Author: "Kanneganti A" / Topic: biology - Searchworks@Jio Institute Digital Library Search Results

309 results on '"Kanneganti A"'

1. 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

2. Fostering experimental and computational synergy to modulate hyperinflammation

Author: Ilya Potapov, Thirumala-Devi Kanneganti, and Antonio del Sol
Subjects: Chemokine, biology, SARS-CoV-2, business.industry, Immunology, COVID-19, medicine.disease, Proinflammatory cytokine, Organ damage, medicine, biology.protein, Cytokines, Humans, Immunology and Allergy, Cytokine Release Syndrome, Cytokine storm, business
Abstract: The molecular underpinnings of the uncontrolled release of proinflammatory cytokines and chemokines ('cytokine storm'), which can cause organ damage and even mortality, are not completely understood. Furthermore, targeted therapeutic options to dampen such hyperinflammation are scarce. Here, we highlight the ways in which technological advances have set the stage for a new age of synergy between experimental and computational researchers to guide the discovery of novel therapeutic targets for modulating hyperinflammation.
Published: 2022

3. 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

4. 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

5. From pyroptosis, apoptosis and necroptosis to PANoptosis: A mechanistic compendium of programmed cell death pathways

Author: Yaqiu Wang and Thirumala-Devi Kanneganti
Subjects: Cell death, Programmed cell death, Necroptosis, Biophysics, Caspase 1, Apoptosis, Review, Biology, Caspase 8, RIPK3, ASC, Biochemistry, Caspase 7, Inflammasome, NLRP3, Structural Biology, Genetics, medicine, Pyroptosis, PANoptosis, ComputingMethodologies_COMPUTERGRAPHICS, ZBP1, PANoptosome, Gasdermin E, Computer Science Applications, Gasdermin D, Crosstalk (biology), Caspase-3, Caspase-1, Caspase-8, Neuroscience, TP248.13-248.65, medicine.drug, Biotechnology, Caspase-7, MLKL
Abstract: Graphical abstract, Pyroptosis, apoptosis and necroptosis are the most genetically well-defined programmed cell death (PCD) pathways, and they are intricately involved in both homeostasis and disease. Although the identification of key initiators, effectors and executioners in each of these three PCD pathways has historically delineated them as distinct, growing evidence has highlighted extensive crosstalk among them. These observations have led to the establishment 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 PCD pathways alone. In this review, we provide a brief overview of the research history of pyroptosis, apoptosis and necroptosis. We then examine the intricate crosstalk among these PCD pathways to discuss the current evidence for PANoptosis. We also detail the molecular evidence for the assembly of the PANoptosome complex, a molecular scaffold for contemporaneous engagement of key molecules from pyroptosis, apoptosis, and/or necroptosis. PANoptosis is now known to be critically involved in many diseases, including infection, sterile inflammation and cancer, and future discovery of novel PANoptotic components will continue to broaden our understanding of the fundamental processes of cell death and inform the development of new therapeutics.
Published: 2021

6. Rising to the challenge of COVID-19: Working on SARS-CoV-2 during the pandemic

Author: Zhiyong Lou, Noam Stern-Ginossar, Sara Cherry, Craig E. Cameron, Thirumala-Devi Kanneganti, Jonathan Abraham, and Laura Martin-Sancho
Subjects: Teamwork, 2019-20 coronavirus outbreak, Biomedical Research, Coronavirus disease 2019 (COVID-19), business.industry, SARS-CoV-2, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), media_common.quotation_subject, Poetry as Topic, COVID-19, Cell Biology, Biology, Public relations, Voices, Pandemic, Quarantine, Humans, business, Molecular Biology, Pandemics, media_common
Abstract: COVID-19 altered our lives and pushed scientific research to operate at breakneck speed, leading to significant breakthroughs in record time. We asked experts in the field about the challenges they faced in transitioning, rapidly but safely, to working on the virus while navigating the shutdown. Their voices converge on the importance of teamwork, forging new collaborations, and working toward a shared goal.
Published: 2021

7. PANoptosis in microbial infection

Author: David E. Place, SangJoon Lee, and Thirumala-Devi Kanneganti
Subjects: Microbiology (medical), Programmed cell death, Necroptosis, Apoptosis, Biology, Bacterial Physiological Phenomena, Infections, Microbiology, Article, Proinflammatory cytokine, 03 medical and health sciences, Immune system, Pyroptosis, 030304 developmental biology, 0303 health sciences, Innate immune system, Cell Death, 030306 microbiology, Fungi, Pattern recognition receptor, Biological Evolution, Infectious Diseases, Cell Death Process, Host-Pathogen Interactions, Immunology, Virus Physiological Phenomena
Abstract: Highlights • Cells exposed to TLR ligands and cytokines during infection activate PANoptosis. • RIPK1-dependent PANoptosome is formed when cell survival signaling is inhibited. • Influenza A virus Z-RNAs bind and activate ZBP1, promoting PANoptosome formation., The immune system has evolved multiple mechanisms to restrict microbial infections and regulate inflammatory responses. Without appropriate regulation, infection-induced inflammatory pathology can be deadly. The innate immune system recognizes the microbial molecules conserved in many pathogens and engages a rapid response by producing inflammatory mediators and activating programmed cell death pathways, including pyroptosis, apoptosis, and necroptosis. Activation of pattern recognition receptors, in combination with inflammatory cytokine-induced signaling through death domain-containing receptors, initiates a highly interconnected cell death process called PANoptosis (pyroptosis, apoptosis, necroptosis). Broadly speaking, PANoptosis is critical for restricting a wide range of pathogens (including bacteria, viruses, fungi, and parasites), which we describe in this review. We propose that re-examining the role of cell death and inflammatory cytokines through the lens of PANoptosis will advance our understanding of host–pathogen evolution and may reveal new treatment strategies for controlling a wide range of infectious diseases.
Published: 2021

8. RIPK3 Promotes Mefv Expression and Pyrin Inflammasome Activation via Modulation of mTOR Signaling

Author: Arjun Balakrishnan, Thirumala-Devi Kanneganti, Ankit Malik, R. K. Subbarao Malireddi, and Deepika Sharma
Subjects: biology, Chemistry, Necroptosis, Immunology, Familial Mediterranean fever, Inflammasome, medicine.disease, MEFV, Pyrin domain, Cell biology, 03 medical and health sciences, 0302 clinical medicine, medicine, biology.protein, Immunology and Allergy, Inflammasome complex, Mechanistic target of rapamycin, PI3K/AKT/mTOR pathway, 030215 immunology, medicine.drug
Abstract: Mutations in MEFV, the gene encoding pyrin in humans, are associated with the autoinflammatory disorder familial Mediterranean fever. Pyrin is an innate sensor that assembles into an inflammasome complex in response to Rho-modifying toxins, including Clostridium difficile toxins A and B. Cell death pathways have been shown to intersect with and modulate inflammasome activation, thereby affecting host defense. Using bone marrow–derived macrophages and a murine model of peritonitis, we show in this study that receptor-interacting protein kinase (RIPK) 3 impacts pyrin inflammasome activation independent of its role in necroptosis. RIPK3 was instead required for transcriptional upregulation of Mefv through negative control of the mechanistic target of rapamycin (mTOR) pathway and independent of alterations in MAPK and NF-κB signaling. RIPK3 did not affect pyrin dephosphorylation associated with inflammasome activation. We further demonstrate that inhibition of mTOR was sufficient to promote Mefv expression and pyrin inflammasome activation, highlighting the cross-talk between the mTOR pathway and regulation of the pyrin inflammasome. Our study reveals a novel interaction between molecules involved in cell death and the mTOR pathway to regulate the pyrin inflammasome, which can be harnessed for therapeutic interventions.
Published: 2020

