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1. Selective Secretion of KDEL-Bearing Proteins: Mechanisms and Functions

Author

Palazzo, F. C., Sitia, R., and Tempio, T.

Subjects
Cell Biology, Developmental Biology
Abstract

In multicellular organisms, cells must continuously exchange messages with the right meaning, intensity, and duration. Most of these messages are delivered through cognate interactions between membrane and secretory proteins. Their conformational maturation is assisted by a vast array of chaperones and enzymes, ensuring the fidelity of intercellular communication. These folding assistants reside in the early secretory compartment (ESC), a functional unit that encompasses endoplasmic reticulum (ER), intermediate compartment and cis-Golgi. Most soluble ESC residents have C-terminal KDEL-like motifs that prevent their transport beyond the Golgi. However, some accumulate in the ER, while others in downstream stations, implying different recycling rates. Moreover, it is now clear that cells can actively secrete certain ESC residents but not others. This essay discusses the physiology of their differential intracellular distribution, and the mechanisms that may ensure selectivity of release.

Published
2022

2. Regulation of H2O2 transport across cell membranes

Author

Bienert,GP, Medraño-Fernandez,I, Sitia,R, Bienert GP, Medraño-Fernandez I, Sitia R, Margreet C M Vissers, Mark B Hampton, Tony J Kettle, Bienert, Gp, Medraño-Fernandez, I, and Sitia, R

Published
2018

3. Transit of H₂O₂ across the endoplasmic reticulum membrane is not sluggish

Author

Appenzeller-Herzog, C. (Christian), Bánhegyi, G. (Gabor), Bogeski, I. (Ivan), Davies, K. J. (Kelvin J.A.), Delaunay-Moisan, A. (Agnès), Forman, H. J. (Henry Jay), Görlach, A. (Agnes), Kietzmann, T. (Thomas), Laurindo, F. (Francisco), Margittai, E. (Eva), Meyer , A. J. (Andreas J.), Riemer, J. (Jan), Rützler, M. (Michael), Simmen, T. (Thomas), Sitia, R. (Roberto), Toledano, M. B. (Michel B.), and Touw, I. P. (Ivo P.)

Abstract

Cellular metabolism provides various sources of hydrogen peroxide (H₂O₂) in different organelles and compartments. The suitability of H₂O₂ as an intracellular signaling molecule therefore also depends on its ability to pass cellular membranes. The propensity of the membranous boundary of the endoplasmic reticulum (ER) to let pass H₂O₂ has been discussed controversially. In this essay, we challenge the recent proposal that the ER membrane constitutes a simple barrier for H₂O₂ diffusion and support earlier data showing that (i) ample H₂O₂ permeability of the ER membrane is a prerequisite for signal transduction, (ii) aquaporin channels are crucially involved in the facilitation of H₂O₂ permeation, and (iii) a proper experimental framework not prone to artifacts is necessary to further unravel the role of H₂O₂ permeation in signal transduction and organelle biology.

Published
2016

6. The balance of proteasome load vs. capacity determines apoptotic sensitivity of multiple myeloma cells to proteasome inhibition

Author

BIANCHI G, OLIVA O, PAOLO CASCIO P, PENGO N, FONTANA F, CERRUTI F, ORSI A, PASQUALETTO E, MEZGHRANI A, CALBI V, PALLADINI G, GIULIANI N, ANDERSON KC, SITIA R, CENCI S, Bianchi, G, Oliva, O, PAOLO CASCIO, P, Pengo, N, Fontana, F, Cerruti, F, Orsi, A, Pasqualetto, E, Mezghrani, A, Calbi, V, Palladini, G, Giuliani, N, Anderson, Kc, Sitia, R, and Cenci, S

