhang, Hong, Zhang, Honghe, Zhang, Huafeng, Zhang, Huaye, Zhang, Hui, Zhang, Hui-Ling, Zhang, Jianbin, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Kalin, Zhang, Leshuai, Zhang, Lin, Zhang, Lisheng, Zhang, Lu, Zhang, Luoying, Zhang, Menghuan, Zhang, Peng, Zhang, Sheng, Zhang, Wei, Zhang, Xiangnan, Zhang, Xiao-Wei, Zhang, Xiaolei, Zhang, Xiaoyan, Zhang, Xin, Zhang, Xinxin, Zhang, Xu Dong, Zhang, Yang, Zhang, Yanjin, Zhang, Yi, Zhang, Ying-Dong, Zhang, Yingmei, Zhang, Yuan-Yuan, Zhang, Yuchen, Zhang, Zhe, Zhang, Zhengguang, Zhang, Zhibing, Zhang, Zhihai, Zhang, Zhiyong, Zhang, Zili, Zhao, Haobin, Zhao, Lei, Zhao, Shuang, Zhao, Tongbiao, Zhao, Xiao-Fan, Zhao, Ying, Zhao, Yongchao, Zhao, Yongliang, Zhao, Yuting, Zheng, Guoping, Zheng, Kai, Zheng, Ling, Zheng, Shizhong, Zheng, Xi-Long, Zheng, Yi, Zheng, Zu-Guo, Zhivotovsky, Boris, Zhong, Qing, Zhou, Ao, Zhou, Ben, Zhou, Cefan, ZHOU, Gang, Zhou, Hao, Zhou, Hong, Zhou, Hongbo, Zhou, Jie, Zhou, Jing, Zhou, Jiyong, Zhou, Kailiang, Zhou, Rongjia, Zhou, Xu-jie, Zhou, Yanshuang, Zhou, Yinghong, Zhou, Yubin, Zhou, Zheng-Yu, Zhou, Zhou, Zhu, Binglin, Zhu, Changlian, Zhu, Guo-Qing, Zhu, Haining, Zhu, Hongxin, Zhu, Hua, Zhu, Wei-Guo, Zhu, Yanping, Zhu, Yushan, Zhuang, Haixia, Zhuang, Xiaohong, Zientara-Rytter, Katarzyna, Zimmermann, Christine, Ziviani, Elena, Zoladek, Teresa, Zong, Wei-Xing, Zorov, Dmitry, Zorzano, Antonio, Zou, Weiping, Zou, Zhen, Zou, Zhengzhi, Zuryn, Steven, Zwerschke, Werner, Brand-Saberi, Beate, Dong, X Charlie, Kenchappa, Chandra Shekar, Li, Zuguo, Lin, Yong, Oshima, Shigeru, Rong, Yueguang, Sluimer, Judith, Stallings, Christina, Tong, Chun-Kit, Ahmad, S. Tariq, Alim Al-Bari, M. Abdul, Bechara, Luiz R.G., Behrens, Georg M.N., Bhuiyan, Md. Shenuarin, Broaddus, V. Courtney, Buchan, J. Ross, Burón, M. Isabel, Carter, A. Brent, Chan, Matthew T.V., Choi, Augustine M.K., D’Adamo, Stefania, D’Amelio, Marcello, D’Arcangelo, Daniela, D’Lugos, Andrew, D’Orazi, Gabriella, De Meyer, Guido R.Y., Delpino, M. Victoria, Distler, Jörg H.W., Dixon, Ian M.C., Dobson, Renwick C.J., 2nd Dorn, Gerald, Eissa, N. Tony, Engelsen, Agnete S.T., Fairlie, W. Douglas, Ferreira, Julio C.B., H.B., Ranjitha, Hanson, Phyllis I., Hejtmancik, J. Fielding, Ho, Idy H.T., Hobbs, G. Aaron, Hoet, Peter H.M., Huang, Michael L.H., Iyer, Anand Krishnan V., Johnson, Gail V.W., Joosten, Leo A.B., Karim, Md. Razaul, Kaufmann, Stefan H.E., Ko, Ben C.B., Leck, Lionel Y.W., Lima, Thania R.R., Livingston, J. Andrew, Martin, Alexandre P.J., Montes, L. Ruth, Murphy, J. Patrick, Ng, Charlene C.W., Nicolao, M. Celeste, O’Donovan, Tracey, O’Leary, Seónadh, O’Rourke, Eyleen, O’Sullivan, Mary, O’Sullivan, Timothy, Omary, M. Bishr, Pereira, Gustavo J.S., Ratnayaka, J. Arjuna, Riazuddin, S. Amer, Rouschop, Kasper M.A., Sanderson, J. Thomas, Scaglione, K. Matthew, Schapira, Anthony H.V., Scovassi, A. Ivana, St. Clair, Daret, Sunahara, Karen K.S., Symons, J. David, Triola, Gemma, van Wijk, Sjoerd J.L., Vanrell, M. Cristina, Vasconcelos, M. Helena, Whitton, J. Lindsay, Williams, Robin S.B., Wong, W. Wei-Lynn, Wu, William K.K., Yakhine-Diop, Sokhna M.S., Yu, W. Haung, Zhang, Kalin Y.B., Dong, X. Charlie, Ain Shams University [ASU], Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University [JGU], Medical University Graz, Centre de Recherche des Cordeliers [CRC (UMR_S_1138 / U1138)], Institut Pasteur d'Iran, Leibniz Institute of Plant Biochemistry [IPB], The University of Texas M.D. Anderson Cancer Center [Houston], Institut de pharmacologie moléculaire et cellulaire [IPMC], Lipides - Nutrition - Cancer [Dijon - U1231] [LNC], Centre méditerranéen de médecine moléculaire [C3M], Institut de Biologie Valrose [IBV], Petites Molécules de neuroprotection, neurorégénération et remyélinisation, Signalisation Hormonale, Physiopathologie Endocrinienne et Métabolique, Institut Cochin [IC UM3 (UMR 8104 / U1016)], Institut NeuroMyoGène [INMG], Paris-Centre de Recherche Cardiovasculaire [PARCC (UMR_S 970/ U970)], Marqueurs cardiovasculaires en situation de stress [MASCOT (UMR_S_942 / U942)], Institut de Recherche sur le Cancer et le Vieillissement [IRCAN], Centre de Recherche en Cancérologie de Marseille [CRCM], Centre for Integrative Biology - CBI [Inserm U964 - CNRS UMR7104 - IGBMC], Oncogenesis, Stress, Signaling [OSS], Institut Necker Enfants-Malades [INEM - UM 111 (UMR 8253 / U1151)], Institut de Biologie Intégrative de la Cellule [I2BC], Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte [M2iSH], Centre de Recherches en Cancérologie de Toulouse [CRCT], Physiopathologie et traitement des maladies du foie, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL], Institut de Génétique et de Biologie Moléculaire et Cellulaire [IGBMC], Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] [BIO-PEROXIL], Centre de recherche sur l'Inflammation [CRI (UMR_S_1149 / ERL_8252 / U1149)], Unité de génétique et biologie des cancers [U830], Laboratoire d'Optique et Biosciences [LOB], Institut des Maladies Métaboliques et Casdiovasculaires [UPS/Inserm U1297 - I2MC], Différenciation et communication neuronale et neuroendocrine [DC2N], Institut de Recherche en Cancérologie de Montpellier [IRCM - U1194 Inserm - UM], Centre d'Immunologie de Marseille - Luminy [CIML], Physiopathologie et imagerie des troubles neurologiques [PhIND], Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée [LBFA], Imagine - Institut des maladies génétiques (IHU) [Imagine - U1163], Institut Mondor de Recherche Biomédicale [IMRB], Franco-czech Laboratory for clinical research on obesity, University of Michigan [Ann Arbor], University of Michigan System, Institut de pharmacologie moléculaire et cellulaire (IPMC), Centre National de la Recherche Scientifique (CNRS)-Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Université Côte d'Azur (UCA), Lipides - Nutrition - Cancer [Dijon - U1231] (LNC), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Centre méditerranéen de médecine moléculaire (C3M), Université Nice Sophia Antipolis (... - 2019) (UNS), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), Institut de Biologie Valrose (IBV), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA)-Centre National de la Recherche Scientifique (CNRS), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Sud - Paris 11 (UP11), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM)-AP-HP Hôpital Bicêtre (Le Kremlin-Bicêtre), Nutrition, Métabolisme, Aquaculture (NuMéA), Université de Pau et des Pays de l'Adour (UPPA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Institut Cochin (IC UM3 (UMR 8104 / U1016)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Institut NeuroMyoGène (INMG), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM), Paris-Centre de Recherche Cardiovasculaire (PARCC - UMR-S U970), Hôpital Européen Georges Pompidou [APHP] (HEGP), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Institut de Recherche sur le Cancer et le Vieillissement (IRCAN), COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015 - 2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Centre des Sciences du Goût et de l'Alimentation [Dijon] (CSGA), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de Recherche en Cancérologie de Marseille (CRCM), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Aix Marseille Université (AMU), Centre for Integrative Biology - CBI (Inserm U964 - CNRS UMR7104 - IGBMC), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institute of genetics and molecular and cellular biology-Centre National de la Recherche Scientifique (CNRS), Chemistry, Oncogenesis, Stress and Signaling (COSS), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-CRLCC Eugène Marquis (CRLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Necker Enfants-Malades (INEM - UM 111 (UMR 8253 / U1151)), Unité de Nutrition Humaine (UNH), Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut de Biologie Intégrative de la Cellule (I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Microbes, Intestin, Inflammation et Susceptibilité de l'Hôte (M2iSH), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre de Recherche en Nutrition Humaine d'Auvergne (CRNH d'Auvergne)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE)-Université Clermont Auvergne (UCA), Institut des Maladies Neurodégénératives [Bordeaux] (IMN), Université de Bordeaux (UB)-Centre National de la Recherche Scientifique (CNRS), Centre International de Recherche en Infectiologie - UMR (CIRI), École normale supérieure - Lyon (ENS Lyon)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre de Recherches en Cancérologie de Toulouse (CRCT), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Physiologie et Génomique des Poissons (LPGP), Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique )-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Hôpital Paul Brousse-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay, Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 (CIIL), Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Centre National de la Recherche Scientifique (CNRS), Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] (BIO-PEROXIL), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Centre de recherche sur l'Inflammation (CRI (UMR_S_1149 / ERL_8252 / U1149)), Institut Jean-Pierre Bourgin (IJPB), AgroParisTech-Université Paris-Saclay-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Unité de génétique et biologie des cancers (U830), Institut Curie [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Laboratoire d'Optique et Biosciences (LOB), École polytechnique (X)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Institut des Maladies Métaboliques et Cardiovasculaires (I2MC), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM), Différenciation et communication neuronale et neuroendocrine (DC2N), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Recherche en Cancérologie de Montpellier (IRCM - U1194 Inserm - UM), CRLCC Val d'Aurelle - Paul Lamarque-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), Centre