9. Impaired NLRP3 inflammasome activation/pyroptosis leads to robust inflammatory cell death via caspase-8/RIPK3 during coronavirus infection

Author: R. K. Subbarao Malireddi, Rudragouda Channappanavar, Richard J. Webby, Evan P. Williams, Rajendra Karki, Balaji Banoth, Thirumala-Devi Kanneganti, Amanda R. Burton, Min Zheng, and Colleen B. Jonsson
Subjects: 0301 basic medicine, Programmed cell death, 030102 biochemistry & molecular biology, viruses, Necroptosis, Pyroptosis, Caspase 1, Inflammasome, Cell Biology, Biology, medicine.disease_cause, Caspase 8, Biochemistry, 03 medical and health sciences, 030104 developmental biology, Apoptosis, Immunology, medicine, Molecular Biology, medicine.drug, Coronavirus
Abstract: Coronaviruses have caused several zoonotic infections in the past two decades, leading to significant morbidity and mortality globally. Balanced regulation of cell death and inflammatory immune responses is essential to promote protection against coronavirus infection; however, the underlying mechanisms that control these processes remain to be resolved. Here we demonstrate that infection with the murine coronavirus mouse hepatitis virus (MHV) activated the NLRP3 inflammasome and inflammatory cell death in the form of PANoptosis. Deleting NLRP3 inflammasome components or the downstream cell death executioner gasdermin D (GSDMD) led to an initial reduction in cell death followed by a robust increase in the incidence of caspase-8- and receptor-interacting serine/threonine-protein kinase 3 (RIPK3)-mediated inflammatory cell deathafter coronavirus infection. Additionally, loss of GSDMD promoted robust NLRP3 inflammasome activation. Moreover, the amounts of some cytokines released during coronavirus infection were significantly altered in the absence of GSDMD. Altogether, our findings show that inflammatory cell death, PANoptosis, is induced by coronavirus infection and that impaired NLRP3 inflammasome function or pyroptosis can lead to negative consequences for the host. These findings may have important implications for studies of coronavirus-induced disease.
Published: 2020

10. 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

11. Intracellular innate immune receptors: Life inside the cell

Author: Thirumala-Devi Kanneganti
Subjects: medicine.anatomical_structure, Innate immune system, Immunology, Cell, medicine, Immunology and Allergy, Receptors, Immunologic, Biology, Receptor, Article, Immunity, Innate, Intracellular, Cell biology
Published: 2020

12. The regulation of the ZBP1‐NLRP3 inflammasome and its implications in pyroptosis, apoptosis, and necroptosis (PANoptosis)

Author: Min Zheng and Thirumala-Devi Kanneganti
Subjects: 0301 basic medicine, Programmed cell death, Inflammasomes, Necroptosis, Immunology, Apoptosis, Biology, medicine.disease_cause, Article, 03 medical and health sciences, 0302 clinical medicine, NLR Family, Pyrin Domain-Containing 3 Protein, Pyroptosis, medicine, Influenza A virus, Immunology and Allergy, Innate immune system, integumentary system, RNA-Binding Proteins, Inflammasome, Cell biology, Crosstalk (biology), 030104 developmental biology, Type I interferon signaling pathway, 030215 immunology, medicine.drug
Abstract: ZBP1 has been characterized as a critical innate immune sensor of not only viral RNA products but also endogenous nucleic acid ligands. ZBP1 sensing of the Z-RNA produced during influenza virus infection induces cell death in the form of pyroptosis, apoptosis, and necroptosis (PANoptosis). PANoptosis is a coordinated cell death pathway that is driven through a multiprotein complex called the PANoptosome and enables crosstalk and co-regulation among these processes. During influenza virus infection, a key step in PANoptosis and PANoptosome assembly is the formation of the ZBP1-NLRP3 inflammasome. When Z-RNA is sensed, ZBP1 recruits RIPK3 and caspase-8 to activate the ZBP1-NLRP3 inflammasome. Several other host factors have been found to be important for ZBP1-NLRP3 inflammasome assembly, including molecules involved in the type I interferon signaling pathway and caspase-6. Additionally, influenza viral proteins, such as M2, NS1, and PB1-F2, have also been shown to regulate the ZBP1-NLRP3 inflammasome. This review explains the functions of ZBP1 and the mechanistic details underlying the activation of the ZBP1-NLRP3 inflammasome and the formation of the PANoptosome. Improved understanding of the ZBP1-NLRP3 inflammasome will direct the development of therapeutic strategies to target infectious and inflammatory diseases.
Published: 2020

13. 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

14. Pedagogy in a pandemic – COVID‐19 and virtual continuing medical education (vCME) in obstetrics and gynecology

Author: Grace Ming Fen Chan, Ida Ismail-Pratt, Soe Na Choo, Mahesh Choolani, Susan Logan, Karen M.X. Lim, and Abhiram Kanneganti
Subjects: medicine.medical_specialty, Coronavirus disease 2019 (COVID-19), Pneumonia, Viral, MEDLINE, Special Editorial, Education, Distance, Betacoronavirus, Continuing medical education, Obstetrics and gynaecology, Obstetrics and Gynaecology, Pandemic, medicine, Humans, Pandemics, biology, SARS-CoV-2, Viral Epidemiology, business.industry, COVID-19, Obstetrics and Gynecology, General Medicine, biology.organism_classification, medicine.disease, Obstetrics, Pneumonia, Gynecology, Family medicine, Education, Medical, Continuing, Coronavirus Infections, business
Published: 2020