Subjects
PROTEOSTASIS, MYELOMA, PROTEASOME INHIBITORS
Abstract

Proteasome inhibitors (PIs) are effective against multiple myeloma (MM), but the mechanisms of action and bases of individual susceptibility remain unclear. Recent work linked PI sensitivity to protein synthesis and proteasome activity, raising the question whether different levels of proteasome expression and workload underlie PI sensitivity inMMcells (MMCs). Exploiting human MM lines characterized by differential PI sensitivity, we reportthat highly sensitive MMCs express lower proteasome levels and higher proteasomal workload than relatively PI-resistant MMCs, resulting in the accumulation of polyubiquitinated proteins at the expense of free ubiquitin (proteasome stress). Manipulating proteasome expression or workload alters apoptotic sensitivity to PI, demonstrating a cause-effect relationship between proteasome stress and apoptotic responses in MMCs. Intracellular immunostaining in primary, patient-derived MMCs reveals that polyubiquitinated proteins hallmark neoplastic plasmacells, in positive correlation with immunoglobulin (Ig) content, both intra- and interpatient. Moreover, overall proteasome activity of primary MMCs inversely correlates with apoptotic sensitivity to PI. Altogether,our data indicate that the balance between proteasome workload and degradative capacity represents a critical determinant of apoptotic sensitivity of MMCs to PI, potentially providing a framework for identifying indicators of responsiveness and designing novel combination therapies. (Blood. 2009;113:3040-3049)

Published
2009

7. Controllo dell'espressione genica

Author

Amicone, L, Battaglioli, E, Bonaldo, P, Bonfanti, P, Braghetta, P, Camaioni, A, Colombo, A, Dalle Donne, I, Duga, S, Gangitano, C, Garbi, C, Limonta, P, Marini, M, Moretti, R, Poletti, A, Sidoti, A, Sitia, R, Strippoli, R, and Zalfa, F

Subjects
Settore BIO/17
Published
2014

14. Ero1-PDI interactions, the response to redox flux and the implications for disulfide bond formation in the mammalian endoplasmic reticulum

Author

Benham, A.M., Lith, M. van, Sitia, R., Braakman, I., Cellular Protein Chemistry, Chemie van glyco-conjugaten, Dep Scheikunde, Sub Cellular Protein Chemistry, Benham, Am, van Lith, M, Sitia, Roberto, Braakman, I., Cellular Protein Chemistry, Chemie van glyco-conjugaten, Dep Scheikunde, and Sub Cellular Protein Chemistry

Subjects
Redox Disulfide bond, DNA, Complementary, Protein Disulfide-Isomerases, Chaperone, Endoplasmic Reticulum, Redox, General Biochemistry, Genetics and Molecular Biology, Cell Line, redox regulation, 03 medical and health sciences, 0302 clinical medicine, ER oxidoreductin, protein folding, protein secretion, chaperone, Animals, Humans, Disulfides, Protein folding, Protein disulfide-isomerase, Secretory pathway, 030304 developmental biology, Mammals, chemistry.chemical_classification, 0303 health sciences, Membrane Glycoproteins, biology, Chemistry, Endoplasmic reticulum, Articles, Electron acceptor, Cell biology, Gene Expression Regulation, redox, Chaperone (protein), oxidative folding, biology.protein, Biophysics, disulfide bond, Oxidoreductases, General Agricultural and Biological Sciences, Oxidation-Reduction, 030217 neurology & neurosurgery, Research Article, Molecular Chaperones
Abstract

The protein folding machinery of the endoplasmic reticulum (ER) ensures that proteins entering the eukaryotic secretory pathway acquire appropriate post-translational modifications and reach a stably folded state. An important component of this protein folding process is the supply of disulfide bonds. These are introduced into client proteins by ER resident oxidoreductases, including ER oxidoreductin 1 (Ero1). Ero1 is usually considered to function in a linear pathway, by ‘donating’ a disulfide bond to protein disulfide isomerase (PDI) and receiving electrons that are passed on to the terminal electron acceptor molecular oxygen. PDI engages with a range of clients as the direct catalyst of disulfide bond formation, isomerization or reduction. In this paper, we will consider the interactions of Ero1 with PDI family proteins and chaperones, highlighting the effect that redox flux has on Ero1 partnerships. In addition, we will discuss whether higher order protein complexes play a role in Ero1 function.