d'Immunologie de Marseille - Luminy (CIML), Aix Marseille Université (AMU)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie et imagerie des troubles neurologiques (PhIND), Université de Caen Normandie (UNICAEN), Laboratory of Fundamental and Applied Bioenergetics = Laboratoire de bioénergétique fondamentale et appliquée (LBFA), Université Grenoble Alpes (UGA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Epithelial biology and disease - Liliane Bettencourt Chair of Developmental Biology (Equipe Inserm U1163), Imagine - Institut des maladies génétiques (IHU) (Imagine - U1163), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Paris (UP), Biomécanique cellulaire et respiratoire (BCR), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12)-Centre National de la Recherche Scientifique (CNRS), Charles University [Prague]-Institut National de la Santé et de la Recherche Médicale (INSERM), This work was supported by the National Institute of General Medical Sciences [GM131919]., Université Paris-Sud - Paris 11 (UP11)-Institut National de la Santé et de la Recherche Médicale (INSERM), Marqueurs cardiovasculaires en situation de stress (MASCOT (UMR_S_942 / U942)), Institut National de la Santé et de la Recherche Médicale (INSERM)-Groupe Hospitalier Saint Louis - Lariboisière - Fernand Widal [Paris], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP)-Université Sorbonne Paris Nord, Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Physiopathologie des Adaptations Nutritionnelles (PhAN), Université de Nantes (UN)-Institut National de la Recherche Agronomique (INRA), Département Plateforme (PF I2BC), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Institut Gustave Roussy (IGR), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO), Chinese Academy of Medical Sciences [Suzhou, Chine] (CAMS), Karolinska Institutet [Stockholm], Karolinska University Hospital [Stockholm], Department of Women's and Children's Health [Stockholm, Sweden], Centre National de la Recherche Scientifique (CNRS)-Centre Hospitalier Régional Universitaire [Lille] (CHRU Lille)-Université de Lille-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut National de la Santé et de la Recherche Médicale (INSERM)-École polytechnique (X), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées, FHU OncoAge - Pathologies liées à l’âge [CHU Nice] (OncoAge), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA)-Institut de Pharmacologie Moléculaire et Cellulaire [UNIV Côte d'Azur] (UPMC), Institut Universitaire du Cancer de Toulouse - Oncopole (IUCT Oncopole - UMR 1037), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-CHU Toulouse [Toulouse]-Institut National de la Santé et de la Recherche Médicale (INSERM), Life Sciences Institute [Ann Arbor, MI, USA], University of Michigan System-University of Michigan System, European Institute of Oncology IRCCS [Milan, Italy] (EIO), Ain Shams University (ASU), Johannes Gutenberg - Universität Mainz = Johannes Gutenberg University (JGU), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université Paris Cité (UPCité), Réseau International des Instituts Pasteur (RIIP), Leibniz Institute of Plant Biochemistry (IPB), Hebrew University of Jerusalem, Université Nice Sophia Antipolis (1965 - 2019) (UNS), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Agro Dijon, Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro)-Institut national d'enseignement supérieur pour l'agriculture, l'alimentation et l'environnement (Institut Agro), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Côte d'Azur (UCA), COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-COMUE Université Côte d'Azur (2015-2019) (COMUE UCA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Côte d'Azur (UCA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité), Paris-Centre de Recherche Cardiovasculaire (PARCC (UMR_S 970/ U970)), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpitaux Universitaires Paris Ouest - Hôpitaux Universitaires Île de France Ouest (HUPO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Cité (UPCité)-Université Sorbonne Paris Nord, Aix Marseille Université (AMU)-Institut Paoli-Calmettes, Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Fédération nationale des Centres de lutte contre le Cancer (FNCLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Oncogenesis, Stress, Signaling (OSS), Institut des Maladies Métaboliques et Casdiovasculaires (UPS/Inserm U1297 - I2MC), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Grenoble Alpes (UGA), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Cité (UPCité), Institut Mondor de Recherche Biomédicale (IMRB), Institut National de la Santé et de la Recherche Médicale (INSERM)-IFR10-Université Paris-Est Créteil Val-de-Marne - Paris 12 (UPEC UP12), Charles University [Prague] (CU)-Institut National de la Santé et de la Recherche Médicale (INSERM), Klionsky, D. 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G., Puertollano, R., Puglielli, L., Pulinilkunnil, T., Puri, D., Puri, R., Puyal, J., Qi, X., Qi, Y., Qian, W., Qiang, L., Qiu, Y., Quadrilatero, J., Quarleri, J., Raben, N., Rabinowich, H., Ragona, D., Ragusa, M. J., Rahimi, N., Rahmati, M., Raia, V., Raimundo, N., Rajasekaran, N. -S., Ramachandra Rao, S., Rami, A., Ramirez-Pardo, I., Ramsden, D. B., Randow, F., Rangarajan, P. N., Ranieri, D., Rao, H., Rao, L., Rao, R., Rathore, S., Ratnayaka, J. A., Ratovitski, E. A., Ravanan, P., Ravegnini, G., Ray, S. K., Razani, B., Rebecca, V., Reggiori, F., Regnier-Vigouroux, A., Reichert, A. S., Reigada, D., Reiling, J. H., Rein, T., Reipert, S., Rekha, R. S., Ren, H., Ren, J., Ren, W., Renault, T., Renga, G., Reue, K., Rewitz, K., Ribeiro de Andrade Ramos, B., Riazuddin, S. A., Ribeiro-Rodrigues, T. M., Ricci, J. -E., Ricci, R., Riccio, V., Richardson, D. R., Rikihisa, Y., Risbud, M. V., Risueno, R. M., Ritis, K., Rizza, S., Rizzuto, R., Roberts, H. C., Roberts, L. D., Robinson, K. 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M., Villalobo, A., Villarejo-Zori, B., Villarroya, F., Villarroya, J., Vincent, O., Vindis, C., Viret, C., Viscomi, M. T., Visnjic, D., Vitale, I., Vocadlo, D. J., Voitsekhovskaja, O. V., Volonte, C., Volta, M., Vomero, M., Von Haefen, C., Vooijs, M. A., Voos, W., Vucicevic, L., Wade-Martins, R., Waguri, S., Waite, K. A., Wakatsuki, S., Walker, D. W., Walker, M. J., Walker, S. A., Walter, J., Wandosell, F. G., Wang, B., Wang, C. -Y., Wang, C., Wang, D., Wang, F., Wang, G., Wang, H., Wang, H. -G., Wang, J., Wang, K., Wang, L., Wang, M. H., Wang, M., Wang, N., Wang, P., Wang, Q. J., Wang, Q., Wang, Q. K., Wang, Q. A., Wang, W. -T., Wang, W., Wang, X., Wang, Y., Wang, Y. -Y., Wang, Z., Warnes, G., Warnsmann, V., Watada, H., Watanabe, E., Watchon, M., Wawrzynska, A., Weaver, T. E., Wegrzyn, G., Wehman, A. M., Wei, H., Wei, L., Wei, T., Wei, Y., Weiergraber, O. H., Weihl, C. C., Weindl, G., Weiskirchen, R., Wells, A., Wen, R. H., Wen, X., Werner, A., Weykopf, B., Wheatley, S. 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S., Yamaguchi, M., Yamaguchi, O., Yamamoto, A., Yamashina, S., Yan, S., Yan, S. -J., Yan, Z., Yanagi, Y., Yang, C., Yang, D. -S., Yang, H., Yang, H. -T., Yang, J. -M., Yang, J., Yang, L., Yang, M., Yang, P. -M., Yang, Q., Yang, S., Yang, S. -F., Yang, W., Yang, W. Y., Yang, X., Yang, Y., Yao, H., Yao, S., Yao, X., Yao, Y. -G., Yao, Y. -M., Yasui, T., Yazdankhah, M., Yen, P. M., Yi, C., Yin, X. -M., Yin, Y., Yin, Z., Ying, M., Ying, Z., Yip, C. K., Yiu, S. P. T., Yoo, Y. H., Yoshida, K., Yoshii, S. R., Yoshimori, T., Yousefi, B., Yu, B., Yu, H., Yu, J., Yu, L., Yu, M. -L., Yu, S. -W., Yu, V. C., Yu, W. H., Yu, Z., Yuan, J., Yuan, L. -Q., Yuan, S., Yuan, S. -S. F., Yuan, Y., Yuan, Z., Yue, J., Yue, Z., Yun, J., Yung, R. L., Zacks, D. N., Zaffagnini, G., Zambelli, V. O., Zanella, I., Zang, Q. S., Zanivan, S., Zappavigna, S., Zaragoza, P., Zarbalis, K. S., Zarebkohan, A., Zarrouk, A., Zeitlin, S. O., Zeng, J., Zeng, J. -D., Zerovnik, E., Zhan, L., Zhang, B., Zhang, D. D., Zhang, H., Zhang, H. -L., Zhang, J., Zhang, J. -P., Zhang, K. Y. B., Zhang, L. W., Zhang, L., Zhang, M., Zhang, P., Zhang, S., Zhang, W., Zhang, X., Zhang, X. -W., Zhang, X. D., Zhang, Y., Zhang, Y. -D., Zhang, Y. -Y., Zhang, Z., Zhao, H., Zhao, L., Zhao, S., Zhao, T., Zhao, X. -F., Zhao, Y., Zheng, G., Zheng, K., Zheng, L., Zheng, S., Zheng, X. -L., Zheng, Y., Zheng, Z. -G., Zhivotovsky, B., Zhong, Q., Zhou, A., Zhou, B., Zhou, C., Zhou, G., Zhou, H., Zhou, J., Zhou, K., Zhou, R., Zhou, X. -J., Zhou, Y., Zhou, Z. -Y., Zhou, Z., Zhu, B., Zhu, C., Zhu, G. -Q., Zhu, H., Zhu, W. -G., Zhu, Y., Zhuang, H., Zhuang, X., Zientara-Rytter, K., Zimmermann, C. M., Ziviani, E., Zoladek, T., Zong, W. -X., Zorov, D. B., Zorzano, A., Zou, W., Zou, Z., Zuryn, S., Zwerschke, W., Brand-Saberi, B., Dong, X. C., Kenchappa, C. S., Lin, Y., Oshima, S., Rong, Y., Sluimer, J. C., Stallings, C. L., Tong, C. -K., and Centre National de la Recherche Scientifique (CNRS)
Subjects: 0301 basic medicine, Programmed cell death, Settore BIO/06, Autophagosome, Autolysosome, [SDV]Life Sciences [q-bio], lnfectious Diseases and Global Health Radboud Institute for Molecular Life Sciences [Radboudumc 4], Autophagy-Related Proteins, Review, Computational biology, [SDV.BC]Life Sciences [q-bio]/Cellular Biology, Biology, Settore MED/04, 03 medical and health sciences, stress, Chaperone-mediated autophagy, ddc:570, Autophagy, LC3, Animals, Humans, cancer, Settore BIO/10, flux, lysosome, macroautophagy, neurodegeneration, phagophore, vacuole, Set (psychology), Molecular Biology, 030102 biochemistry & molecular biology, business.industry, Interpretation (philosophy), Autophagosomes, Cell Biology, Multicellular organism, 030104 developmental biology, Knowledge base, Biological Assay, Lysosomes, business, Biomarkers, [SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
Abstract: Contains fulltext : 232759.pdf (Publisher’s version ) (Closed access) In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021