15. 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

16. 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

17. Decoding the vital segments in human ATP-dependent RNA helicase

Author: Vandana Kamjula, Ashish Runthala, Sudarshan Idupulapati, Kusuma Nidamanuri, Ananya Kanneganti, and Rohan Metla
Subjects: InterPro, 0303 health sciences, RNA helicase, biology, motif, 030302 biochemistry & molecular biology, MODELLER, Active site, Helicase, General Medicine, Computational biology, RNA Helicase A, Conserved sequence, flexibility, 03 medical and health sciences, Hydrolase, biology.protein, Research-Article, UniProt, innate immunity, 030304 developmental biology
Abstract: An analysis of the ATP-dependent RNA helicase using known functionally close analogs helps disclose the structural and functional information of the enzyme. The enzyme plays several interlinked biological functions and there is an urgent need to interpret its key active-site residues to infer function and establish role. The human protein q96c10.1 is annotated using tools such as interpro, go and cdd. The physicochemical properties are estimated using the tool protparam. We describe the enzyme protein model developed using modeller to identify active site residues. We used consurf to estimate the structural conservation and is evolutionary relationship is inferred using known close sequence homologs. The active site is predicted using castp and its topological flexibility is estimated through cabs-flex. The protein is annotated as a hydrolase using available data and ddx58 is found as its top-ranked interacting protein partner. We show that about 124 residues are found to be highly conserved among 259 homologs, clustered in 7 clades with the active-site showing low sequence conservation. It is further shown that only 9 loci among the 42 active-site residues are conserved with limited structural fluctuation from the wild type structure. Thus, we document various useful information linked to function, sequence similarity and phylogeny of the enzyme for annotation as potential helicase as designated by uniprot. Data shows limited degree of conserved sequence segments with topological flexibility unlike in other subfamily members of the protein.
Published: 2020

18. 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

19. 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

20. Fungal cell wall components modulate our immune system

Author: Nicolas Papon, Benoit Briard, Thierry Fontaine, Neil A. R. Gow, Thirumala-Devi Kanneganti, Centre d’Etude des Pathologies Respiratoires (CEPR), UMR 1100 (CEPR), Université de Tours-Institut National de la Santé et de la Recherche Médicale (INSERM), Biologie et Pathogénicité fongiques, Institut Pasteur [Paris]-Institut National de la Recherche Agronomique (INRA), St Jude Children's Research Hospital, University of Aberdeen, University of Exeter, Groupe d'Étude des Interactions Hôte-Pathogène (GEIHP), Université d'Angers (UA), Université de Brest (UBO), NG acknowledges welcome support of a Senior Investigator (101873/Z/13/Z), Collaborative (200208/A/15/Z, 215599/Z/19/Z) and Strategic Awards (097377/Z11/Z) and the MRC Centre for Medical Mycology [MR/N006364/2]., Université de Tours (UT)-Institut National de la Santé et de la Recherche Médicale (INSERM), Biologie et Pathogénicité fongiques - Fungal Biology and Pathogenicity (BPF), Institut Pasteur [Paris] (IP)-Université Paris Cité (UPCité)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), SFR UA 4208 Interactions Cellulaires et Applications Thérapeutiques (ICAT), and Fontaine, Thierry
Subjects: Host immunity, Cell death, [SDV]Life Sciences [q-bio], Galactosaminogalactan, Trained immunity, Biology, Skin infection, [SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity, Applied Microbiology and Biotechnology, Microbiology, Article, Inflammasome, Cell wall, 03 medical and health sciences, chemistry.chemical_compound, Immune system, Polysaccharides, Melanin, medicine, Pyroptosis, PANoptosis, [SDV.IMM.II] Life Sciences [q-bio]/Immunology/Innate immunity, Molecular Biology, ComputingMilieux_MISCELLANEOUS, 030304 developmental biology, Innate immunity, 0303 health sciences, Immunometabolism, Innate immune system, QH573-671, 030306 microbiology, Cell Biology, medicine.disease, 3. Good health, chemistry, Immunology, Cytology, medicine.drug
Abstract: International audience; Invasive fungal infections remain highly problematic for human health. Collectively, they account for more than 1 million deaths a year in addition to more than 100 million mucosal infections and 1 billion skin infections. To be able to make progress it is important to understand the pathobiology of fungal interactions with the immune system. Here, we highlight new advancements pointing out the pivotal role of fungal cell wall components (β-glucan, mannan, galactosaminogalactan and melanin) in modulating host immunity and discuss how these open new opportunities for the development of immunomodulatory strategies to combat deadly fungal infectious diseases.
Published: 2021

21. Sepsis take-out: Inhibiting bacterial deliveries

Author: Shelbi Christgen and Thirumala-Devi Kanneganti
Subjects: Lipopolysaccharides, 0301 basic medicine, Immunology, chemical and pharmacologic phenomena, Disease, Bioinformatics, HMGB1, Sepsis, 03 medical and health sciences, 0302 clinical medicine, Immunity, medicine, Humans, Immunology and Allergy, HMGB1 Protein, biology, Cytosolic delivery, Treatment options, Heparin, medicine.disease, 030104 developmental biology, Infectious Diseases, 030220 oncology & carcinogenesis, biology.protein, Gram-Negative Bacterial Infections, Signal Transduction, medicine.drug
Abstract: Summary Sepsis remains a deadly disease with limited treatment options. In this issue of Immunity, Tang et al. propose that heparin provides protection during gram-negative sepsis by dampening harmful CASP11-dependent signaling through inhibition of HMGB1- and heparanase-mediated cytosolic delivery of LPS.
Published: 2021

22. Pathogen's dynamic standoff with the host

Author: Wolf-Dietrich Hardt and Thirumala-Devi Kanneganti
Subjects: Microbiology (medical), Host (biology), Bacterial Infections, Biology, Bacterial Physiological Phenomena, Microbiology, Immunity, Innate, Article, Infectious Diseases, Virus Diseases, Host-Pathogen Interactions, Humans, Pathogen, Virus Physiological Phenomena
Published: 2021

