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8 results on '"Lilliana Radoshevich"'

1. ISG15 Is Required for the Dissemination of Vaccinia Virus Extracellular Virions

Author

Martina Bécares, Manuel Albert, Céline Tárrega, Rocío Coloma, Michela Falqui, Emma K. Luhmann, Lilliana Radoshevich, and Susana Guerra

Subjects
ISG15, VACV, actin tails, Microbiology, QR1-502
Abstract

ABSTRACT Viruses have developed many different strategies to counteract immune responses, and Vaccinia virus (VACV) is one of a kind in this aspect. To ensure an efficient infection, VACV undergoes a complex morphogenetic process resulting in the production of two types of infective virions: intracellular mature virus (MV) and extracellular enveloped virus (EV), whose spread depends on different dissemination mechanisms. MVs disseminate after cell lysis, whereas EVs are released or propelled in actin tails from living cells. Here, we show that ISG15 participates in the control of VACV dissemination. Infection of Isg15−/− mouse embryonic fibroblasts with VACV International Health Department-J (IHD-J) strain resulted in decreased EV production, concomitant with reduced induction of actin tails and the abolition of comet-shaped plaque formation, compared to Isg15+/+ cells. Transmission electron microscopy revealed the accumulation of intracellular virus particles and a decrease in extracellular virus particles in the absence of interferon-stimulated gene 15 (ISG15), a finding consistent with altered virus egress. Immunoblot and quantitative proteomic analysis of sucrose gradient-purified virions from both genotypes reported differences in protein levels and composition of viral proteins present on virions, suggesting an ISG15-mediated control of viral proteome. Lastly, the generation of a recombinant IHD-J expressing V5-tagged ISG15 (IHD-J-ISG15) allowed us to identify several viral proteins as potential ISG15 targets, highlighting the proteins A34 and A36, which are essential for EV formation. Altogether, our results indicate that ISG15 is an important host factor in the regulation of VACV dissemination. IMPORTANCE Viral infections are a constant battle between the virus and the host. While the host’s only goal is victory, the main purpose of the virus is to spread and conquer new territories at the expense of the host’s resources. Along millions of years of incessant encounters, poxviruses have developed a unique strategy consisting in the production two specialized “troops”: intracellular mature virions (MVs) and extracellular virions (EVs). MVs mediate transmission between hosts, and EVs ensure advance on the battlefield mediating the long-range dissemination. The mechanism by which the virus “decides” to shed from the primary site of infection and its significant impact in viral transmission is not yet fully established. Here, we demonstrate that this process is finely regulated by ISG15/ISGylation, an interferon-induced ubiquitin-like protein with broad antiviral activity. Studying the mechanism that viruses use during infection could result in new ways of understanding our perpetual war against disease and how we might win the next great battle.

Published
2023
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2. ISG15 counteracts Listeria monocytogenes infection

Author

Lilliana Radoshevich, Francis Impens, David Ribet, Juan J Quereda, To Nam Tham, Marie-Anne Nahori, Hélène Bierne, Olivier Dussurget, Javier Pizarro-Cerdá, Klaus-Peter Knobeloch, and Pascale Cossart

Subjects
Listeria monocytogenes, ISG15, innate immunity, ISGylation, endoplasmic reticulum, Medicine, Science, Biology (General), QH301-705.5
Abstract

ISG15 is an interferon-stimulated, linear di-ubiquitin-like protein, with anti-viral activity. The role of ISG15 during bacterial infection remains elusive. We show that ISG15 expression in nonphagocytic cells is dramatically induced upon Listeria infection. Surprisingly this induction can be type I interferon independent and depends on the cytosolic surveillance pathway, which senses bacterial DNA and signals through STING, TBK1, IRF3 and IRF7. Most importantly, we observed that ISG15 expression restricts Listeria infection in vitro and in vivo. We made use of stable isotope labeling in tissue culture (SILAC) to identify ISGylated proteins that could be responsible for the protective effect. Strikingly, infection or overexpression of ISG15 leads to ISGylation of ER and Golgi proteins, which correlates with increased secretion of cytokines known to counteract infection. Together, our data reveal a previously uncharacterized ISG15-dependent restriction of Listeria infection, reinforcing the view that ISG15 is a key component of the innate immune response.