Published
2013

16. Neurodegeneration

Author

Milardi, D, Rizzarelli, Enrico, Williams, R. J. P., FRAUSTO DA SILVA, J. J. R., Saaranen, M. J., Ruddock, L. W., Cenci, S, Sitia, R, Kagan, B. L., Grasso, Giuseppe, LA MENDOLA, D, Amadoro, G, Calissano, P, Rembach, A, Duce, J. A., O'Sullivan, L. A., Tanzi, R. E., Bush, A. I., Zucca, F. A., Cupaioli, f. a., Zecca, L, Bolognin, S, Zatta, P, Lelie, H. L., Whitelegge, J. P., Borchelt, D. R., Valentine, J. S., and Millhauser, G. L.

Subjects
Proteostasis, Neurodegeneration, medicine, Biology, medicine.disease, Neuroscience
Published
2011

39. Modulating secretion of antibodies

Author

Fra, A. M., Alberini, C., Bet, P., Dario Finazzi, Valetti, C., and Sitia, R.

Subjects
B-Lymphocytes, Adjuvants, Immunologic, Immunoglobulin M, Humans, Immunoglobulins, Biological Transport, Cell Differentiation, Cysteine, Endoplasmic Reticulum
Abstract

Cells have means to ensure that only properly folded and assembled molecules are transported to their final destination, a phenomenon referred to as "quality control" of protein synthesis. Thus, plasma cells secrete only the polymeric form of IgM, retaining and degrading intracellularly assembly intermediates. Due to the failure to polymerize secretory IgM, B lymphocytes do not secrete IgM, while they express the membrane form of IgM on their surface. The selective retention of IgM assembly intermediates is due to disulphide interchange reactions which involve the C terminal cysteine of secretory microseconds chains and unknown protein(s) of the endoplasmic reticulum (ER). Assembly inhibits these reactions, as does addition of reducing agents. In the latter condition, assembly intermediates, otherwise retained and degraded in the ER, are transported to the Golgi, glycosylated and secreted. The developmental control of immunoglobulin secretion is discussed in the more general context of "quality control" of newly synthesized protein within the exocytic compartment.

Published
1991

45. Endoplasmic reticulum oxidoreductase 1 alpha modulates prostate cancer hallmarks

Author

Edoardo Pozzi, Ilaria T. Cavarretta, Tiziana Tempio, Giovanni Lavorgna, Irene Locatelli, Francesco Montorsi, Agostino Mattei, Andrea Salonia, Roberto Sitia, Julian Cornelius, Tiziana Anelli, Cornelius, J., Cavarretta, I., Pozzi, E., Lavorgna, G., Locatelli, I., Tempio, T., Montorsi, F., Mattei, A., Sitia, R., Salonia, A., and Anelli, T.

Subjects
Gene knockdown, Urology, Endoplasmic reticulum, Redoxstasis, Cancer, Biology, medicine.disease, urologic and male genital diseases, Prostate cancer, Reproductive Medicine, Downregulation and upregulation, Endoplasmatic reticulum, RNA interference, Tumor progression, medicine, Cancer research, Gene silencing, Endoplasmic reticulum oxidoreductase 1 alpha (Ero 1a), Original Article, Gleason score, Prostate cancer (PCa)
Abstract

Background Therapies available for late stage prostate cancer (PCa) patients are limited and mostly palliative. The necessary development of unexplored therapeutic options relies on a deeper knowledge of molecular mechanisms leading to cancer progression. Redox signals are known to modulate the intensity and duration of oncogenic circuits; cues originating from the endoplasmic reticulum (ER) and downstream exocytic organelles are relevant in secretory tumors, including PCa. Ero 1α is a master regulator of redox homeostasis and oxidative folding. Methods We assessed Ero 1α mRNA expression by bioinformatic analysis of three public datasets and protein expression levels in PCa cell lines representing different degrees of tumor progression and different human prostate specimens. Transient Ero 1α knockdown was achieved by RNA interference (siRNA). Consequences of Ero 1α downregulation were monitored by PCa proliferation, migration and invasion properties. Results Ero 1α mRNA and protein levels are upregulated in PCa cell lines compared to non-tumorigenic cells (P=0.0273). Ero 1α expression increases with the grade of malignancy, reaching the highest level in the androgen resistant PC3. In patients' samples from 3 datasets, Ero 1α mRNA expression correlates with pathological Gleason scores. Ero 1α knockdown inhibits proliferation (P=0.0081), migration (P=0.0085) and invasion (P=0.0007) of PC3 cells and alters the levels of integrin β1 (P=0.0024). Conclusions Results indicate that Ero 1α levels correlate with PCa aggressiveness; Ero 1α silencing inhibits key steps over the PCa metastatic process. Therefore, Ero 1α has the potential to be exploited as a novel biomarker and a therapeutic target in PCa.