23. 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, 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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, 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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, 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Anna, Hernández, Agustín, Hernandez, Carlos, Hernandez-Diaz, Sergio, Hernandez-Gea, Virginia, Herpin, Amaury, Herreros, Judit, Hervás, Javier, Hesselson, Daniel, Hetz, Claudio, Heussler, Volker, Higuchi, Yujiro, Hilfiker, Sabine, Hill, Joseph, Hlavacek, William, Ho, Emmanuel, Ho, Idy, Ho, Philip Wing-Lok, Ho, Shu-Leong, Ho, Wan Yun, Hobbs, G Aaron, Hochstrasser, Mark, Hoet, Peter, Hofius, Daniel, Hofman, Paul, Höhn, Annika, Holmberg, Carina, Hombrebueno, Jose, Yi-Ren Hong, Chang-Won Hong, Hooper, Lora, Hoppe, Thorsten, Horos, Rastislav, Hoshida, Yujin, Hsin, I-Lun, Hsu, Hsin-Yun, Hu, Bing, Hu, Dong, Hu, Li-Fang, Hu, Ming Chang, Hu, Ronggui, Hu, Wei, Hu, Yu-Chen, Hu, Zhuo-Wei, Hua, Fang, Hua, Jinlian, Hua, Yingqi, Huan, Chongmin, Huang, Canhua, Huang, Chuanshu, Huang, Chuanxin, Huang, Chunling, Huang, Haishan, Huang, Kun, Huang, Michael, Huang, Rui, Huang, Shan, Huang, Tianzhi, Huang, Xing, Huang, Yuxiang Jack, Huber, Tobias, Hubert, Virginie, Hubner, Christian, Hughes, Stephanie, 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Chengyu, Liang, Qiangrong, Liang, Weicheng, Liang, Yongheng, Liang, YongTian, Liao, Guanghong, Liao, Lujian, Liao, Mingzhi, Liao, Yung-Feng, Librizzi, Mariangela, Lie, Pearl, Lilly, Mary, Lim, Hyunjung, Lima, Thania, Limana, Federica, Lin, Chao, Lin, Chih-Wen, Lin, Dar-Shong, Lin, Fu-Cheng, Lin, Jiandie, Lin, Kurt, Lin, Kwang-Huei, Lin, Liang-Tzung, LIN, Pei-Hui, Lin, Qiong, Lin, Shaofeng, Lin, Su-Ju, Lin, Wenyu, Lin, Xueying, Lin, Yao-Xin, Lin, Yee-Shin, Linden, Rafael, Lindner, Paula, Ling, Shuo-Chien, Lingor, Paul, Linnemann, Amelia, Liou, Yih-Cherng, Lipinski, Marta, Lipovšek, Saška, Lira, Vitor, Lisiak, Natalia, Liton, Paloma, Liu, Chao, Liu, Ching-Hsuan, Liu, Chun-Feng, Liu, Cui Hua, Liu, Fang, Liu, Hao, Liu, Hsiao-Sheng, Liu, Hua-feng, Liu, Huifang, Liu, Jia, Liu, Jing, Liu, Julia, Liu, Leyuan, Liu, Longhua, Liu, Meilian, Liu, Qin, Liu, Wei, Liu, Wende, Liu, Xiao-Hong, Liu, Xiaodong, Liu, Xingguo, Liu, Xu, Liu, Xuedong, Liu, Yanfen, Liu, Yang, Liu, Yueyang, Liu, Yule, 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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. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., Adamopoulos, I. E., Adeli, K., Adolph, T. E., Adornetto, A., Aflaki, E., Agam, G., Agarwal, A., Aggarwal, B. B., Agnello, M., Agostinis, P., Agrewala, J. N., Agrotis, A., Aguilar, P. V., Ahmad, S. T., Ahmed, Z. M., Ahumada-Castro, U., Aits, S., Aizawa, S., Akkoc, Y., Akoumianaki, T., Akpinar, H. A., Al-Abd, A. M., Al-Akra, L., Al-Gharaibeh, A., Alaoui-Jamali, M. A., Alberti, S., Alcocer-Gomez, E., Alessandri, C., Ali, M., Alim Al-Bari, M. A., Aliwaini, S., Alizadeh, J., Almacellas, E., Almasan, A., Alonso, A., Alonso, G. D., Altan-Bonnet, N., Altieri, D. C., Alvarez, E. M. C., Alves, S., Alves da Costa, C., Alzaharna, M. M., Amadio, M., Amantini, C., Amaral, C., Ambrosio, S., Amer, A. O., Ammanathan, V., An, Z., Andersen, S. U., Andrabi, S. A., Andrade-Silva, M., Andres, A. M., Angelini, S., Ann, D., Anozie, U. C., Ansari, M. 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T., Balduini, W., Ballabio, A., Ballester, M., Balazadeh, S., Balzan, R., Bandopadhyay, R., Banerjee, S., Banreti, A., Bao, Y., Baptista, M. S., Baracca, A., Barbati, C., Bargiela, A., Barila, D., Barlow, P. G., Barmada, S. J., Barreiro, E., Barreto, G. E., Bartek, J., Bartel, B., Bartolome, A., Barve, G. R., Basagoudanavar, S. H., Bassham, D. C., Bast, R. C., Basu, A., Batoko, H., Batten, I., Baulieu, E. E., Baumgarner, B. L., Bayry, J., Beale, R., Beau, I., Beaumatin, F., Bechara, L. R. G., Beck, G. R., Beers, M. F., Begun, J., Behrends, C., Behrens, G. M. N., Bei, R., Bejarano, E., Bel, S., Behl, C., Belaid, A., Belgareh-Touze, N., Bellarosa, C., Belleudi, F., Bello Perez, M., Bello-Morales, R., Beltran, J. S. D. O., Beltran, S., Benbrook, D. M., Bendorius, M., Benitez, B. A., Benito-Cuesta, I., Bensalem, J., Berchtold, M. W., Berezowska, S., Bergamaschi, D., Bergami, M., Bergmann, A., Berliocchi, L., Berlioz-Torrent, C., Bernard, A., Berthoux, L., Besirli, C. 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K., Shutt, T. E., Sica, V., Siddiqui, A., Sierra, A., Sierra-Torre, V., Signorelli, S., Sil, P., Silva, B. J. D. A., Silva, J. D., Silva-Pavez, E., Silvente-Poirot, S., Simmonds, R. E., Simon, A. K., Simon, H. -U., Simons, M., Singh, A., Singh, L. P., Singh, R., Singh, S. V., Singh, S. K., Singh, S. B., Singh, S., Singh, S. P., Sinha, D., Sinha, R. A., Sinha, S., Sirko, A., Sirohi, K., Sivridis, E. L., Skendros, P., Skirycz, A., Slaninova, I., Smaili, S. S., Smertenko, A., Smith, M. D., Soenen, S. J., Sohn, E. J., Sok, S. P. M., Solaini, G., Soldati, T., Soleimanpour, S. A., Soler, R. M., Solovchenko, A., Somarelli, J. A., Sonawane, A., Song, F., Song, H. K., Song, J. -X., Song, K., Song, Z., Soria, L. R., Sorice, M., Soukas, A. A., Soukup, S. -F., Sousa, D., Sousa, N., Spagnuolo, P. A., Spector, S. A., Srinivas Bharath, M. M., S, t. Clair D., Stagni, V., Staiano, L., Stalnecker, C. A., Stankov, M. V., Stathopulos, P. B., Stefan, K., Stefan, S. M., Stefanis, L., Steffan, J. S., Steinkasserer, A., Stenmark, H., Sterneckert, J., Stevens, C., Stoka, V., Storch, S., Stork, B., Strappazzon, F., Strohecker, A. M., Stupack, D. G., Su, H., Su, L. -Y., Su, L., Suarez-Fontes, A. M., Subauste, C. S., Subbian, S., Subirada, P. V., Sudhandiran, G., Sue, C. M., Sui, X., Summers, C., Sun, G., Sun, J., Sun, K., Sun, M. -X., Sun, Q., Sun, Y., Sun, Z., Sunahara, K. K. S., Sundberg, E., Susztak, K., Sutovsky, P., Suzuki, H., Sweeney, G., Symons, J. D., Sze, S. C. W., Szewczyk, N. J., Tabecka-Lonczynska, A., Tabolacci, C., Tacke, F., Taegtmeyer, H., Tafani, M., Tagaya, M., Tai, H., Tait, S. W. G., Takahashi, Y., Takats, S., Talwar, P., Tam, C., Tam, S. Y., Tampellini, D., Tamura, A., Tan, C. T., Tan, E. -K., Tan, Y. -Q., Tanaka, M., Tang, D., Tang, J., Tang, T. -S., Tanida, I., Tao, Z., Taouis, M., Tatenhorst, L., Tavernarakis, N., Taylor, A., Taylor, G. A., Taylor, J. M., Tchetina, E., Tee, A. R., Tegeder, I., Teis, D., Teixeira, N., Teixeira-Clerc, F., Tekirdag, K. A., Tencomnao, T., Tenreiro, S., Tepikin, A. V., Testillano, P. S., Tettamanti, G., Tharaux, P. -L., Thedieck, K., Thekkinghat, A. A., Thellung, S., Thinwa, J. W., Thirumalaikumar, V. P., Thomas, S. M., Thomes, P. G., Thorburn, A., Thukral, L., Thum, T., Thumm, M., Tian, L., Tichy, A., Till, A., Timmerman, V., Titorenko, V. I., Todi, S. V., Todorova, K., Toivonen, J. M., Tomaipitinca, L., Tomar, D., Tomas-Zapico, C., Tomic, S., Tong, B. C. -K., Tong, C., Tong, X., Tooze, S. A., Torgersen, M. L., Torii, S., Torres-Lopez, L., Torriglia, A., Towers, C. G., Towns, R., Toyokuni, S., Trajkovic, V., Tramontano, D., Tran, Q. -G., Travassos, L. H., Trelford, C. B., Tremel, S., Trougakos, I. P., Tsao, B. P., Tschan, M. P., Tse, H. -F., Tse, T. F., Tsugawa, H., Tsvetkov, A. S., Tumbarello, D. A., Tumtas, Y., Tunon, M. J., Turcotte, S., Turk, B., Turk, V., Turner, B. J., Tuxworth, R. I., Tyler, J. K., Tyutereva, E. V., Uchiyama, Y., Ugun-Klusek, A., Uhlig, H. H., Ulamek-Koziol, M., Ulasov, I. V., Umekawa, M., Ungermann, C., Unno, R., Urbe, S., Uribe-Carretero, E., Ustun, S., Uversky, V. N., Vaccari, T., Vaccaro, M. I., Vahsen, B. F., Vakifahmetoglu-Norberg, H., Valdor, R., Valente, M. J., Valko, A., Vallee, R. B., Valverde, A. M., Van den Berghe, G., van der Veen, S., Van Kaer, L., van Loosdregt, J., van Wijk, S. J. L., Vandenberghe, W., Vanhorebeek, I., Vannier-Santos, M. A., Vannini, N., Vanrell, M. C., Vantaggiato, C., Varano, G., Varela-Nieto, I., Varga, M., Vasconcelos, M. H., Vats, S., Vavvas, D. G., Vega-Naredo, I., Vega-Rubin-de-Celis, S., Velasco, G., Velazquez, A. P., Vellai, T., Vellenga, E., Velotti, F., Verdier, M., Verginis, P., Vergne, I., Verkade, P., Verma, M., Verstreken, P., Vervliet, T., Vervoorts, J., Vessoni, A. T., Victor, V. M., Vidal, M., Vidoni, C., Vieira, O. V., Vierstra, R. D., Vigano, S., Vihinen, H., Vijayan, V., Vila, M., Vilar, M., Villalba, J. 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. P., Whitton, J. L., Whitworth, A. J., Wiktorska, K., Wildenberg, M. E., Wileman, T., Wilkinson, S., Willbold, D., Williams, B., Williams, R. S. B., Williams, R. L., Williamson, P. R., Wilson, R. A., Winner, B., Winsor, N. J., Witkin, S. S., Wodrich, H., Woehlbier, U., Wollert, T., Wong, E., Wong, J. H., Wong, R. W., Wong, V. K. W., Wong, W. W. -L., Wu, A. -G., Wu, C., Wu, J., Wu, K. K., Wu, M., Wu, S. -Y., Wu, S., Wu, W. K. K., Wu, X., Wu, Y. -W., Wu, Y., Xavier, R. J., Xia, H., Xia, L., Xia, Z., Xiang, G., Xiang, J., Xiang, M., Xiang, W., Xiao, B., Xiao, G., Xiao, H., Xiao, H. -T., Xiao, J., Xiao, L., Xiao, S., Xiao, Y., Xie, B., Xie, C. -M., Xie, M., Xie, Y., Xie, Z., Xilouri, M., Xu, C., Xu, E., Xu, H., Xu, J., Xu, L., Xu, W. W., Xu, X., Xue, Y., Yakhine-Diop, S. M. 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