27. Galactosaminogalactan activates the inflammasome to provide host protection

Author: Emilia Mellado, Jean-Paul Latgé, Parimal Samir, Shelbi Christgen, Thierry Fontaine, Cam Robinson, R. K. Subbarao Malireddi, Rajendra Karki, Laetitia Muszkieta, David E. Place, Perrine Bomme, Rémi Beau, Ravi C. Kalathur, Thirumala-Devi Kanneganti, Oumaïma Ibrahim-Granet, Benoit Briard, Bernard Henrissat, Peter Vogel, St. Jude Children’s Research Hospital [Memphis], Aspergillus, Institut Pasteur [Paris], Plateforme BioImagerie Ultrastructurale – Ultrastructural BioImaging Platform (UTechS UBI), Instituto de Salud Carlos III [Madrid] (ISC), Cytokines et Inflammation, Architecture et fonction des macromolécules biologiques (AFMB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), King Abdulaziz University, We thank members of the Kanneganti laboratory for their comments, suggestions and technical assistance, R. Tweedell for scientific editing of the manuscript, the St Jude Children’s Research Hospital Veterinary Pathology Core, SJCRH Center for Proteomics and Metabolomics and SJCRH Cell and Tissue Imaging Center (supported by the NCI P30 CA021765), D. Sheppard for sharing the A. fumigatus deletion mutant ∆agd, and V. M. Dixit and N. Kayagaki for the Casp1−/−Casp11−/− mutant mouse strain. T.-D.K. is supported by NIH grants AI101935, AI124346, AR056296 and CA253095 and by the American Lebanese Syrian Associated Charities. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. J.-P.L. is supported by the Aviesan project Aspergillus, the French Government’s Investissement d’Avenir program, Laboratoire d’Excellence ‘Integrative Biology of Emerging Infectious Diseases’ (grant number ANR-10-LABX-62-IBEID) and la Fondation pour la Recherche Médicale (DEQ20150331722 LATGE Equipe FRM 2015)., ANR-10-LABX-0062,IBEID,Integrative Biology of Emerging Infectious Diseases(2010), St Jude Children's Research Hospital, and Institut Pasteur [Paris] (IP)
Subjects: Male, Inflammasomes, [SDV]Life Sciences [q-bio], Galactosaminogalactan, caspase-1, Ribosome, Inflammasome, Aspergillus fumigatus, chemistry.chemical_compound, Mice, Protein biosynthesis, innate immunity, GAG, 0303 health sciences, Multidisciplinary, biology, Chemistry, Dextran Sulfate, Translation (biology), Colitis, galactosaminogalactan, 3. Good health, Cell biology, host defense, Female, medicine.drug, Ribosomal Proteins, Article, Fungal Proteins, 03 medical and health sciences, NLRP3, Ribosomal protein, Polysaccharides, NLR Family, Pyrin Domain-Containing 3 Protein, medicine, Animals, Aspergillosis, 030304 developmental biology, Innate immune system, 030306 microbiology, Pathogen-Associated Molecular Pattern Molecules, biology.organism_classification, Immunity, Innate, Biofilms, Protein Biosynthesis, fungi, Ribosomes, Gene Deletion
Abstract: International audience; Galactosaminogalactan of Aspergillus fumigatus acts as a pathogen-associated molecular pattern that activates the NLRP3 inflammasome, which is crucial for anti-fungal host defence.Inflammasomes are important sentinels of innate immune defence that are activated in response to diverse stimuli, including pathogen-associated molecular patterns (PAMPs)(1). Activation of the inflammasome provides host defence against aspergillosis(2,3), which is a major health concern for patients who are immunocompromised. However, the Aspergillus fumigatus PAMPs that are responsible for inflammasome activation are not known. Here we show that the polysaccharide galactosaminogalactan (GAG) of A. fumigatus is a PAMP that activates the NLRP3 inflammasome. The binding of GAG to ribosomal proteins inhibited cellular translation machinery, and thus activated the NLRP3 inflammasome. The galactosamine moiety bound to ribosomal proteins and blocked cellular translation, which triggered activation of the NLRP3 inflammasome. In mice, a GAG-deficient Aspergillus mutant (Delta gt4c) did not elicit protective activation of the inflammasome, and this strain exhibited enhanced virulence. Moreover, administration of GAG protected mice from colitis induced by dextran sulfate sodium in an inflammasome-dependent manner. Thus, ribosomes connect the sensing of this fungal PAMP to the activation of an innate immune response.
Published: 2020

28. NLRP3 inflammasome activation triggers gasdermin D–independent inflammation

Author: Gabriel Mbalaviele, Yael Alippe, Jianqiu Xiao, Tong Yang, Thirumala-Devi Kanneganti, Joseph B. Monahan, Kai Sun, Yousef Abu-Amer, Canxin Xu, Judy Lieberman, and Chun Wang
Subjects: Pore Forming Cytotoxic Proteins, Inflammasomes, Immunology, Mice, Transgenic, Inflammation, Pyrin domain, Article, Mice, Mice, Congenic, NLR Family, Pyrin Domain-Containing 3 Protein, medicine, Animals, Receptor, Pathogen, Cells, Cultured, Mice, Knockout, integumentary system, Chemistry, A protein, Gasdermin D, Inflammasome, General Medicine, Phosphate-Binding Proteins, Cell biology, NLRP3 inflammasome activation, medicine.symptom, medicine.drug
Abstract: NOD-like receptor (NLR), family pyrin domain containing 3 (NLRP3) assembles an intracellular protein complex known as the NLRP3 inflammasome upon sensing certain pathogen products or sterile danger signals. Gain-of-function mutations such as the D301N substitution in NLRP3, which cause its constitutive activation (NLRP3(CA)) also results in inflammasome assembly. This inflammasome processes pro-interleukin-1 β (pro-IL-1β) and pro-IL-18 into bioactive IL-1β and IL-18, respectively, and cleaves gasdermin D (GSDMD). GSDMD N-terminal fragments form plasma membrane pores that facilitate the secretion of IL-1β and IL-18 and lead to the inflammatory cell death pyroptosis. Accordingly, GSDMD inactivation results in negligible spontaneous inflammation in various experimental models such as in Nlrp3(CA/+) mice lacking GSDMD (Nlrp3(CA/+);Gsdmd(−/−) mice). Here, we found that Nlrp3(CA/+);Gsdmd(−/−) mice, when challenged with LPS or TNF-α, still secreted IL-1β and IL-18, indicating inflammasome activation independent of GSDMD. Accordingly, Gsdmd(−/−) macrophages failed to secrete IL-1β and undergo pyroptosis when briefly exposed to NLRP3 inflammasome activators (LPS and nigericin), but released these cytokines when persistently activated. Sustained NLRP3 inflammasome induced caspase-8/−3 and GSDME cleavage, and IL-1β maturation in vitro in Gsdmd(−/−) macrophages. Thus, a salvage inflammatory pathway involving caspase-8/−3-GSDME was activated following NLRP3 activation when the canonical NLRP3-GSDMD signaling was blocked. Consistent with genetic data, the active metabolite of FDA-approved disulfiram CuET, which inhibited GSDMD and GSDME cleavage in macrophages, reduced the severe inflammation and tissue damage that occurred in the Nlrp3(CA) mice. Thus, NLRP3 inflammasome activation overwhelms the protection afforded by GSDMD deficiency, rewiring signaling cascades through mechanisms that include GSDME to propagate inflammation.
Published: 2021

29. Caspase-8 is a lynchpin in caspase-3 and gasdermin D activation to control cell death, cytokine release, and host defense during influenza A virus infection

Author: Yaqiu Wang, Balabhaskararao Kancharana, Thirumala-Devi Kanneganti, Rajendra Karki, Shondra M. Pruett-Miller, SangJoon Lee, Sannula Kesavardhana, Baranda S Hansen, and Min Zheng
Subjects: Programmed cell death, Necroptosis, Immunology, medicine.disease_cause, Caspase 8, Article, Mice, Orthomyxoviridae Infections, Influenza A virus, medicine, Immunology and Allergy, Animals, Caspase, Innate immune system, biology, Cell Death, Caspase 3, Pyroptosis, Intracellular Signaling Peptides and Proteins, Phosphate-Binding Proteins, Cell biology, Apoptosis, biology.protein, Cytokines
Abstract: Programmed cell death (PCD) is essential for the innate immune response, which serves as the first line of defense against pathogens. Caspases regulate PCD, immune responses, and homeostasis. Caspase-8 specifically plays multifaceted roles in PCD pathways including pyroptosis, apoptosis, and necroptosis. However, because caspase-8–deficient mice are embryonically lethal, little is known about how caspase-8 coordinates different PCD pathways under physiological conditions. Here, we report an anti-inflammatory role of caspase-8 during influenza A virus infection. We generated viable mice carrying an uncleavable version of caspase-8 (Casp8DA/DA). We demonstrated that caspase-8 autoprocessing was responsible for activating caspase-3, thereby suppressing gasdermin D–mediated pyroptosis and inflammatory cytokine release. We also found that apoptotic and pyroptotic pathways were activated at the same time during influenza A virus infection, which enabled the cell-intrinsic anti-inflammatory function of the caspase-8–caspase-3 axis. Our findings provide new insight into the immunological consequences of caspase-8–coordinated PCD cross-talk under physiological conditions.
Published: 2021

30. ADAR1 restricts ZBP1-mediated immune response and PANoptosis to promote tumorigenesis

Author: R. K. Subbarao Malireddi, Balamurugan Sundaram, Peter Vogel, Geoffrey Neale, Bhesh Raj Sharma, Lam Nhat Nguyen, SangJoon Lee, Shelbi Christgen, Rajendra Karki, Thirumala-Devi Kanneganti, Yaqiu Wang, Min Zheng, and Parimal Samir
Subjects: Male, Programmed cell death, Skin Neoplasms, Adenosine Deaminase, QH301-705.5, Necroptosis, Melanoma, Experimental, necroptosis, Biology, medicine.disease_cause, General Biochemistry, Genetics and Molecular Biology, Article, Interferon-gamma, Antineoplastic Combined Chemotherapy Protocols, ADAR1, medicine, Animals, Humans, Biology (General), Nuclear export signal, Mice, Knockout, Cell Death, pyroptosis, Pyroptosis, apoptosis, RNA, RNA-Binding Proteins, Inflammasome, ZBP1, Triazoles, Gene Expression Regulation, Neoplastic, Mice, Inbred C57BL, tumorigenesis, Cell Transformation, Neoplastic, HEK293 Cells, Hydrazines, Apoptosis, Receptor-Interacting Protein Serine-Threonine Kinases, Cancer research, Female, Carcinogenesis, Colorectal Neoplasms, medicine.drug, Signal Transduction
Abstract: Summary: Cell death provides host defense and maintains homeostasis. Zα-containing molecules are essential for these processes. Z-DNA binding protein 1 (ZBP1) activates inflammatory cell death, PANoptosis, whereas adenosine deaminase acting on RNA 1 (ADAR1) serves as an RNA editor to maintain homeostasis. Here, we identify and characterize ADAR1’s interaction with ZBP1, defining its role in cell death regulation and tumorigenesis. Combining interferons (IFNs) and nuclear export inhibitors (NEIs) activates ZBP1-dependent PANoptosis. ADAR1 suppresses this PANoptosis by interacting with the Zα2 domain of ZBP1 to limit ZBP1 and RIPK3 interactions. Adar1fl/flLysMcre mice are resistant to development of colorectal cancer and melanoma, but deletion of the ZBP1 Zα2 domain restores tumorigenesis in these mice. In addition, treating wild-type mice with IFN-γ and the NEI KPT-330 regresses melanoma in a ZBP1-dependent manner. Our findings suggest that ADAR1 suppresses ZBP1-mediated PANoptosis, promoting tumorigenesis. Defining the functions of ADAR1 and ZBP1 in cell death is fundamental to informing therapeutic strategies for cancer and other diseases.
Published: 2021

31. The IFN-inducible GTPase IRGB10 regulates viral replication and inflammasome activation during influenza A virus infection in mice

Author: Min Zheng, Shelbi Christgen, Masahiro Yamamoto, Thirumala-Devi Kanneganti, David E. Place, and Benoit Briard
Subjects: Mice, Knockout, Inflammasomes, Immunology, Pyroptosis, Inflammasome, Context (language use), GTPase, Biology, medicine.disease_cause, Virus Replication, Article, Microbiology, GTP Phosphohydrolases, Mice, Influenza A Virus, H1N1 Subtype, Viral replication, Orthomyxoviridae Infections, Interferon, medicine, Influenza A virus, Immunology and Allergy, Animals, IRGs, medicine.drug
Abstract: The upregulation of interferon (IFN)-inducible GTPases in response to pathogenic insults is vital to host defense against many bacterial, fungal, and viral pathogens. Several IFN-inducible GTPases play key roles in mediating inflammasome activation and providing host protection after bacterial or fungal infections, though their role in inflammasome activation after viral infection is less clear. Among the IFN-inducible GTPases, the expression of immunity-related GTPases (IRGs) varies widely across species for unknown reasons. Here, we report that IRGB10, but not IRGM1, IRGM2, or IRGM3, is required for NLRP3 inflammasome activation in response to influenza A virus (IAV) infection. While IRGB10 functions to release inflammasome ligands in the context of bacterial and fungal infections, we found that IRGB10 facilitates endosomal maturation and nuclear translocation and viral replication of IAV. Corresponding with our in vitro results, we found that Irgb10-/- mice were more resistant to IAV-induced mortality than wild-type mice. The results of our study demonstrate a detrimental role of IRGB10 in host immunity in response to IAV and a novel function of IRGB10, but not IRGMs, in promoting viral translocation into the nucleus. This article is protected by copyright. All rights reserved.
Published: 2021