Published
2021

46. Biogenesis of secretory immunoglobulin M requires intermediate non-native disulfide bonds and engagement of the protein disulfide isomerase ERp44

Author

Chiara Giannone, Maria Rita Chelazzi, Andrea Orsi, Tiziana Anelli, Tuan Nguyen, Johannes Buchner, Roberto Sitia, Giannone, C., Chelazzi, M. R., Orsi, A., Anelli, T., Nguyen, T., Buchner, J., and Sitia, R.

Subjects
General Immunology and Microbiology, General Neuroscience, Membrane Proteins, disulfide bonds, Articles, General Biochemistry, Genetics and Molecular Biology, secretion, HEK293 Cells, Immunoglobulin M, Humans, Disulfides, protein quality control, ERp44, Molecular Biology, polymeric immunoglobulins, Molecular Chaperones
Abstract

Antibodies of the immunoglobulin M (IgM) class represent the frontline of humoral immune responses. They are secreted as planar polymers in which flanking µ(2)L(2) “monomeric” subunits are linked by two disulfide bonds, one formed by the penultimate cysteine (C575) in the tailpiece of secretory µ chains (µ(s)tp) and the second by C414 in the Cµ3. The latter bond is not present in membrane IgM. Here, we show that C575 forms a non‐native, intra‐subunit disulfide bond as a key step in the biogenesis of secretory IgM. The abundance of this unexpected intermediate correlates with the onset and extent of polymerization. The rearrangement of the C‐terminal tails into a native quaternary structure is guaranteed by the engagement of protein disulfide isomerase ERp44, which attacks the non‐native C575 bonds. The resulting conformational changes promote polymerization and formation of C414 disulfide linkages. This unusual assembly pathway allows secretory polymers to form without the risk of disturbing the role of membrane IgM as part of the B cell antigen receptor.

Published
2021

47. A virtuous cycle operated by ERp44 and ERGIC-53 guarantees proteostasis in the early secretory compartment

Author

Tiziana Tempio, Andrea Orsi, Edgar Djaha Yoboue, Tiziana Anelli, Daria Sicari, Roberto Sitia, Caterina Valetti, Tempio, T., Orsi, A., Sicari, D., Valetti, C., Yoboue, E. D., Anelli, T., and Sitia, R.

Subjects
0301 basic medicine, Multidisciplinary, Chemistry, Endoplasmic reticulum, Vesicle, Biochemistry, Biological Sciences, Cell Biology, Molecular Biology, 02 engineering and technology, 021001 nanoscience & nanotechnology, Article, Cell biology, Transport protein, 03 medical and health sciences, 030104 developmental biology, Proteostasis, Compartment (development), lcsh:Q, Secretion, lcsh:Science, 0210 nano-technology, Receptor, COPII
Abstract