24. 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

25. 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

26. 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

27. 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

28. 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

29. 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

30. CovidExpress: an interactive portal for intuitive investigation on SARS-CoV-2 related transcriptomes

Author: Yawei Hui, Hongjian Jin, Dale Hedges, Wojciech Rosikiewicz, Patrick Schreiner, Beisi Xu, Mohamed Nadhir Djekidel, Thirumala-Devi Kanneganti, Gang Wu, Yiping Fan, and Jamy C. Peng
Subjects: GSEA, Coronavirus disease 2019 (COVID-19), SARS-CoV-2, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), viruses, MEDLINE, COVID-19, drug, RNA-Seq, Computational biology, Disease, Biology, Article, Data sharing, Transcriptome, portal, Pandemic, expression, visualization
Abstract: Infection with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in humans could cause coronavirus disease 2019 (COVID-19). Since its first discovery in Dec 2019, SARS-CoV-2 has become a global pandemic and caused 3.3 million direct/indirect deaths (2021 May). Amongst the scientific community’s response to COVID-19, data sharing has emerged as an essential aspect of the combat against SARS-CoV-2. Despite the ever-growing studies about SARS-CoV-2 and COVID-19, to date, only a few databases were curated to enable access to gene expression data. Furthermore, these databases curated only a small set of data and do not provide easy access for investigators without computational skills to perform analyses. To fill this gap and advance open-access to the growing gene expression data on this deadly virus, we collected about 1,500 human bulk RNA-seq datasets from publicly available resources, developed a database and visualization tool, named CovidExpress (https://stjudecab.github.io/covidexpress). This open access database will allow research investigators to examine the gene expression in various tissues, cell lines, and their response to SARS-CoV-2 under different experimental conditions, accelerating the understanding of the etiology of this disease to inform the drug and vaccine development. Our integrative analysis of this big dataset highlights a set of commonly regulated genes in SARS-CoV-2 infected lung and Rhinovirus infected nasal tissues, including OASL that were under-studied in COVID-19 related reports. Our results also suggested a potential FURIN positive feedback loop that might explain the evolutional advantage of SARS-CoV-2.
Published: 2021