32. PANoptosis in viral infection: The missing puzzle piece in the cell death field

Author: Lam Nhat Nguyen and Thirumala-Devi Kanneganti
Subjects: Cell death, Programmed cell death, Necroptosis, Viral pathogenesis, viruses, Apoptosis, Review Article, Biology, Models, Biological, Virus, Inflammasome, Structural Biology, medicine, otorhinolaryngologic diseases, Pyroptosis, Animals, Humans, PANoptosis, Molecular Biology, Inflammation, Innate immune system, PANoptosome, Virology, respiratory tract diseases, Crosstalk (biology), Viral infection, Virus Diseases, medicine.drug
Abstract: In the past decade, emerging virus outbreaks like SARS-CoV-2, Zika and Ebola have presented major challenges to the global health system. Viruses are unique pathogens in that they fully rely on the host cell to complete their lifecycle and potentiate disease. Therefore, programmed cell death (PCD), a key component of the host innate immune response, is an effective strategy for the host cell to curb viral spread. The most well-established PCD pathways, pyroptosis, apoptosis and necroptosis, can be activated in response to viruses. Recently, extensive crosstalk between PCD pathways has been identified, together with evidence that molecules from all three PCD pathways can be activated during virus infection. These findings have led to the emergence of the concept of PANoptosis, defined as an inflammatory PCD pathway regulated by the PANoptosome complex with key features of pyroptosis, apoptosis, and/or necroptosis that cannot be accounted for by any of these three PCD pathways alone. While PCD is important to eliminate infected cells, many viruses are equipped to hijack host PCD pathways to benefit their own propagation and subvert host defense, and PCD can also lead to the production of inflammatory cytokines and inflammation. Therefore, viral infection can induce PANoptosis to contribute to either host defense or viral pathogenesis, depending on the virus. In this review, we will discuss the multi-faceted roles of PCD pathways in controlling viral infections.
Published: 2021

33. Molecular mechanism of RIPK1 and caspase-8 in homeostatic type I interferon production and regulation

Author: Yaqiu Wang, Rajendra Karki, Raghvendra Mall, Bhesh Raj Sharma, Ravi C. Kalathur, SangJoon Lee, Balabhaskararao Kancharana, Matthew So, Katie L. Combs, and Thirumala-Devi Kanneganti
Subjects: Caspase 8, Mice, Receptor-Interacting Protein Serine-Threonine Kinases, Interferon Type I, Animals, Homeostasis, Lymphadenopathy, Antiviral Agents, General Biochemistry, Genetics and Molecular Biology
Abstract: Type I interferons (IFNs) are essential innate immune proteins that maintain tissue homeostasis through tonic expression and can be upregulated to drive antiviral resistance and inflammation upon stimulation. However, the mechanisms that inhibit aberrant IFN upregulation in homeostasis and the impacts of tonic IFN production on health and disease remain enigmatic. Here, we report that caspase-8 negatively regulates type I IFN production by inhibiting the RIPK1-TBK1 axis during homeostasis across multiple cell types and tissues. When caspase-8 is deleted or inhibited, RIPK1 interacts with TBK1 to drive elevated IFN production, leading to heightened resistance to norovirus infection in macrophages but also early onset lymphadenopathy in mice. Combined deletion of caspase-8 and RIPK1 reduces the type I IFN signaling and lymphadenopathy, highlighting the critical role of RIPK1 in this process. Overall, our study identifies a mechanism to constrain tonic type I IFN during homeostasis which could be targeted for infectious and inflammatory diseases.
Published: 2022

34. Hierarchical Cell Death Program Disrupts the Intracellular Niche Required for Burkholderia thailandensis Pathogenesis

Author: Thirumala-Devi Kanneganti, Shelbi Christgen, Shraddha Tuladhar, R. K. Subbarao Malireddi, Peter Vogel, and David E. Place
Subjects: Male, caspase-3, caspase-11, Burkholderia thailandensis, caspase-1, Apoptosis, caspase-7, caspase-8, Mice, 0302 clinical medicine, 0303 health sciences, biology, gasdermin D, Pyroptosis, Respiratory infection, Burkholderia Infections, QR1-502, T6SS, Caspases, Female, VgrG5, Research Article, MLKL, Programmed cell death, RIPK1, Burkholderia, Necroptosis, Caspase 1, necroptosis, macrophage, Caspase-11, RIPK3, Microbiology, 03 medical and health sciences, NLRP3, inflammasome, Virology, Animals, PANoptosis, 030304 developmental biology, NLRC4, cell fusion, Macrophages, PANoptosome, biology.organism_classification, Immunity, Innate, virulence, type six secretion system, 030215 immunology
Abstract: Burkholderia infections can result in serious diseases with high mortality, such as melioidosis, and they are difficult to treat with antibiotics. Innate immunity is critical for cell-autonomous clearance of intracellular pathogens like Burkholderia by regulating programmed cell death. Inflammasome-dependent inflammatory cytokine release and cell death contribute to host protection against Burkholderia pseudomallei and Burkholderia thailandensis; however, the contribution of apoptosis and necroptosis to protection is not known. Here, we found that bone marrow-derived macrophages (BMDMs) lacking key components of pyroptosis died via apoptosis during infection. BMDMs lacking molecules required for pyroptosis, apoptosis, and necroptosis (PANoptosis), however, were significantly resistant to B. thailandensis-induced cell death until later stages of infection. Consequently, PANoptosis-deficient BMDMs failed to limit B. thailandensis-induced cell-cell fusion, which permits increased intercellular spread and replication compared to wild-type or pyroptosis-deficient BMDMs. Respiratory B. thailandensis infection resulted in higher mortality in PANoptosis-deficient mice than in pyroptosis-deficient mice, indicating that, in the absence of pyroptosis, apoptosis is essential for efficient control of infection in vivo. Together, these findings suggest both pyroptosis and apoptosis are necessary for host-mediated control of Burkholderia infection. IMPORTANCE Burkholderia infections result in a high degree of mortality when left untreated; therefore, understanding the host immune response required to control infection is critical. In this study, we found a hierarchical cell death program utilized by infected cells to disrupt the intracellular niche of Burkholderia thailandensis, which limits bacterial intercellular spread, host cell-cell fusion, and bacterial replication. In macrophages, combined loss of key PANoptosis components results in extensive B. thailandensis infection-induced cell-cell fusion, bacterial replication, and increased cell death at later stages of infection compared with both wild-type (WT) and pyroptosis-deficient cells. During respiratory infection, mortality was increased in PANoptosis-deficient mice compared to pyroptosis-deficient mice, identifying an essential role for multiple cell death pathways in controlling B. thailandensis infection. These findings advance our understanding of the physiological role of programmed cell death in controlling Burkholderia infection.
Published: 2021

35. Role of AIM2 inflammasome in inflammatory diseases, cancer and infection

Author: Thirumala-Devi Kanneganti, Rajendra Karki, and Bhesh Raj Sharma
Subjects: 0301 basic medicine, Programmed cell death, Inflammasomes, Interleukin-1beta, Immunology, Gut flora, Skin Diseases, Article, 03 medical and health sciences, AIM2, 0302 clinical medicine, Diabetes Mellitus, Pyroptosis, medicine, Animals, Humans, Immunology and Allergy, Secretion, Renal Insufficiency, Chronic, Innate immune system, biology, Effector, Interleukin-18, Inflammasome, Bacterial Infections, DNA, biology.organism_classification, Cell biology, DNA-Binding Proteins, 030104 developmental biology, Gene Expression Regulation, Mycoses, Cardiovascular Diseases, Virus Diseases, Colorectal Neoplasms, 030215 immunology, medicine.drug
Abstract: AIM2 is a cytosolic innate immune receptor which recognizes double-stranded DNA (dsDNA) released during cellular perturbation and pathogenic assault. AIM2 recognition of dsDNA leads to the assembly of a large multiprotein oligomeric complex termed the inflammasome. This inflammasome assembly leads to the secretion of bioactive interleukin-1β (IL-1β) and IL-18 and induction of an inflammatory form of cell death called pyroptosis. Sensing of dsDNA by AIM2 in the cytosol is crucial to mediate protection against the invading pathogens including bacteria, virus, fungi and parasites. AIM2 also responds to dsDNA released from damaged host cells, resulting in the secretion of the effector cytokines thereby driving the progression of sterile inflammatory diseases such as skin disease, neuronal disease, chronic kidney disease, cardiovascular disease and diabetes. Additionally, the protection mediated by AIM2 in the development of colorectal cancer depends on its ability to regulate epithelial cell proliferation and gut microbiota in maintaining intestinal homeostasis independently of the effector cytokines. In this review, we will highlight the recent progress on the role of the AIM2 inflammasome as a guardian of cellular integrity in modulating chronic inflammatory diseases, cancer and infection.
Published: 2019

36. Cell death–mediated cytokine release and its therapeutic implications

Author: Place, David E. and Kanneganti, Thirumala-Devi
Subjects: 0301 basic medicine, Programmed cell death, Necroptosis, medicine.medical_treatment, Immunology, Reviews, Review, Disease, 03 medical and health sciences, 0302 clinical medicine, Immune system, Pyroptosis, medicine, Animals, Humans, Immunology and Allergy, Cell Death, business.industry, Crosstalk (biology), 030104 developmental biology, Cytokine, Apoptosis, 030220 oncology & carcinogenesis, Cancer research, Cytokines, business, Interleukin-1
Abstract: Place and Kanneganti review the role of pyroptosis and necroptosis in driving inflammatory diseases, current cytokine blockade therapies, and the potential benefits of targeting the executioners of lytic cell death., Targeting apoptosis to treat diseases has seen tremendous success over the past decades. More recently, alternative forms of regulated cell death, including pyroptosis and necroptosis, have been described. Understanding the molecular cascades regulating both pyroptosis and necroptosis will yield even more targets to treat diseases. These lytic forms of cell death are distinct from apoptosis due to their characteristic lysis and release of cellular components that promote disease or direct a beneficial immune response. In this review, we focus on how pyroptosis and necroptosis, which release potent immune cytokines such as IL-1 and IL-18, contribute to various diseases. We also consider the important role that the executioners of these cell death pathways, GSDMD and MLKL, play in the progression of inflammatory diseases. Crosstalk between the different cell death pathways likely plays a major role physiologically. New therapeutic strategies targeting these specific molecules hold enormous potential for managing inflammatory diseases.
Published: 2019

37. Differential role of the <scp>NLRP</scp> 3 inflammasome in infection and tumorigenesis

Author: Sarang Tartey and Thirumala-Devi Kanneganti
Subjects: Carcinogenesis, Inflammasomes, Immunology, Inflammation, Nod, Infections, Immune system, Neoplasms, NOD2, NLR Family, Pyrin Domain-Containing 3 Protein, NOD1, Animals, Humans, Immunology and Allergy, Medicine, Review Articles, integumentary system, business.industry, Cancer, Inflammasome, medicine.disease, Cancer research, medicine.symptom, business, Periodic fever syndrome, medicine.drug
Abstract: Dysregulated inflammation is one of the hallmarks of cancer initiation and progression. Emerging evidence indicates that inflammasomes play a central role in regulating immune cell functions in various infections and cancer. Inflammasomes are multimeric complexes consisting of nucleotide-binding oligomerization domain (NOD) -like receptors (NLRs). Among the NLRs, NOD1, NOD2 and NLRP3 respond to a variety of endogenous (i.e. damage-associated molecular patterns) and exogenous (i.e. pathogen-associated molecular patterns) stimuli. The NLRP3 inflammasome is associated with the onset and progression of autoinflammatory and autoimmune diseases, including metabolic disorders, multiple sclerosis, inflammatory bowel disease, and cryopyrin-associated periodic fever syndrome. NLRP3 is also associated with a wide variety of infections and tumorigenesis that are closely correlated with chemotherapy response and prognosis. In this review, we explore the rapidly expanding body of research on the expression and functions of NLRP3 in infections and cancers and outline novel inhibitors targeting the NLRP3 inflammasome that could be developed as therapeutic alternatives to current anticancer treatment.
Published: 2019