Summary The composition of the secretome depends on the combined action of cargo receptors that facilitate protein transport and sequential checkpoints that restrict it to native conformers. Acting after endoplasmic reticulum (ER)-resident chaperones, ERp44 retrieves its clients from downstream compartments. To guarantee efficient quality control, ERp44 should exit the ER as rapidly as its clients, or more. Here, we show that appending ERp44 to different cargo proteins increases their secretion rates. ERp44 binds the cargo receptor ER-Golgi intermediate compartment (ERGIC)-53 in the ER to negotiate preferential loading into COPII vesicles. Silencing ERGIC-53, or competing for its COPII binding with 4-phenylbutyrate, causes secretion of Prdx4, an enzyme that relies on ERp44 for intracellular localization. In more acidic, zinc-rich downstream compartments, ERGIC-53 releases its clients and ERp44, which can bind and retrieve non-native conformers via KDEL receptors. By coupling the transport of cargoes and inspector proteins, cells ensure efficiency and fidelity of secretion., Graphical abstract, Highlights • ERGIC-53 binds ERp44 and accelerates its exit from the ER • Genetic or pharmacological inhibition of ERGIC-53 impairs ERp44 retrieval function • ERp44 and ERGIC-53 form a functional couple needed for post-ER QC, Biological Sciences; Biochemistry; Molecular Biology; Cell Biology

Published
2021

48. Correction: Role of the early secretory pathway in SARS-CoV-2 infection

Author

Daria Sicari, Roberto Sitia, Theodoros Koutsandreas, Eric Chevet, Aristotelis Chatziioannou, Sicari, D., Chatziioannou, A., Koutsandreas, T., Sitia, R., and Chevet, E.

Subjects
2019-20 coronavirus outbreak, Coronavirus disease 2019 (COVID-19), Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), Correction, Cell Biology, Biology, Virology, Secretory pathway
Published
2020

49. Role of the early secretory pathway in SARS-CoV-2 infection

Author

Aristotelis Chatziioannou, Eric Chevet, Theodoros Koutsandreas, Daria Sicari, Roberto Sitia, 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), Universita Vita Salute San Raffaele = Vita-Salute San Raffaele University [Milan, Italie] (UniSR), CRLCC Eugène Marquis (CRLCC), Biomedical Research Foundation of the Academy of Athens (BRFAA), Institut National de la Santé et de la Recherche Médicale, eRARE-ERAAT, Agence Nationale de la Recherche, PLBIO_2018, Institut National Du Cancer, Frm DEQ20180339169, Fondation pour la Recherche Médicale, Associazione Italiana per la Ricerca sul Cancro, European Commission, Horizon 2020 Framework Programme, MSCA-RISE-734749, H2020 Marie Skłodowska-Curie Actions, MIS 5002780, ELIXIR-GR, Université de Rennes (UR)-CRLCC Eugène Marquis (CRLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM), HAL UR1, Admin, Sicari, D., Chatziioannou, A., Koutsandreas, T., Sitia, R., and Chevet, E.

Subjects
Protein Homeostasis, viruses, Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), Pneumonia, Viral, [SDV.CAN]Life Sciences [q-bio]/Cancer, Biology, Virus Replication, Antiviral Agents, Virus, Betacoronavirus, 03 medical and health sciences, 0302 clinical medicine, [SDV.CAN] Life Sciences [q-bio]/Cancer, Exponential growth, Virology, Humans, Disease, skin and connective tissue diseases, Pandemics, Secretory pathway, 030304 developmental biology, 0303 health sciences, Secretory Pathway, Trafficking, SARS-CoV-2, fungi, COVID-19, RNA, Cell Biology, Molecular machine, respiratory tract diseases, Cell biology, Transport protein, body regions, 030220 oncology & carcinogenesis, Perspective, Coronavirus Infections, Biogenesis
Abstract

Sicari et al. discuss the early secretory pathway in the SARS-CoV-2 infection cycle and provide a perspective on potential therapeutic implications., Similar to other RNA viruses, SARS-CoV-2 must (1) enter a target/host cell, (2) reprogram it to ensure its replication, (3) exit the host cell, and (4) repeat this cycle for exponential growth. During the exit step, the virus hijacks the sophisticated machineries that host cells employ to correctly fold, assemble, and transport proteins along the exocytic pathway. Therefore, secretory pathway–mediated assemblage and excretion of infective particles represent appealing targets to reduce the efficacy of virus biogenesis, if not to block it completely. Here, we analyze and discuss the contribution of the molecular machines operating in the early secretory pathway in the biogenesis of SARS-CoV-2 and their relevance for potential antiviral targeting. The fact that these molecular machines are conserved throughout evolution, together with the redundancy and tissue specificity of their components, provides opportunities in the search for unique proteins essential for SARS-CoV-2 biology that could also be targeted with therapeutic objectives. Finally, we provide an overview of recent evidence implicating proteins of the early secretory pathway as potential antiviral targets with effective therapeutic applications.