31. Targeting Apoptosis Inhibition to Activate Antitumor Immunity

Author: Thirumala-Devi Kanneganti and Sannula Kesavardhana
Subjects: 0301 basic medicine, biology, Antitumor immunity, business.industry, Extramural, Immunology, medicine.disease, Article, 03 medical and health sciences, 030104 developmental biology, 0302 clinical medicine, Breast cancer, Apoptosis, Cancer research, medicine, biology.protein, Immunology and Allergy, Apoptosis Inhibition, Cytotoxicity, business, Caspase, Original Research, 030215 immunology
Abstract: Caspase 3 (CASP3) has a key role in the execution of apoptosis, and many cancer cells are believed to disable CASP3 as a mechanism of resistance to cytotoxic therapeutics. Alongside, CASP3 regulates stress-responsive immunomodulatory pathways, including secretion of type I interferon (IFN). Here, we report that mouse mammary carcinoma TSA cells lacking Casp3 or subjected to chemical caspase inhibition were as sensitive to the cytostatic and cytotoxic effects of radiation therapy (RT) in vitro as their control counterparts, yet secreted increased levels of type I IFN. This effect originated from the accrued accumulation of irradiated cells with cytosolic DNA, likely reflecting the delayed breakdown of cells experiencing mitochondrial permeabilization in the absence of CASP3. Casp3(-/-) TSA cells growing in immunocompetent syngeneic mice were more sensitive to RT than their CASP3-proficient counterparts, and superior at generating bona fide abscopal responses in the presence of an immune checkpoint blocker. Finally, multiple genetic signatures of apoptotic proficiency were unexpectedly found to have robust negative (rather than positive) prognostic significance in a public cohort of breast cancer patients. However, these latter findings were not consistent with genetic signatures of defective type I IFN signaling, which were rather associated with improved prognosis. Differential gene expression analysis on patient subgroups with divergent prognosis (as stratified by independent signatures of apoptotic proficiency) identified SLC7A2 as a new biomarker with independent prognostic value in breast cancer patients. With the caveats associated with the retrospective investigation of heterogeneous, public databases, our data suggest that apoptotic caspases may influence the survival of breast cancer patients (or at least some subsets thereof) via mechanisms not necessarily related to type I IFN signaling as they identify a novel independent prognostic biomarker that awaits prospective validation.
Published: 2019

32. 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

33. 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

34. 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

35. 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

36. Altered cleavage of Caspase-1 in hepatocytes limits control of malaria in the liver

Author: Prajwal Gurung, Samarchith P. Kurup, John T. Harty, Photini Sinnis, Rodrigo P. Baptista, Lecia L. Pewe, Camila Marques-da-Silva, Barun Poudel, Lisa S. Hancox, Justine C. Shiau, Melanie J. Shears, Thirumala-Devi Kanneganti, Kristen Peissig, and Dennis E. Kyle
Subjects: Innate immune system, Caspase 1, Pyroptosis, Biology, biology.organism_classification, medicine.disease, Plasmodium, Microbiology, AIM2, Immune system, parasitic diseases, medicine, Secretion, Malaria
Abstract: Malaria, caused by Plasmodium parasites, is a devastating disease that kills over half a million people each year1. Plasmodium sporozoites inoculated by mosquitoes into mammalian hosts undergo a clinically silent phase of obligatory development and replication in hepatocytes before initiating the life-threatening blood-stage of malaria2. Thus, understanding the immune responses elicited by Plasmodium infection in the liver is key to controlling clinical malaria and transmission3,4. Here, we show that Plasmodium DNA can be detected by AIM2 (absent in melanoma 2) sensors in the infected hepatocytes, resulting in Caspase-1 activation and pyroptotic cell-death. However, Caspase-1 was observed to undergo only partial cleavage in hepatocytes, limiting pyroptosis, and the maturation of pro-inflammatory cytokines classically associated with Caspase-1 activation. We discovered that the extent of Caspase-1 cleavage in cells is determined by the expression of ASC (apoptosis-associated speck-like protein containing a CARD). ASC expression is inherently low in hepatocytes, and transgenically enhancing it in the hepatocytes induced complete processing of Caspase-1, efficient secretion of pro-inflammatory cytokines, enhanced pyroptotic cell-death, and markedly improved control of malaria infection in the liver. In addition to describing a novel pathway of natural immunity to malaria, our findings uncover a key aspect of liver biology that may have been exploited during evolution by successful hepatotropic pathogens.
Published: 2021

37. 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

38. Newly Identified Function of Caspase-6 in ZBP1-mediated Innate Immune Responses, NLRP3 Inflammasome Activation, PANoptosis, and Host Defense

Author: Min Zheng and Thirumala-Devi Kanneganti
Subjects: RIPK1, Necroptosis, Caspase 1, Apoptosis, Caspase 6, Biology, RIPK3, Caspase 8, Article, Inflammasome, NLRP3, Pyroptosis, medicine, PANoptosis, Innate immunity, Innate immune system, ZBP1, PANoptosome, Cell biology, Influenza A virus, Caspase-1, Caspase-8, Caspase-6, medicine.drug
Abstract: Caspase-6 was discovered decades ago, but its roles in biological processes remain largely unknown. Recently, we have demonstrated that caspase-6 plays a critical role in influenza A virus (IAV)-induced cell death and innate immune responses. During IAV infection, Z-DNA binding protein 1 (ZBP1) initiates ZBP1-PANoptosome assembly to drive inflammasome activation and cell death, and we showed that caspase-6 interacts with RIPK3 to enhance the interaction between RIPK3 and ZBP1, thus promoting PANoptosome assembly. Moreover, the caspase activity of caspase-6 is not required for tins process, suggesting a caspase-independent function of caspase-6 during IAV infection. Additionally, we found that caspase-6 is required for the alternative activation of alveolar macrophages in response to IAV infection. Our findings provide an opportunity to reconsider the physiological role of caspase-6.
Published: 2020

39. 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

40. Abstract 13711: Coronary Artery Calcium, Ankle-brachial Index, High Sensitivity C-reactive Protein, and a Family History of Coronary Artery Disease as Predictors of Incident Cardiovascular Events at Different Stages of Hypertension: The Multi-ethnic Study of Atherosclerosis