38. Gasdermin D Promotes AIM2 Inflammasome Activation and Is Required for Host Protection against Francisella novicida

Author: Arjun Balakrishnan, Thirumala-Devi Kanneganti, Rajendra Karki, Min Zheng, and Qifan Zhu
Subjects: Lipopolysaccharides, Male, 0301 basic medicine, Programmed cell death, Inflammasomes, Interleukin-1beta, Immunology, Biology, medicine.disease_cause, Article, 03 medical and health sciences, AIM2, 0302 clinical medicine, Pyroptosis, medicine, Animals, Immunology and Allergy, Francisella novicida, Francisella tularensis, Receptor, Cells, Cultured, Mice, Knockout, Receptors, Interleukin-1 Type I, Macrophages, Caspase 1, Interleukin-18, Intracellular Signaling Peptides and Proteins, Inflammasome, Transfection, Phosphate-Binding Proteins, bacterial infections and mycoses, Cell biology, DNA-Binding Proteins, Mice, Inbred C57BL, 030104 developmental biology, Female, Apoptosis Regulatory Proteins, Gram-Negative Bacterial Infections, Inflammasome complex, 030215 immunology, medicine.drug
Abstract: The DNA sensor absent in melanoma 2 (AIM2) forms an inflammasome complex with ASC and caspase-1 in response to Francisella tularensis subspecies novicida infection, leading to maturation of IL-1b and IL-18 and pyroptosis. AIM2 is critical for host protection against F. novicida infection in vivo; however, the role of pyroptosis downstream of the AIM2 inflammasome is unknown. Recent studies have identified gasdermin D (GSDMD) as the molecule executing pyroptosis by forming pores on the plasma membrane following activation by inflammatory caspase-1 and -11. In this study, we report that GSDMD-deficient mice were susceptible to F. novicida infection compared with wild type mice. Interestingly, we observed that GSDMD is required for optimal caspase-1 activation and pyroptotic cell death in F. novicida–infected bone marrow–derived macrophages. Furthermore, caspase-1 activation was compromised in bone marrow–derived macrophages lacking GSDMD stimulated with other AIM2 inflammasome triggers, including poly(dA:dT) transfection and mouse CMV infection. Overall, our study highlights a function, to our knowledge previously unknown, for GSDMD in promoting caspase-1 activation by AIM2 inflammasome.
Published: 2018

39. TNF/TNFR axis promotes pyrin inflammasome activation and distinctly modulates pyrin inflammasomopathy

Author: Clifford S. Guy, Deepika Sharma, Peter Vogel, Thirumala-Devi Kanneganti, and Ankit Malik
Subjects: 0301 basic medicine, Inflammasomes, Familial Mediterranean fever, Inflammation, Pyrin domain, Proinflammatory cytokine, Mice, 03 medical and health sciences, 0302 clinical medicine, medicine, Animals, Receptors, Tumor Necrosis Factor, Type II, Myeloid Cells, Gene Knock-In Techniques, Receptor, Mice, Knockout, Tumor Necrosis Factor-alpha, business.industry, Inflammasome, General Medicine, Pyrin, medicine.disease, MEFV, 030104 developmental biology, Receptors, Tumor Necrosis Factor, Type I, Immunology, Tumor necrosis factor alpha, medicine.symptom, business, Research Article, Signal Transduction, 030215 immunology, medicine.drug
Abstract: Pyrin is an inflammasome sensor that promotes caspase-1–mediated pyroptotic cell death and maturation of proinflammatory cytokines IL-1β and IL-18. Familial Mediterranean fever (FMF), an autoinflammatory disorder, is associated with mutations in the gene encoding pyrin (MEFV). FMF-knockin (FMF-KI) mice that express chimeric pyrin protein with FMF mutation (Mefv(V726A/V726A)) exhibit an autoinflammatory disorder mediated by autoactivation of the pyrin inflammasome. Increase in the levels of TNF are observed in FMF-KI mice, and many features of FMF overlap with the autoinflammatory disorder associated with TNF receptor signaling. In this study, we assessed the contribution of TNF signaling to pyrin inflammasome activation and its consequent role in distinct FMF pathologies. TNF signaling promoted the expression of pyrin in response to multiple stimuli and was required for inflammasome activation in response to canonical pyrin stimuli and in myeloid cells from FMF-KI mice. TNF signaling promoted systemic wasting, anemia, and neutrophilia in the FMF-KI mice. Further, TNF-induced pathology was induced specifically through the TNFR1 receptor, while TNFR2-mediated signaling was distinctly protective in colitis and ankle joint inflammation. Overall, our data show that TNF is a critical modulator of pyrin expression, inflammasome activation, and pyrin-inflammasomopathy. Further, specific blockade of TNFR1 or activation of TNFR2 could provide substantial protection against FMF pathologies.
Published: 2018

40. Intestinal tête-à-tête: helminths blunt immunity against flaviviruses

Author: David E. Place and Thirumala-Devi Kanneganti
Subjects: viruses, Biology, CD8-Positive T-Lymphocytes, Severity of Illness Index, Article, Mice, Blunt, Immunity, Helminths, parasitic diseases, Animals, Intestinal Mucosa, Molecular Biology, Strongylida Infections, Neurons, Nematospiroides dubius, Coinfection, Flavivirus, Cell Biology, Virology, Research Highlight, Receptors, Interleukin-4, Intestines, Mice, Inbred C57BL, Disease Models, Animal, Disease Susceptibility, STAT6 Transcription Factor, West Nile virus, Signal Transduction
Abstract: Although enteric helminth infections modulate immunity to mucosal pathogens, their effects on systemic microbes remain less established. Here, we observe increased mortality in mice coinfected with the enteric helminth Heligmosomoides polygyrus bakeri (Hpb) and West Nile virus (WNV). This enhanced susceptibility is associated with altered gut morphology and transit, translocation of commensal bacteria, impaired WNV-specific T cell responses, and increased virus infection in the gastrointestinal tract and central nervous system. These outcomes were due to type 2 immune skewing, as coinfection in Stat6(−/−) mice rescues mortality, treatment of helminth-free WNV-infected mice with IL-4 mirrors coinfection, and IL-4 receptor signaling in intestinal epithelial cells mediates the susceptibility phenotypes. Moreover, tuft cell-deficient mice show improved outcomes with coinfection, whereas treatment of helminth-free mice with tuft cell-derived cytokine IL-25 or ligand succinate worsens WNV disease. Thus, helminth activation of tuft cell-IL-4-receptor circuits in the gut exacerbates infection and disease of a neurotropic flavivirus.
Published: 2021

41. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)1

Author: Klionsky, Daniel J, Abdel-Aziz, Amal Kamal, Abdelfatah, Sara, Abdellatif, Mahmoud, Abdoli, Asghar, Abel, Steffen, Abeliovich, Hagai, Abildgaard, Marie H, Abudu, Yakubu Princely, Acevedo-Arozena, Abraham, Adamopoulos, Iannis E, Adeli, Khosrow, Adolph, Timon E, Adornetto, Annagrazia, Aflaki, Elma, Agam, Galila, Agarwal, Anupam, Aggarwal, Bharat B, Agnello, Maria, Agostinis, Patrizia, Agrewala, Javed N, Agrotis, Alexander, Aguilar, Patricia V, Ahmad, S Tariq, Ahmed, Zubair M, Ahumada-Castro, Ulises, Aits, Sonja, Aizawa, Shu, Akkoc, Yunus, Akoumianaki, Tonia, Akpinar, Hafize Aysin, Al-Abd, Ahmed M, Al-Akra, Lina, Al-Gharaibeh, Abeer, Alaoui-Jamali, Moulay A, Alberti, Simon, Alcocer-Gómez, Elísabet, Alessandri, Cristiano, Ali, Muhammad, Alim Al-Bari, M Abdul, Aliwaini, Saeb, Alizadeh, Javad, Almacellas, Eugènia, Almasan, Alexandru, Alonso, Alicia, Alonso, Guillermo D, Altan-Bonnet, Nihal, Altieri, Dario C, Álvarez, Élida MC, Alves, Sara, Alves Da Costa, Cristine, Alzaharna, Mazen M, Amadio, Marialaura, Amantini, Consuelo, Amaral, Cristina, Ambrosio, Susanna, Amer, Amal O, Ammanathan, Veena, An, Zhenyi, Andersen, Stig U, Andrabi, Shaida A, Andrade-Silva, Magaiver, Andres, Allen M, Angelini, Sabrina, Ann, David, Anozie, Uche C, Ansari, Mohammad Y, Antas, Pedro, Antebi, Adam, Antón, Zuriñe, Anwar, Tahira, Apetoh, Lionel, Apostolova, Nadezda, Araki, Toshiyuki, Araki, Yasuhiro, Arasaki, Kohei, Araújo, Wagner L, Araya, Jun, Arden, Catherine, Arévalo, Maria-Angeles, Arguelles, Sandro, Arias, Esperanza, Arikkath, Jyothi, Arimoto, Hirokazu, Ariosa, Aileen R, Armstrong-James, Darius, Arnauné-Pelloquin, Laetitia, Aroca, Angeles, Arroyo, Daniela S, Arsov, Ivica, Artero, Rubén, Asaro, Dalia Maria Lucia, Aschner, Michael, Ashrafizadeh, Milad, Ashur-Fabian, Osnat, Atanasov, Atanas G, Au, Alicia K, Auberger, Patrick, Auner, Holger W, Aurelian, Laure, Autelli, Riccardo, Avagliano, Laura, Ávalos, Yenniffer, Aveic, Sanja, Aveleira, Célia Alexandra, Avin-Wittenberg, Tamar, Aydin, Yucel, Ayton, Scott, Ayyadevara, Srinivas, Azzopardi, Maria, Baba, Misuzu, Backer, Jonathan M, Backues, Steven K, Bae, Dong-Hun, Bae, Ok-Nam, Bae, Soo Han, Baehrecke, Eric H, Baek, Ahruem, Baek, Seung-Hoon, Baek, Sung Hee, Bagetta, Giacinto, Bagniewska-Zadworna, Agnieszka, Bai, Hua, Bai, Jie, Bai, Xiyuan, Bai, Yidong, Bairagi, Nandadulal, Baksi, Shounak, Balbi, Teresa, Baldari, Cosima T, Balduini, Walter, Ballabio, Andrea, Ballester, Maria, Balazadeh, Salma, Balzan, Rena, Bandopadhyay, Rina, Banerjee, Sreeparna, Banerjee, Sulagna, Bánréti, Ágnes, Bao, Yan, Baptista, Mauricio S, Baracca, Alessandra, Barbati, Cristiana, Bargiela, Ariadna, Barilà, Daniela, Barlow, Peter G, Barmada, Sami J, Barreiro, Esther, Barreto, George E, Bartek, Jiri, Bartel, Bonnie, Bartolome, Alberto, Barve, Gaurav R, Basagoudanavar, Suresh H, Bassham, Diane C, Bast, Robert C, Basu, Alakananda, Batoko, Henri, Batten, Isabella, Baulieu, Etienne E, Baumgarner, Bradley L, Bayry, Jagadeesh, Beale, Rupert, Beau, 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Anthony, Sinha, Sangita, Sirko, Agnieszka, Sirohi, Kapil, Sivridis, Efthimios L, Skendros, Panagiotis, Skirycz, Aleksandra, Slaninová, Iva, Smaili, Soraya S, Smertenko, Andrei, Smith, Matthew D, Soenen, Stefaan J, Sohn, Eun Jung, Sok, Sophia PM, Solaini, Giancarlo, Soldati, Thierry, Soleimanpour, Scott A, Soler, Rosa M, Solovchenko, Alexei, Somarelli, Jason A, Sonawane, Avinash, Song, Fuyong, Song, Hyun Kyu, Song, Ju-Xian, Song, Kunhua, Song, Zhiyin, Soria, Leandro R, Sorice, Maurizio, Soukas, Alexander A, Soukup, Sandra-Fausia, Sousa, Diana, Sousa, Nadia, Spagnuolo, Paul A, Spector, Stephen A, Srinivas Bharath, MM, St Clair, Daret, Stagni, Venturina, Staiano, Leopoldo, Stalnecker, Clint A, Stankov, Metodi V, Stathopulos, Peter B, Stefan, Katja, Stefan, Sven Marcel, Stefanis, Leonidas, Steffan, Joan S, Steinkasserer, Alexander, Stenmark, Harald, Sterneckert, Jared, Stevens, Craig, Stoka, Veronika, Storch, Stephan, Stork, Björn, Strappazzon, Flavie, Strohecker, Anne Marie, Stupack, 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Tsao, Betty P, Tschan, Mario P, Tse, Hung-Fat, Tse, Tak Fu, Tsugawa, Hitoshi, Tsvetkov, Andrey S, Tumbarello, David A, Tumtas, Yasin, Tuñón, María J, Turcotte, Sandra, Turk, Boris, Turk, Vito, Turner, Bradley J, Tuxworth, Richard I, Tyler, Jessica K, Tyutereva, Elena V, Uchiyama, Yasuo, Ugun-Klusek, Aslihan, Uhlig, Holm H, Ułamek-Kozioł, Marzena, Ulasov, Ilya V, Umekawa, Midori, Ungermann, Christian, Unno, Rei, Urbe, Sylvie, Uribe-Carretero, Elisabet, Üstün, Suayib, Uversky, Vladimir N, Vaccari, Thomas, Vaccaro, Maria I, Vahsen, Björn F, Vakifahmetoglu-Norberg, Helin, Valdor, Rut, Valente, Maria J, Valko, Ayelén, Vallee, Richard B, Valverde, Angela M, Van Den Berghe, Greet, Van Der Veen, Stijn, Van Kaer, Luc, Van Loosdregt, Jorg, Van Wijk, Sjoerd JL, Vandenberghe, Wim, Vanhorebeek, Ilse, Vannier-Santos, Marcos A, Vannini, Nicola, Vanrell, M Cristina, Vantaggiato, Chiara, Varano, Gabriele, Varela-Nieto, Isabel, Varga, Máté, Vasconcelos, M Helena, Vats, Somya, Vavvas, Demetrios G, Vega-Naredo, Ignacio, Vega-Rubin-De-Celis, Silvia, Velasco, Guillermo, Velázquez, Ariadna P, Vellai, Tibor, Vellenga, Edo, Velotti, Francesca, Verdier, Mireille, Verginis, Panayotis, Vergne, Isabelle, Verkade, Paul, Verma, Manish, Verstreken, Patrik, Vervliet, Tim, Vervoorts, Jörg, Vessoni, Alexandre T, Victor, Victor M, Vidal, Michel, Vidoni, Chiara, Vieira, Otilia V, Vierstra, Richard D, Viganó, Sonia, Vihinen, Helena, Vijayan, Vinoy, Vila, Miquel, Vilar, Marçal, Villalba, José M, Villalobo, Antonio, Villarejo-Zori, Beatriz, Villarroya, Francesc, Villarroya, Joan, Vincent, Olivier, Vindis, Cecile, Viret, Christophe, Viscomi, Maria Teresa, Visnjic, Dora, Vitale, Ilio, Vocadlo, David J, Voitsekhovskaja, Olga V, Volonté, Cinzia, Volta, Mattia, Vomero, Marta, Von Haefen, Clarissa, Vooijs, Marc A, Voos, Wolfgang, Vucicevic, Ljubica, Wade-Martins, Richard, Waguri, Satoshi, Waite, Kenrick A, Wakatsuki, Shuji, Walker, David W, Walker, Mark J, Walker, Simon A, Walter, Jochen, Wandosell, Francisco G, Wang, Bo, Wang, Chao-Yung, Wang, Chen, Wang, Chenran, Wang, Chenwei, Wang, Cun-Yu, Wang, Dong, Wang, Fangyang, Wang, Feng, Wang, Fengming, Wang, Guansong, Wang, Han, Wang, Hao, Wang, Hexiang, Wang, Hong-Gang, Wang, Jianrong, Wang, Jigang, Wang, Jiou, Wang, Jundong, Wang, Kui, Wang, Lianrong, Wang, Liming, Wang, Maggie Haitian, Wang, Meiqing, Wang, Nanbu, Wang, Pengwei, Wang, Peipei, Wang, Ping, Wang, Qing Jun, Wang, Qing, Wang, Qing Kenneth, Wang, Qiong A, Wang, Wen-Tao, Wang, Wuyang, Wang, Xinnan, Wang, Xuejun, Wang, Yan, Wang, Yanchang, Wang, Yanzhuang, Wang, Yen-Yun, Wang, Yihua, Wang, Yipeng, Wang, Yu, Wang, Yuqi, Wang, Zhe, Wang, Zhenyu, Wang, Zhouguang, Warnes, Gary, Warnsmann, Verena, Watada, Hirotaka, Watanabe, Eizo, Watchon, Maxinne, Wawrzyńska, Anna, Weaver, Timothy E, Wegrzyn, Grzegorz, Wehman, Ann M, Wei, Huafeng, Wei, Lei, Wei, Taotao, Wei, Yongjie, Weiergräber, Oliver H, Weihl, Conrad C, Weindl, Günther, Weiskirchen, Ralf, Wells, Alan, Wen, Runxia H, Wen, Xin, Werner, Antonia, Weykopf, Beatrice, Wheatley, Sally P, Whitton, J Lindsay, Whitworth, Alexander J, Wiktorska, Katarzyna, Wildenberg, Manon E, Wileman, Tom, Wilkinson, Simon, Willbold, Dieter, Williams, Brett, Williams, Robin SB, Williams, Roger L, Williamson, Peter R, Wilson, Richard A, Winner, Beate, Winsor, Nathaniel J, Witkin, Steven S, Wodrich, Harald, Woehlbier, Ute, Wollert, Thomas, Wong, Esther, Wong, Jack Ho, Wong, Richard W, Wong, Vincent Kam Wai, Wong, W Wei-Lynn, Wu, An-Guo, Wu, Chengbiao, Wu, Jian, Wu, Junfang, Wu, Kenneth K, Wu, Min, Wu, Shan-Ying, Wu, Shengzhou, Wu, Shu-Yan, Wu, Shufang, Wu, William KK, Wu, Xiaohong, Wu, Xiaoqing, Wu, Yao-Wen, Wu, Yihua, Xavier, Ramnik J, Xia, Hongguang, Xia, Lixin, Xia, Zhengyuan, Xiang, Ge, Xiang, Jin, Xiang, Mingliang, Xiang, Wei, Xiao, Bin, Xiao, Guozhi, Xiao, Hengyi, Xiao, Hong-Tao, Xiao, Jian, Xiao, Lan, Xiao, Shi, Xiao, Yin, Xie, Baoming, Xie, Chuan-Ming, Xie, Min, Xie, Yuxiang, Xie, Zhiping, Xie, Zhonglin, Xilouri, Maria, Xu, Congfeng, Xu, En, Xu, Haoxing, Xu, Jing, Xu, JinRong, Xu, Liang, Xu, Wen Wen, Xu, Xiulong, Xue, Yu, Yakhine-Diop, Sokhna MS, Yamaguchi, Masamitsu, Yamaguchi, Osamu, Yamamoto, Ai, Yamashina, Shunhei, Yan, Shengmin, Yan, Shian-Jang, Yan, Zhen, Yanagi, Yasuo, Yang, Chuanbin, Yang, Dun-Sheng, Yang, Huan, Yang, Huang-Tian, Yang, Hui, Yang, Jin-Ming, Yang, Jing, Yang, Jingyu, Yang, Ling, Yang, Liu, Yang, Ming, Yang, Pei-Ming, Yang, Qian, Yang, Seungwon, Yang, Shu, Yang, Shun-Fa, Yang, Wannian, Yang, Wei Yuan, Yang, Xiaoyong, Yang, Xuesong, Yang, Yi, Yang, Ying, Yao, Honghong, Yao, Shenggen, Yao, Xiaoqiang, Yao, Yong-Gang, Yao, Yong-Ming, Yasui, Takahiro, Yazdankhah, Meysam, Yen, Paul M, Yi, Cong, Yin, Xiao-Ming, Yin, Yanhai, Yin, Zhangyuan, Yin, Ziyi, Ying, Meidan, Ying, Zheng, Yip, Calvin K, Yiu, Stephanie Pei Tung, Yoo, Young H, Yoshida, Kiyotsugu, Yoshii, Saori R, Yoshimori, Tamotsu, Yousefi, Bahman, Yu, Boxuan, Yu, Haiyang, Yu, Jun, Yu, Li, Yu, Ming-Lung, Yu, Seong-Woon, Yu, Victor C, Yu, W Haung, Yu, Zhengping, Yu, Zhou, Yuan, Junying, Yuan, Ling-Qing, Yuan, Shilin, Yuan, Shyng-Shiou F, Yuan, Yanggang, Yuan, Zengqiang, Yue, Jianbo, Yue, Zhenyu, Yun, Jeanho, Yung, Raymond L, Zacks, David N, Zaffagnini, Gabriele, Zambelli, Vanessa O, Zanella, Isabella, Zang, Qun S, Zanivan, Sara, Zappavigna, Silvia, Zaragoza, Pilar, Zarbalis, Konstantinos S, Zarebkohan, Amir, Zarrouk, Amira, Zeitlin, Scott O, Zeng, Jialiu, Zeng, Ju-Deng, Žerovnik, Eva, Zhan, Lixuan, Zhang, Bin, Zhang, Donna D, Zhang, Hanlin, Zhang, Hong, Zhang, Honghe, Zhang, Huafeng, Zhang, Huaye, Zhang, Hui, Zhang, Hui-Ling, Zhang, Jianbin, Zhang, Jianhua, Zhang, Jing-Pu, Zhang, Kalin YB, Zhang, Leshuai W, Zhang, Lin, Zhang, Lisheng, Zhang, Lu, Zhang, Luoying, Zhang, Menghuan, Zhang, Peng, Zhang, Sheng, Zhang, Wei, Zhang, Xiangnan, Zhang, Xiao-Wei, Zhang, Xiaolei, Zhang, Xiaoyan, Zhang, Xin, Zhang, Xinxin, Zhang, Xu Dong, Zhang, Yang, Zhang, Yanjin, Zhang, Yi, Zhang, Ying-Dong, Zhang, Yingmei, Zhang, Yuan-Yuan, Zhang, Yuchen, Zhang, Zhe, Zhang, Zhengguang, Zhang, Zhibing, Zhang, Zhihai, Zhang, Zhiyong, Zhang, Zili, Zhao, Haobin, Zhao, Lei, Zhao, Shuang, Zhao, Tongbiao, Zhao, Xiao-Fan, Zhao, Ying, Zhao, Yongchao, Zhao, Yongliang, Zhao, Yuting, Zheng, Guoping, Zheng, Kai, Zheng, Ling, Zheng, Shizhong, Zheng, Xi-Long, Zheng, Yi, Zheng, Zu-Guo, Zhivotovsky, Boris, Zhong, Qing, Zhou, Ao, Zhou, Ben, Zhou, Cefan, Zhou, Gang, Zhou, Hao, Zhou, Hong, Zhou, Hongbo, Zhou, Jie, Zhou, Jing, Zhou, Jiyong, Zhou, Kailiang, Zhou, Rongjia, Zhou, Xu-Jie, Zhou, Yanshuang, Zhou, Yinghong, Zhou, Yubin, Zhou, Zheng-Yu, Zhou, Zhou, Zhu, Binglin, Zhu, Changlian, Zhu, Guo-Qing, Zhu, Haining, Zhu, Hongxin, Zhu, Hua, Zhu, Wei-Guo, Zhu, Yanping, Zhu, Yushan, Zhuang, Haixia, Zhuang, Xiaohong, Zientara-Rytter, Katarzyna, Zimmermann, Christine M, Ziviani, Elena, Zoladek, Teresa, Zong, Wei-Xing, Zorov, Dmitry B, Zorzano, Antonio, Zou, Weiping, Zou, Zhen, Zou, Zhengzhi, Zuryn, Steven, Zwerschke, Werner, Brand-Saberi, Beate, Dong, X Charlie, Kenchappa, Chandra Shekar, Li, Zuguo, Lin, Yong, Oshima, Shigeru, Rong, Yueguang, Sluimer, Judith C, Stallings, Christina L, and Tong, Chun-Kit
Subjects: phagophore, vacuole, Autophagosome, neurodegeneration, Autophagosomes, Autophagy-Related Proteins, flux, macroautophagy, stress, LC3, lysosome, Autophagy, cancer, Animals, Humans, Biological Assay, Lysosomes, Biomarkers
Abstract: In 2008, we published the first set of guidelines for standardizing research in autophagy. Since then, this topic has received increasing attention, and many scientists have entered the field. Our knowledge base and relevant new technologies have also been expanding. Thus, it is important to formulate on a regular basis updated guidelines for monitoring autophagy in different organisms. Despite numerous reviews, there continues to be confusion regarding acceptable methods to evaluate autophagy, especially in multicellular eukaryotes. Here, we present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes. These guidelines are not meant to be a dogmatic set of rules, because the appropriateness of any assay largely depends on the question being asked and the system being used. Moreover, no individual assay is perfect for every situation, calling for the use of multiple techniques to properly monitor autophagy in each experimental setting. Finally, several core components of the autophagy machinery have been implicated in distinct autophagic processes (canonical and noncanonical autophagy), implying that genetic approaches to block autophagy should rely on targeting two or more autophagy-related genes that ideally participate in distinct steps of the pathway. Along similar lines, because multiple proteins involved in autophagy also regulate other cellular pathways including apoptosis, not all of them can be used as a specific marker for bona fide autophagic responses. Here, we critically discuss current methods of assessing autophagy and the information they can, or cannot, provide. Our ultimate goal is to encourage intellectual and technical innovation in the field.
Published: 2021
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42. Role of inflammasomes/pyroptosis and PANoptosis during fungal infection