Published
2020

50. The importance of naturally attenuated SARS‐CoV ‐2 in the fight against COVID ‐19

Author

Armengaud, Jean, Delaunay‐Moisan, Agnès, Thuret, Jean‐Yves, Anken, Eelco, Acosta‐Alvear, Diego, Aragón, Tomás, Arias, Carolina, Blondel, Marc, Braakman, Ineke, Collet, Jean‐François, Courcol, René, Danchin, Antoine, Deleuze, Jean‐François, Lavigne, Jean‐Philippe, Lucas, Sophie, Michiels, Thomas, Moore, Edward R. B., Nixon‐Abell, Jonathon, Rossello‐Mora, Ramon, Shi, Zheng‐Li, Siccardi, Antonio G., Sitia, Roberto, Tillett, Daniel, Timmis, Kenneth N., Toledano, Michel B., Sluijs, Peter, Vicenzi, Elisa, Médicaments et Technologies pour la Santé (MTS), Université Paris-Saclay-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), 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), Stress Oxydatif et Cancer (SOC), Département Biologie Cellulaire (BioCell), 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 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)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Centre National de la Recherche Scientifique (CNRS), Sénescence et stabilité génomique (SEN), Département Biologie des Génomes (DBG), San Raffaele Scientific Institute, Vita-Salute San Raffaele University and Center for Translational Genomics and Bioinformatics, University of California [Santa Barbara] (UC Santa Barbara), University of California (UC), Universidad Pública de Navarra [Espagne] = Public University of Navarra (UPNA), Génétique, génomique fonctionnelle et biotechnologies (UMR 1078) (GGB), EFS-Université de Brest (UBO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO), Université de Bretagne Occidentale - UFR Médecine et Sciences de la Santé (UBO UFR MSS), Utrecht University [Utrecht], Université Catholique de Louvain = Catholic University of Louvain (UCL), Walloon Excellence in Life sciences and BIOtechnology [Liège] (WELBIO), 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 Paris Cité (UPCité), Centre National de Recherche en Génomique Humaine (CNRGH), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Institut de Biologie François JACOB (JACOB), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Virulence bactérienne et maladies infectieuses (VBMI), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Montpellier (UM), University of Gothenburg (GU), Sahlgrenska University Hospital [Gothenburg], University of Cambridge [UK] (CAM), Institut Mediterrani d'Estudis Avancats (IMEDEA), Consejo Superior de Investigaciones Científicas [Madrid] (CSIC)-Universidad de las Islas Baleares (UIB), Wuhan Institute of Virology [Wuhan, China], Chinese Academy of Sciences [Wuhan Branch], Technische Universität Braunschweig = Technical University of Braunschweig [Braunschweig], ANR-17-CE18-0023,Phylopeptidomics,Identification rapide de bactéries pathogènes et résistances aux antibiotiques(2017), Armengaud, Jean [0000-0003-1589-445X], Thuret, Jean-Yves [0000-0001-5385-7620], Anken, Eelco van [0000-0001-9529-2701], Acosta-Alvear, Diego [0000-0002-1139-8486], Aragón, Tomás [0000-0002-1700-2729], Arias, Carolina [0000-0002-4445-0826], Blondel, Marc [0000-0003-4897-2995], Braakman, Ineke [0000-0003-1592-4364], Collet, Jean-François [0000-0001-8069-7036], Courcol, René [0000-0003-2324-5687], Danchin, Antoine [0000-0002-6350-5001], Deleuze, Jean-François [0000-0002-5358-4463], Lavigne, Jean-Philippe [0000-0002-9484-0304], Lucas, Sophie [0000-0003-1287-7996], Michiels, Thomas [0000-0001-9615-8053], Moore, Edward R.B. [0000-0001-7693-924X], Nixon-Abell, Jonathon [0000-0003-4169-0012], Rosselló-Mora, Ramón [0000-0001-8253-3107], Shi, Zheng-Li [0000-0001-8089-163X], Siccardi, Antonio G. [0000-0002-1654-5545], Sitia, Roberto [0000-0001-7086-4152], Tillett, Daniel [0000-0003-1061-0489], Timmis, Kenneth N. [0000-0002-0066-4670], Toledano, Michel B. [0000-0002-3079-1179], Sluijs, Peter van der [0000-0002-4485-3342], Vicenzi, Elisa [0000-0003-0051-3968], University of California [Santa Barbara] (UCSB), University of California, Institut Brestois Santé Agro Matière (IBSAM), Université de Brest (UBO)-Université de Brest (UBO)-EFS-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Paris (UP), Technical University Braunschweig, Armengaud, Jean, Thuret, Jean-Yves, Anken, Eelco van, Acosta-Alvear, Diego, Aragón, Tomás, Arias, Carolina, Blondel, Marc, Braakman, Ineke, Collet, Jean-François, Courcol, René, Danchin, Antoine, Deleuze, Jean-François, Lavigne, Jean-Philippe, Lucas, Sophie, Michiels, Thomas, Moore, Edward R.B., Nixon-Abell, Jonathon, Rosselló-Mora, Ramón, Shi, Zheng-Li, Siccardi, Antonio G., Sitia, Roberto, Tillett, Daniel, Timmis, Kenneth N., Toledano, Michel B., Sluijs, Peter van der, Vicenzi, Elisa, Armengaud, J., Delaunay-Moisan, A., Thuret, J. -Y., van Anken, E., Acosta-Alvear, D., Aragon, T., Arias, C., Blondel, M., Braakman, I., Collet, J. -F., Courcol, R., Danchin, A., Deleuze, J. -F., Lavigne, J. -P., Lucas, S., Michiels, T., Moore, E. R. B., Nixon-Abell, J., Rossello-Mora, R., Shi, Z., Siccardi, A. G., Sitia, R., Tillett, D., Timmis, K. N., Toledano, M. B., van der Sluijs, P., Vicenzi, E., and UCL - SSS/DDUV - Institut de Duve