Published
2015
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3. Ring finger protein 213 assembles into a sensor for ISGylated proteins with antimicrobial activity

Author

Caroline Asselman, Madeleine Vessely, Katie Boucher, George D. Moschonas, Koen Sedeyn, Francis Impens, Denzel Eggermont, Tino Hochepied, Qi Wen Teo, Xavier Saelens, Lilliana Radoshevich, Jingshu Zhang, Clara Bredow, Bart Dermaut, Klaus-Peter Knobeloch, Sven Eyckerman, Lia Martina, Sumana Sanyal, Nico Callewaert, Antje Beling, Yifeng Zhang, Heidi Repo, Delphine De Sutter, Fabien Thery, Nele Festjens, and Kevin Leandro

Subjects
Male, Proteomics, ISG15, THP-1 Cells, General Physics and Astronomy, Herpesvirus 1, Human, medicine.disease_cause, Anti-Infective Agents, INTERFERON-STIMULATED GENE, Interferon, Lipid droplet, Medicine and Health Sciences, LISTERIA-MONOCYTOGENES, Enterovirus, LIGASE, Adenosine Triphosphatases, Multidisciplinary, Effector, Chemistry, HUMAN INTERACTOME, PAPAIN-LIKE PROTEASE, Cell biology, Mechanisms of disease, Interferon Type I, Small Ubiquitin-Related Modifier Proteins, Cytokines, VIRUS, AUTOPHAGY, MYCOBACTERIUM-TUBERCULOSIS, Ring Finger Protein 213, Protein Binding, medicine.drug, Listeria, Science, Ubiquitin-Protein Ligases, Article, General Biochemistry, Genetics and Molecular Biology, Virus, medicine, Animals, Humans, MOYAMOYA-DISEASE, Ubiquitins, Ubiquitin, Intracellular parasite, Cerebrovascular disorder, Biology and Life Sciences, Lipid Droplets, General Chemistry, Listeria monocytogenes, Mice, Inbred C57BL, HEK293 Cells, Herpes simplex virus, A549 Cells, Protein Multimerization, HeLa Cells, Post-translational modifications
Abstract

ISG15 is an interferon-stimulated, ubiquitin-like protein that can conjugate to substrate proteins (ISGylation) to counteract microbial infection, but the underlying mechanisms remain elusive. Here, we use a virus-like particle trapping technology to identify ISG15-binding proteins and discover Ring Finger Protein 213 (RNF213) as an ISG15 interactor and cellular sensor of ISGylated proteins. RNF213 is a poorly characterized, interferon-induced megaprotein that is frequently mutated in Moyamoya disease, a rare cerebrovascular disorder. We report that interferon induces ISGylation and oligomerization of RNF213 on lipid droplets, where it acts as a sensor for ISGylated proteins. We show that RNF213 has broad antimicrobial activity in vitro and in vivo, counteracting infection with Listeria monocytogenes, herpes simplex virus 1, human respiratory syncytial virus and coxsackievirus B3, and we observe a striking co-localization of RNF213 with intracellular bacteria. Together, our findings provide molecular insights into the ISGylation pathway and reveal RNF213 as a key antimicrobial effector., During microbial infection, proteins are modified by the ubiquitin-like protein ISG15. Here, the authors uncover RNF213 as a sensor for ISGylated proteins on the surface of lipid droplets, showing that RNF213 has antiviral properties but also directly targets intracellular bacteria in infected cells.

Published
2021

4. Protein modification with ISG15 blocks coxsackievirus pathology by antiviral and metabolic reprogramming

Author

Clara Bredow, Karin Klingel, Henry Fechner, Anna Paeschke, Lilliana Radoshevich, Fabien Thery, Ziya Kaya, Joachim Spranger, Klaus-Peter Knobeloch, Johannes Eckstein, Antje Beling, Francis Impens, Martin Voß, Eva K. Wirth, Martin Zickler, Nikolaus Berndt, Meike Kespohl, Michael Fähling, and Wolfgang Poller