Author: Radha Kanneganti, Khurram Nasir, Zeina Dardari, Arthur S. Agatston, Karol E. Watson, Roger S. Blumenthal, Matthew J. Budoff, Erin D. Michos, Rajesh Tota-Maharaj, Ron Blankstein, Michael J. Blaha, and Gregory L. Burke
Subjects: medicine.medical_specialty, biology, business.industry, C-reactive protein, medicine.disease, Coronary artery disease, Coronary artery calcium, medicine.anatomical_structure, Physiology (medical), Internal medicine, biology.protein, Cardiology, Medicine, Ankle, Family history, Cardiology and Cardiovascular Medicine, business
Abstract: Background: Coronary artery calcium (CAC), ankle-brachial index (ABI), high-sensitivity CRP (hsCRP), and family history (FHx) of coronary artery disease (CAD) are used as complementary aids in cardiac risk stratification. The 2017 ACC/AHA hypertension guideline’s new Stage I hypertension group has created uncertainty regarding intensity of blood pressure (BP) treatment in this group. We evaluated the comparative utility of CAC, ABI, hsCRP and FHx CAD as risk predictors of cardiovascular (CVD) events within different BP strata. Methods: The MESA cohort was followed for a median of 13 years with regards to incident coronary heart disease (CHD) and CVD events. BP was categorized per ACC/AHA guideline: normal- 300, CAC>75 t h %, ABI2 mg/L and FHx CAD, stratifying by BP groups after adjusting for demographics, CVD risk factors and use of BP and cholesterol medications. Results: Of 6268 persons, 539 incident CHD events and 572 incident CVD events were noted. CAC>300 and CAC>75 th % predicted an increased CHD event risk throughout all BP groups. ABI300 predicted a 2-fold increased CVD risk in all BP groups after adjustment. In the Stage I group, CAC>300, CAC>75 th % and ABI300 had a consistently higher C-statistic throughout all BP categories compared to other risk markers. Conclusion: CAC>300 was associated with increased CHD and CVD risk in all BP groups and demonstrated superior prognostic utility compared to other risk markers. CAC>300, CAC>75 th % and ABI
Published: 2020

41. Programming inflammatory cell death for therapy

Author: Shelbi Christgen, Rebecca E. Tweedell, and Thirumala-Devi Kanneganti
Subjects: Pharmacology, Programmed cell death, Cell signaling, Innate immune system, Cell Death, Necroptosis, Pyroptosis, Caspase 1, Apoptosis, Context (language use), Biology, Article, Immunity, Innate, RIPK1, otorhinolaryngologic diseases, Humans, Pharmacology (medical), Neuroscience
Abstract: Programmed cell death (PCD) is an essential part of organismal development and plays fundamental roles in host defense against pathogens and the maintenance of homeostasis. However, excess activation of PCD pathways has proven to be detrimental and can drive disease. Additionally, resistance to PCD can also contribute to disease development. Modulation of PCD, therefore, has great therapeutic potential in a wide range of diseases, including infectious, neurodegenerative, autoinflammatory, and metabolic diseases and cancer. Nevertheless, manipulation of cell death and inflammation for therapeutic intervention is a delicate process, highly specific to the context of the disease of interest, making the selection of the appropriate target molecule crucially important. Several PCD pathways are associated with innate immunity, including pyroptosis, apoptosis, necroptosis, and PANoptosis, which is defined as an inflammatory PCD pathway with key features of pyroptosis, apoptosis, and/or necroptosis that cannot be accounted for by any of these three PCD pathways alone. All of these PCD pathways are regulated by upstream sensors and signaling cascades that assemble multimeric complexes to serve as activation platforms for downstream molecules; these sensors and signaling molecules provide attractive target points for therapeutic intervention. Here, we discuss the molecular mechanisms of innate immune-mediated cell death in health and disease, with a particular focus on the molecules putatively involved in the formation of the PANoptosome and the induction of inflammatory cell death. Further, we discuss the implications and feasibility of targeting these molecules to improve disease outcomes, as well as current clinical approaches.
Published: 2022

42. 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

43. 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

44. 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

45. ZBP1: A STARGᐰTE to decode the biology of Z-nucleic acids in disease

Author: Thirumala-Devi Kanneganti and Sannula Kesavardhana
Subjects: 0301 basic medicine, Programmed cell death, ZBP1, Necroptosis, Immunology, Pyroptosis, Disease, Biology, Ligand (biochemistry), Cell biology, 03 medical and health sciences, 030104 developmental biology, 0302 clinical medicine, Apoptosis, Nucleic acid, Immunology and Allergy, 030217 neurology & neurosurgery
Abstract: ZBP1 triggers NLRP3 inflammasome activation/pyroptosis, apoptosis, and necroptosis; the specific ligand for ZBP1 activation remains ambiguous. Recent studies, including Devos et al. in this issue of JEM (https://doi.org/10.1084/jem.20191913), collectively suggest that ZBP1 sensing Z-nucleic acids is critical for cell death/inflammatory disease.
Published: 2020

46. The PANoptosome: A Deadly Protein Complex Driving Pyroptosis, Apoptosis, and Necroptosis (PANoptosis)

Author: Parimal Samir, Thirumala-Devi Kanneganti, and R. K. Subbarao Malireddi
Subjects: 0301 basic medicine, Microbiology (medical), Programmed cell death, RIPK1, Necroptosis, 030106 microbiology, Immunology, caspase-1, lcsh:QR1-502, Caspase 1, Apoptosis, Review, Computational biology, ASC, RIPK3, Microbiology, Pyrin domain, caspase-8, lcsh:Microbiology, 03 medical and health sciences, Cellular and Infection Microbiology, Pyroptosis, Humans, PANoptosis, FADD, Phylogeny, Caspase, biology, ZBP1, PANoptosome, 030104 developmental biology, Infectious Diseases, biology.protein
Abstract: Programmed cell death is regulated by evolutionarily conserved pathways that play critical roles in development and the immune response. A newly recognized pathway for proinflammatory programmed cell death called PANoptosis is controlled by a recently identified cytoplasmic multimeric protein complex named the PANoptosome. The PANoptosome can engage, in parallel, three key modes of programmed cell death—pyroptosis, apoptosis, and necroptosis. The PANoptosome components have been implicated in a wide array of human diseases including autoinflammatory diseases, neurodegenerative diseases, cancer, microbial infections, and metabolic diseases. Here, we review putative components of the PANoptosome and present a phylogenetic analysis of their molecular domains and interaction motifs that support complex assembly. We also discuss genetic data that suggest PANoptosis is coordinated by scaffolding and catalytic functions of the complex components and propose mechanistic models for PANoptosome assembly. Overall, this review presents potential mechanisms governing PANoptosis based on evolutionary analysis of the PANoptosome components.
Published: 2020

47. 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

48. Identification of the PANoptosome: A Molecular Platform Triggering Pyroptosis, Apoptosis, and Necroptosis (PANoptosis)