Author: Benoit Briard, R. K. Subbarao Malireddi, and Thirumala-Devi Kanneganti
Subjects: Inflammasomes, Apoptosis, Yeast and Fungal Models, Pathology and Laboratory Medicine, Biochemistry, Immune Receptors, Pearls, Aspergillus fumigatus, White Blood Cells, Medical Conditions, Animal Cells, Medicine and Health Sciences, Biology (General), Toll-like Receptors, Candida, Fungal Pathogens, Immune System Proteins, biology, Cell Death, Pyroptosis, Fungal Diseases, Eukaryota, Aspergillus, Infectious Diseases, Experimental Organism Systems, Aspergillus Fumigatus, Medical Microbiology, Fungal Molds, Cell Processes, Receptor-Interacting Protein Serine-Threonine Kinases, Pathogens, Cellular Types, Signal Transduction, Programmed cell death, QH301-705.5, Immune Cells, Immunology, Mycology, Research and Analysis Methods, Microbiology, Virology, NLR Family, Pyrin Domain-Containing 3 Protein, Genetics, Animals, Humans, Candida Albicans, Molecular Biology, Microbial Pathogens, Blood Cells, Macrophages, Organisms, Fungi, Biology and Life Sciences, Proteins, Cell Biology, RC581-607, biology.organism_classification, Yeast, Mycoses, Animal Studies, Parasitology, Immunologic diseases. Allergy
Published: 2021

43. DDX3X coordinates host defense against influenza virus by activating the NLRP3 inflammasome and type I interferon response

Author: Min Zheng, Parimal Samir, Rajendra Karki, Benoit Briard, David E. Place, R. K. Subbarao Malireddi, Thirumala-Devi Kanneganti, Bhesh Raj Sharma, Sannula Kesavardhana, and Peter Vogel
Subjects: 0301 basic medicine, P-eIF2α, phosphorylation of eIF2α, Inflammasomes, NS1, CASP1, caspase-1, Biochemistry, P-IRF3, phosphorylation of IRF3, DEAD-box RNA Helicases, Mice, iBMDMs, immortalized BMDMs, Interferon, innate immunity, Ars, arsenite, MCMV, murine cytomegalovirus, NP, nucleoprotein, STAT1, signal transducer and activator of transcription 1, MOI, multiplicity of infection, Toll-like receptor, RIG-I, HRP, horseradish peroxidase, Inflammasome, CASP3, caspase-3, Cell biology, G3BP1, GTPase-activating protein-binding protein 1, host defense, Interferon Type I, DDX3X, medicine.drug, Research Article, TLR, Toll-like receptor, VSV, vesicular stomatitis virus, PR8, Puerto Rico/8/34, IRF1, interferon regulatory factor 1, Biology, stress granule, 03 medical and health sciences, Immune system, Stress granule, NLRP3, inflammasome, NLR Family, Pyrin Domain-Containing 3 Protein, CASP8, caspase-8, IAV, influenza A virus, medicine, Animals, influenza A virus, DDX3X, DEAD-box helicase 3 X-linked, IFN, interferon, Molecular Biology, immune evasion, NS1, nonstructural protein 1, Innate immune system, ΔNS1, NS1 deletion mutant, 030102 biochemistry & molecular biology, Cell Biology, ASC, apoptosis-associated speck-like protein containing a caspase recruitment domain, SG, stress granule, NLRP3, nucleotide-binding oligomerization domain-like receptor with a pyrin domain 3, Immunity, Innate, IL, interleukin, RIG-I, retinoic acid–inducible gene I, 030104 developmental biology, IRF1, BMDM, bone marrow–derived macrophage, type I IFN
Abstract: Viruses and hosts have coevolved for millions of years, leading to the development of complex host-pathogen interactions. Influenza A virus (IAV) causes severe pulmonary pathology and is a recurrent threat to human health. Innate immune sensing of IAV triggers a complex chain of host responses. IAV has adapted to evade host defense mechanisms, and the host has coevolved to counteract these evasion strategies. However, the molecular mechanisms governing the balance between host defense and viral immune evasion is poorly understood. Here, we show that the host protein DEAD-box helicase 3 X-linked (DDX3X) is critical to orchestrate a multifaceted antiviral innate response during IAV infection, coordinating the activation of the nucleotide-binding oligomerization domain-like receptor with a pyrin domain 3 (NLRP3) inflammasome, assembly of stress granules, and type I interferon (IFN) responses. DDX3X activated the NLRP3 inflammasome in response to WT IAV, which carries the immune evasive nonstructural protein 1 (NS1). However, in the absence of NS1, DDX3X promoted the formation of stress granules that facilitated efficient activation of type I IFN signaling. Moreover, induction of DDX3X-containing stress granules by external stimuli after IAV infection led to increased type I IFN signaling, suggesting that NS1 actively inhibits stress granule-mediated host responses and DDX3X-mediated NLRP3 activation counteracts this action. Furthermore, the loss of DDX3X expression in myeloid cells caused severe pulmonary pathogenesis and morbidity in IAV-infected mice. Together, our findings show that DDX3X orchestrates alternate modes of innate host defense which are critical to fight against NS1-mediated immune evasion strategies during IAV infection.
Published: 2021

44. Osteoclast fusion and bone loss are restricted by interferon inducible guanylate binding proteins

Author: Jieun Kim, R. K. Subbarao Malireddi, David E. Place, Masahiro Yamamoto, Peter Vogel, and Thirumala-Devi Kanneganti
Subjects: musculoskeletal diseases, 0301 basic medicine, Science, Osteoimmunology, Immunology, Osteoclasts, General Physics and Astronomy, Mice, Transgenic, Inflammation, Osteoclast fusion, Article, General Biochemistry, Genetics and Molecular Biology, Bone remodeling, Cell Fusion, 03 medical and health sciences, 0302 clinical medicine, GTP-Binding Proteins, Osteogenesis, Osteoclast, Interferon, Osteoarthritis, medicine, Animals, Bone Resorption, Cells, Cultured, Mice, Knockout, Multidisciplinary, Innate immune system, Chemistry, Age Factors, Cell Differentiation, General Chemistry, Cell biology, Mice, Inbred C57BL, 030104 developmental biology, medicine.anatomical_structure, IRF1, 030220 oncology & carcinogenesis, Interferons, medicine.symptom, Cell signalling, Signal Transduction, medicine.drug
Abstract: Chronic inflammation during many diseases is associated with bone loss. While interferons (IFNs) are often inhibitory to osteoclast formation, the complex role that IFN and interferon-stimulated genes (ISGs) play in osteoimmunology during inflammatory diseases is still poorly understood. We show that mice deficient in IFN signaling components including IFN alpha and beta receptor 1 (IFNAR1), interferon regulatory factor 1 (IRF1), IRF9, and STAT1 each have reduced bone density and increased osteoclastogenesis compared to wild type mice. The IFN-inducible guanylate-binding proteins (GBPs) on mouse chromosome 3 (GBP1, GBP2, GBP3, GBP5, GBP7) are required to negatively regulate age-associated bone loss and osteoclastogenesis. Mechanistically, GBP2 and GBP5 both negatively regulate in vitro osteoclast differentiation, and loss of GBP5, but not GBP2, results in greater age-associated bone loss in mice. Moreover, mice deficient in GBP5 or chromosome 3 GBPs have greater LPS-mediated inflammatory bone loss compared to wild type mice. Overall, we find that GBP5 contributes to restricting age-associated and inflammation-induced bone loss by negatively regulating osteoclastogenesis., The innate immune system and inflammation modulate bone homeostasis through complex regulation of bone remodelling cells including osteoblasts and osteoclasts. Here, the authors show that the type I interferon pathway and guanylate binding proteins functionally limit bone loss by inhibiting osteoclast functions.
Published: 2021

45. TLR2 senses the SARS-CoV-2 envelope protein to produce inflammatory cytokines

Author: Evan P. Williams, Colleen B. Jonsson, Thirumala-Devi Kanneganti, Peter Vogel, Rajendra Karki, Elizabeth A. Fitzpatrick, Min Zheng, and Dong Yang
Subjects: 0301 basic medicine, Male, Chemokine, viruses, medicine.medical_treatment, Immunology, Primary Cell Culture, Severity of Illness Index, Proinflammatory cytokine, 03 medical and health sciences, Coronavirus Envelope Proteins, Mice, 0302 clinical medicine, Viral entry, Chlorocebus aethiops, medicine, Immunology and Allergy, Animals, Humans, Vero Cells, Mice, Knockout, Innate immune system, biology, SARS-CoV-2, Gene Expression Profiling, Macrophages, COVID-19, medicine.disease, Immunity, Innate, Toll-Like Receptor 2, COVID-19 Drug Treatment, TLR2, Cytokine release syndrome, Disease Models, Animal, 030104 developmental biology, Cytokine, Myeloid Differentiation Factor 88, biology.protein, Leukocytes, Mononuclear, Cytokines, Female, Cytokine storm, Cytokine Release Syndrome, 030215 immunology, Signal Transduction
Abstract: The innate immune response is critical for recognizing and controlling infections through the release of cytokines and chemokines. However, severe pathology during some infections, including SARS-CoV-2, is driven by hyperactive cytokine release, or a cytokine storm. The innate sensors that activate production of proinflammatory cytokines and chemokines during COVID-19 remain poorly characterized. In the present study, we show that both TLR2 and MYD88 expression were associated with COVID-19 disease severity. Mechanistically, TLR2 and Myd88 were required for β-coronavirus-induced inflammatory responses, and TLR2-dependent signaling induced the production of proinflammatory cytokines during coronavirus infection independent of viral entry. TLR2 sensed the SARS-CoV-2 envelope protein as its ligand. In addition, blocking TLR2 signaling in vivo provided protection against the pathogenesis of SARS-CoV-2 infection. Overall, our study provides a critical understanding of the molecular mechanism of β-coronavirus sensing and inflammatory cytokine production, which opens new avenues for therapeutic strategies to counteract the ongoing COVID-19 pandemic. The innate sensors of SARS-CoV-2 are still being determined. Kanneganti and colleagues find that SARS-CoV-2 envelope protein is sensed by TLR2 and this drives pathogenic inflammatory cytokine production.
Published: 2020