Subjects
Opinion, viruses, Pneumonia, Viral, Gene Expression, Microbiology, Disease Outbreaks, Evolution, Molecular, Betacoronavirus, [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases, Animals, Humans, Health emergency, Selection, Genetic, Pandemics, Ecology, Evolution, Behavior and Systematics, [SDV.MHEP.ME]Life Sciences [q-bio]/Human health and pathology/Emerging diseases, Virulence, SARS-CoV-2, fungi, COVID-19, SARS Virus, Adaptation, Physiological, Severe acute respiratory syndrome-related coronavirus, Host-Pathogen Interactions, Mutation, Spike Glycoprotein, Coronavirus, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology, Coronavirus Infections
Abstract

The current SARS‐CoV‐2 pandemic is wreaking havoc throughout the world and has rapidly become a global health emergency. A central question concerning COVID‐19 is why some individuals become sick and others not. Many have pointed already at variation in risk factors between individuals. However, the variable outcome of SARS‐CoV‐2 infections may, at least in part, be due also to differences between the viral subspecies with which individuals are infected. A more pertinent question is how we are to overcome the current pandemic. A vaccine against SARS‐CoV‐2 would offer significant relief, although vaccine developers have warned that design, testing and production of vaccines may take a year if not longer. Vaccines are based on a handful of different designs (i), but the earliest vaccines were based on the live, attenuated virus. As has been the case for other viruses during earlier pandemics, SARS‐CoV‐2 will mutate and may naturally attenuate over time (ii). What makes the current pandemic unique is that, thanks to state‐of‐the‐art nucleic acid sequencing technologies, we can follow in detail how SARS‐CoV‐2 evolves while it spreads. We argue that knowledge of naturally emerging attenuated SARS‐CoV‐2 variants across the globe should be of key interest in our fight against the pandemic.

Published
2020
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