Author: Sannula Kesavardhana, Amanda R. Burton, Thirumala-Devi Kanneganti, David E. Place, R. K. Subbarao Malireddi, Rajendra Karki, Bhesh Raj Sharma, Min Zheng, Shelbi Christgen, Parimal Samir, Benoit Briard, Balaji Banoth, and Shraddha Tuladhar
Subjects: 0301 basic medicine, Microbiology (medical), Salmonella typhimurium, Programmed cell death, RIPK1, Necroptosis, 030106 microbiology, Immunology, Caspase 1, caspase-1, lcsh:QR1-502, Apoptosis, Biology, Caspase 8, ASC, RIPK3, Microbiology, caspase-8, Vesicular stomatitis Indiana virus, lcsh:Microbiology, 03 medical and health sciences, Mice, Cellular and Infection Microbiology, NLRP3, medicine, Pyroptosis, Animals, PANoptosis, Original Research, Macrophages, Inflammasome, PANoptosome, Listeria monocytogenes, Caspases, Initiator, Cell biology, 030104 developmental biology, Infectious Diseases, Influenza A virus, Receptor-Interacting Protein Serine-Threonine Kinases, medicine.drug
Abstract: Programmed cell death plays crucial roles in organismal development and host defense. Recent studies have highlighted mechanistic overlaps and extensive, multifaceted crosstalk between pyroptosis, apoptosis, and necroptosis, three programmed cell death pathways traditionally considered autonomous. The growing body of evidence, in conjunction with the identification of molecules controlling the concomitant activation of all three pathways by pathological triggers, has led to the development of the concept of PANoptosis. During PANoptosis, inflammatory cell death occurs through the collective activation of pyroptosis, apoptosis, and necroptosis, which can circumvent pathogen-mediated inhibition of individual death pathways. Many of the molecular details of this emerging pathway are unclear. Here, we describe the activation of PANoptosis by bacterial and viral triggers and report protein interactions that reveal the formation of a PANoptosome complex. Infection of macrophages with influenza A virus, vesicular stomatitis virus, Listeria monocytogenes, or Salmonella enterica serovar Typhimurium resulted in robust cell death and the hallmarks of PANoptosis activation. Combined deletion of the PANoptotic components caspase-1 (CASP1), CASP11, receptor-interacting serine/threonine-protein kinase 3 (RIPK3), and CASP8 largely protected macrophages from cell death induced by these pathogens, while deletion of individual components provided reduced or no protection. Further, molecules from the pyroptotic, apoptotic, and necroptotic cell death pathways interacted to form a single molecular complex that we have termed the PANoptosome. Overall, our study identifies pathogens capable of activating PANoptosis and the formation of a PANoptosome complex.
Published: 2020

49. The Zα2 domain of ZBP1 is a molecular switch regulating influenza-induced PANoptosis and perinatal lethality during development

Author: Amanda R. Burton, R. K. Subbarao Malireddi, Shondra M. Pruett-Miller, Thirumala-Devi Kanneganti, Peter Vogel, Shaina N. Porter, and Sannula Kesavardhana
Subjects: 0301 basic medicine, Programmed cell death, Inflammasomes, Necroptosis, Embryonic Development, Inflammation, Biology, Biochemistry, Microbiology, 03 medical and health sciences, RIPK1, Orthomyxoviridae Infections, Protein Domains, Influenza, Human, medicine, Pyroptosis, Animals, Humans, Amino Acid Sequence, Molecular Biology, Sequence Deletion, Innate immune system, 030102 biochemistry & molecular biology, Kinase, RNA-Binding Proteins, Inflammasome, Cell Biology, Cell biology, Mice, Inbred C57BL, 030104 developmental biology, Embryo Loss, medicine.symptom, medicine.drug
Abstract: Z-DNA-binding protein 1 (ZBP1) is an innate immune sensor of nucleic acids that regulates host defense responses and development. ZBP1 activation triggers inflammation and pyroptosis, necroptosis, and apoptosis (PANoptosis) by activating receptor-interacting Ser/Thr kinase 3 (RIPK3), caspase-8, and the NLRP3 inflammasome. ZBP1 is unique among innate immune sensors because of its N-terminal Zα1 and Zα2 domains, which bind to nucleic acids in the Z-conformation. However, the specific role of these Zα domains in orchestrating ZBP1 activation and subsequent inflammation and cell death is not clear. Here we generated Zbp1(ΔZα2/ΔZα2) mice that express ZBP1 lacking the Zα2 domain and demonstrate that this domain is critical for influenza A virus–induced PANoptosis and underlies perinatal lethality in mice in which the RIP homotypic interaction motif domain of RIPK1 has been mutated (Ripk1(mRHIM/mRHIM)). Deletion of the Zα2 domain in ZBP1 abolished influenza A virus–induced PANoptosis and NLRP3 inflammasome activation. Furthermore, deletion of the Zα2 domain of ZBP1 was sufficient to rescue Ripk1(mRHIM/mRHIM) mice from perinatal lethality caused by ZBP1-driven cell death and inflammation. Our findings identify the essential role of the Zα2 domain of ZBP1 in several physiological functions and establish a link between Z-RNA sensing via the Zα2 domain and promotion of influenza-induced PANoptosis and perinatal lethality.
Published: 2020

50. Zα2 domain of ZBP1 is a molecular switch regulating Influenza-induced PANoptosis and perinatal lethality during development

Author: Shondra M. Pruett-Miller, Amanda R. Burton, R. K. Subbarao Malireddi, Peter Vogel, Shaina N. Porter, Sannula Kesavardhana, and Thirumala-Devi Kanneganti
Subjects: 0303 health sciences, Programmed cell death, ZBP1, Necroptosis, 030302 biochemistry & molecular biology, Pyroptosis, Inflammasome, Inflammation, Biology, medicine.disease_cause, 3. Good health, Cell biology, 03 medical and health sciences, Apoptosis, medicine, Influenza A virus, medicine.symptom, 030304 developmental biology, medicine.drug
Abstract: Z-DNA-binding protein 1 (ZBP1) is an innate nucleic acid sensor which regulates host defense responses and development. ZBP1 activation triggers inflammation and pyroptosis, necroptosis, and apoptosis (PANoptosis) by activating RIPK3, caspase-8, and the NLRP3 inflammasome. ZBP1 is unique among innate sensors because of its N-terminal Zα1 and Zα2 domains, which bind to nucleic acids in the Z-conformation. However, the specific role of these Zα domains in orchestrating ZBP1 activation and subsequent inflammation and cell death is not clear. Here we have generated Zbp1ΔZα2/ΔZα2 mice that lack the Zα2 domain of ZBP1 and demonstrate that this domain is critical for influenza A virus (IAV)-induced PANoptosis and perinatal lethality in RIPK1-RHIM mutated (Ripk1RHIM/RHIM) mice. Deletion of the Zα2 domain in ZBP1 abolished IAV-induced PANoptosis and NLRP3 inflammasome activation. Furthermore, deletion of the Zα2 domain of ZBP1 was sufficient to rescue Ripk1RHIM/RHIM mice from the perinatal lethality which is caused by ZBP1-driven cell death and inflammation. Our findings identify the essential role of the Zα2 domain of ZBP1 in physiological functions and establish a link between sensing of Z-RNAs via the Zα2 domain and the promotion of influenza-induced PANoptosis and perinatal lethality.
Published: 2020
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