46. Synergism of TNF-α and IFN-γ triggers inflammatory cell death, tissue damage, and mortality in SARS-CoV-2 infection and cytokine shock syndromes

Author: Bhesh Raj Sharma, Shraddha Tuladhar, Patrick Schreiner, Rajendra Karki, Balaji Banoth, Richard Webby, Min Zheng, Parimal Samir, Balamurugan Sundaram, Colleen B. Jonsson, R. K. Subbarao Malireddi, Thirumala-Devi Kanneganti, Lillian Zalduondo, Evan P. Williams, Peter Vogel, and Geoffrey Neale
Subjects: Male, inflammatory cytokines, THP-1 Cells, medicine.medical_treatment, hemophagocytic lymphohistiocytosis (HLH), caspase-8, cytokine shock syndromes, sepsis, Mice, STAT1, 0302 clinical medicine, Medicine, FADD, IFN-γ, 0303 health sciences, Cell Death, biology, pyroptosis, gasdermin D, gasdermin E, apoptosis, Pyroptosis, iNOS, Cytokine release syndrome, Cytokine, cytokine storm, Female, Tumor necrosis factor alpha, medicine.symptom, Cytokine Release Syndrome, MLKL, Programmed cell death, RIPK1, caspase, Necroptosis, necroptosis, Mice, Transgenic, Inflammation, macrophage activation syndrome (MAS), RIPK3, Lymphohistiocytosis, Hemophagocytic, Article, General Biochemistry, Genetics and Molecular Biology, Proinflammatory cytokine, Interferon-gamma, 03 medical and health sciences, systemic inflammatory response syndrome (SIRS), nitric oxide, Human Umbilical Vein Endothelial Cells, Animals, Humans, PANoptosis, 030304 developmental biology, SARS-CoV-2, Tumor Necrosis Factor-alpha, business.industry, acute respiratory distress syndrome (ARDS), COVID-19, IRF1, medicine.disease, Antibodies, Neutralizing, Disease Models, Animal, TNF-α, Immunology, biology.protein, business, Cytokine storm, 030217 neurology & neurosurgery
Abstract: COVID-19 is characterized by excessive production of pro-inflammatory cytokines and acute lung damage associated with patient mortality. While multiple inflammatory cytokines are produced by innate immune cells during SARS-CoV-2 infection, we found that only the combination of TNF-α and IFN-γ induced inflammatory cell death characterized by pyroptosis, apoptosis, and necroptosis (PANoptosis). Mechanistically, TNF-α and IFN-γ co-treatment activated the JAK/STAT1/IRF1 axis, inducing nitric oxide production and driving caspase-8/FADD–mediated PANoptosis. TNF-α and IFN-γ caused a lethal cytokine shock in mice that mirrors the tissue damage and inflammation of COVID-19, and inhibiting PANoptosis protected mice from this pathology and death. Furthermore, treating with neutralizing antibodies against TNF-α and IFN-γ protected mice from mortality during SARS-CoV-2 infection, sepsis, hemophagocytic lymphohistiocytosis, and cytokine shock. Collectively, our findings suggest that blocking the cytokine-mediated inflammatory cell death signaling pathway identified here may benefit patients with COVID-19 or other infectious and autoinflammatory diseases by limiting tissue damage/inflammation., Highlights • Of several cytokines tested, only synergism of TNF-α and IFN-γ induces PANoptosis • TNF-α and IFN-γ–mediated PANoptosis perpetuates cytokine storm • TNF-α and IFN-γ shock mirrors cytokine storm syndromes, including COVID-19 • Neutralizing TNF-α and IFN-γ protects against SARS-CoV-2, HLH, and sepsis in mice
Published: 2020

47. A MyD88/IL1R Axis Regulates PD-1 Expression on Tumor-Associated Macrophages and Sustains Their Immunosuppressive Function in Melanoma

Author: Geoffrey Neale, Sarang Tartey, Thirumala-Devi Kanneganti, Peter Vogel, and R. K. Subbarao Malireddi
Subjects: 0301 basic medicine, Male, Cancer Research, Skin Neoplasms, Angiogenesis, medicine.medical_treatment, Programmed Cell Death 1 Receptor, Biology, Metastasis, 03 medical and health sciences, Mice, 0302 clinical medicine, Cell Line, Tumor, Tumor-Associated Macrophages, medicine, Immune Tolerance, Animals, Humans, Receptor, Melanoma, Tissue homeostasis, Mice, Knockout, Receptors, Interleukin-1, Immunotherapy, medicine.disease, Gene Expression Regulation, Neoplastic, Disease Models, Animal, 030104 developmental biology, Oncology, TRIF, Tumor progression, 030220 oncology & carcinogenesis, Myeloid Differentiation Factor 88, Cancer research, Disease Progression, Female, Signal Transduction
Abstract: Macrophages are critical mediators of tissue homeostasis, cell proliferation, and tumor metastasis. Tumor-associated macrophages (TAM) are generally associated with tumor-promoting immunosuppressive functions in solid tumors. Here, we examined the transcriptional landscape of adaptor molecules downstream of Toll-like receptors in human cancers and found that higher expression of MYD88 correlated with tumor progression. In murine melanoma, MyD88, but not Trif, was essential for tumor progression, angiogenesis, and maintaining the immunosuppressive phenotype of TAMs. In addition, MyD88 expression in myeloid cells drove melanoma progression. The MyD88/IL1 receptor (IL1R) axis regulated programmed cell death (PD)-1 expression on TAMs by promoting recruitment of NF-κBp65 to the Pdcd1 promoter. Furthermore, a combinatorial immunotherapy approach combining the MyD88 inhibitor with anti–PD-1 blockade elicited strong antitumor effects. Thus, the MyD88/IL1R axis maintains the immunosuppressive function of TAMs and promotes tumor growth by regulating PD-1 expression. Significance: These findings indicate that MyD88 regulates TAM-immunosuppressive activity, suggesting that macrophage-mediated immunotherapy combining MYD88 inhibitors with PD-1 blockade could result in better treatment outcomes in a wide variety of cancers.
Published: 2020

48. Metabolic regulation of pyroptotic cell death expands the therapeutic landscape for treating inflammatory disease

Author: Thirumala-Devi Kanneganti and David E. Place
Subjects: Lipopolysaccharides, Male, Cancer Research, Programmed cell death, Encephalomyelitis, Autoimmune, Experimental, Multiple Sclerosis, Biochemical Phenomena, Inflammasomes, Dimethyl Fumarate, Immunology, Citric Acid Cycle, lcsh:Medicine, Disease, Bioinformatics, Article, Mice, Genetics, Pyroptosis, Medicine, Animals, Humans, Cysteine, lcsh:QH301-705.5, Inflammation, business.industry, Drug discovery, Macrophages, lcsh:R, Caspase 1, Intracellular Signaling Peptides and Proteins, Macrophage Activation, Phosphate-Binding Proteins, Research Highlight, Mice, Mutant Strains, Familial Mediterranean Fever, Mice, Inbred C57BL, HEK293 Cells, Metabolic regulation, lcsh:Biology (General), Caspases, Female, business, Protein Processing, Post-Translational
Abstract: Activated macrophages undergo a metabolic switch to aerobic glycolysis, accumulating Krebs' cycle intermediates that alter transcription of immune response genes. We extended these observations by defining fumarate as an inhibitor of pyroptotic cell death. We found that dimethyl fumarate (DMF) delivered to cells or endogenous fumarate reacts with gasdermin D (GSDMD) at critical cysteine residues to form S-(2-succinyl)-cysteine. GSDMD succination prevents its interaction with caspases, limiting its processing, oligomerization, and capacity to induce cell death. In mice, the administration of DMF protects against lipopolysaccharide shock and alleviates familial Mediterranean fever and experimental autoimmune encephalitis by targeting GSDMD. Collectively, these findings identify GSDMD as a target of fumarate and reveal a mechanism of action for fumarate-based therapeutics that include DMF, for the treatment of multiple sclerosis.
Published: 2020

49. Coronaviruses: Innate Immunity, Inflammasome Activation, Inflammatory Cell Death, and Cytokines

Author: Rudragouda Channappanavar, SangJoon Lee, and Thirumala-Devi Kanneganti
Subjects: 0301 basic medicine, RNA virus, Inflammasomes, viruses, Immunology, Inflammation, Review, Biology, medicine.disease_cause, Virus, Inflammasome, Pathogenesis, MERS-CoV, 03 medical and health sciences, 0302 clinical medicine, MHV, medicine, Immunology and Allergy, Animals, Humans, PANoptosis, Coronavirus, Innate immunity, Innate immune system, Cell Death, SARS-CoV-2, virus diseases, COVID-19, SARS-CoV, PANoptosome, respiratory system, biochemical phenomena, metabolism, and nutrition, medicine.disease, Immunity, Innate, respiratory tract diseases, 030104 developmental biology, Middle East respiratory syndrome, Cytokines, Cytokine secretion, medicine.symptom, 030215 immunology, medicine.drug
Abstract: The innate immune system acts as the first line of defense against pathogens, including coronaviruses. SARS-CoV and MERS-CoV are epidemic zoonotic coronaviruses that emerged at the beginning of the 21st century. The recently emerged virus SARS-CoV-2 is a novel strain of coronavirus that has caused the COVID-19 pandemic. Scientific advancements made by studying the SARS-CoV and MERS-CoV outbreaks have provided a foundation for understanding pathogenesis and innate immunity against SARS-CoV-2. In this review, we focus on our present understanding of innate immune responses, inflammasome activation, inflammatory cell death pathways, and cytokine secretion during SARS-CoV, MERS-CoV, and SARS-CoV-2 infection. We also discuss how the pathogenesis of these viruses influences these biological processes., HIGHLIGHTS • TLR- and RLR-mediated type I IFN production is essential for providing protection against CoV infection; the timing of the IFN response relative to CoV replication determines infection outcomes. • Optimal NLRP3 inflammasome activation is beneficial for the host but aberrant activation may lead to detrimental CoV infection outcomes. • Specific CoV infections can activate inflammatory cell death (PANoptosis), thereby inducing cytokine release. • CoV disease tolerance occurs in age-, species-, and sex-dependent manners. • More studies are needed to define the innate immune response, specifically during SARS-CoV-2 infection, and to inform the development of candidate therapeutics.
Published: 2020

50. Advances in Inflammasome Research: Recent Breakthroughs and Future Hurdles

Author: Rebecca E. Tweedell and Thirumala-Devi Kanneganti
Subjects: 0301 basic medicine, Inflammasomes, Necroptosis, Apoptosis, NLR Proteins, Biology, Article, Proinflammatory cytokine, 03 medical and health sciences, AIM2, 0302 clinical medicine, NLRC4, medicine, Pyroptosis, Animals, Humans, Molecular Biology, Research, Inflammasome, Cell biology, 030104 developmental biology, Molecular Medicine, Cytokines, Inflammation Mediators, 030217 neurology & neurosurgery, Biomarkers, medicine.drug
Abstract: Inflammasomes are a group of cytosolic multiprotein complexes that are assembled in response to pathogen- and damage-associated molecular patterns and cellular stress. Inflammasome assembly drives the maturation and secretion of proinflammatory cytokines and induces pyroptosis. Here, we will highlight some key advancements in inflammasome research with therapeutic potential.
Published: 2020

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