Subjects
genetic structures, medicine.medical_treatment, Metabolic network, Mice, 0302 clinical medicine, INTERFERON-STIMULATED GENE, Medicine and Health Sciences, Research Articles, Mice, Knockout, 0303 health sciences, Multidisciplinary, biology, Intracellular Signaling Peptides and Proteins, Signal transducing adaptor protein, RNA-Binding Proteins, SciAdv r-articles, Life Sciences, MOUSE MODEL, Cell biology, Enterovirus B, Human, Liver, Cytokines, SECRETION, Female, Ubiquitin Thiolesterase, Research Article, MYOCARDITIS, Coxsackievirus Infections, Coxsackievirus, INFLUENZA-A VIRUS, 03 medical and health sciences, TARGETS, UBIQUITIN-LIKE PROTEIN, medicine, Animals, Secretion, Health and Medicine, Shotgun proteomics, Ubiquitins, 030304 developmental biology, Adaptor Proteins, Signal Transducing, Protease, Interferon-stimulated gene, Gluconeogenesis, ISGYLATION, biology.organism_classification, ISG15, CONJUGATION, REPLICATION, Protein Processing, Post-Translational, 030217 neurology & neurosurgery
Abstract

Protein modification with ISG15 acts cooperatively with IFIT proteins and preserves glucose homeostasis., Protein modification with ISG15 (ISGylation) represents a major type I IFN–induced antimicrobial system. Common mechanisms of action and species-specific aspects of ISGylation, however, are still ill defined and controversial. We used a multiphasic coxsackievirus B3 (CV) infection model with a first wave resulting in hepatic injury of the liver, followed by a second wave culminating in cardiac damage. This study shows that ISGylation sets nonhematopoietic cells into a resistant state, being indispensable for CV control, which is accomplished by synergistic activity of ISG15 on antiviral IFIT1/3 proteins. Concurrent with altered energy demands, ISG15 also adapts liver metabolism during infection. Shotgun proteomics, in combination with metabolic network modeling, revealed that ISG15 increases the oxidative capacity and promotes gluconeogenesis in liver cells. Cells lacking the activity of the ISG15-specific protease USP18 exhibit increased resistance to clinically relevant CV strains, therefore suggesting that stabilizing ISGylation by inhibiting USP18 could be exploited for CV-associated human pathologies.

Published
2020

5. The in vivo ISGylome links ISG15 to metabolic pathways and autophagy upon Listeria monocytogenes infection

Author

Pascale Cossart, Olivier Dussurget, Kevin Leandro, Lilliana Radoshevich, Clara Bredow, Mariko Foecke, Daniel Jiménez-Fernández, Nicholas C. Wu, Yifeng Zhang, Emma K. Luhmann, Fabien Thery, Antje Beling, Francis Impens, Klaus-Peter Knobeloch, Carver College of Medicine, University of Iowa, VIB-UGent Center for Medical Biotechnology, Department for Biomolecular Medicine, Universiteit Gent = Ghent University (UGENT), Department of Integrative Structural and Computational Biology [La Jolla, CA, USA], The Scripps Research Institute [La Jolla, San Diego], Interactions Bactéries-Cellules (UIBC), Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM), Charité - UniversitätsMedizin = Charité - University Hospital [Berlin], Berlin Institute of Health (BIH), Institute of Neuropathology, University of Freiburg [Freiburg], VIB Center for Medical Biotechnology, Universiteit Gent = Ghent University [Belgium] (UGENT), Scripps Research Institute, Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), and Lallemant, Pascal

Subjects
Proteomics, 0301 basic medicine, [SDV]Life Sciences [q-bio], General Physics and Astronomy, ns1 protein, 0302 clinical medicine, Medicine and Health Sciences, Listeriosis, lcsh:Science, Multidisciplinary, TOR Serine-Threonine Kinases, Acetylation, Bacterial host response, ANTIVIRAL MOLECULE, 3. Good health, Cell biology, [SDV] Life Sciences [q-bio], secretion, Liver, INFLUENZA, NS1 PROTEIN, Cytokines, targets, SECRETION, Infection, influenza, Metabolic Networks and Pathways, complex, conjugation, Science, Quantitative proteomics, Genetics and Molecular Biology, Biology, Article, General Biochemistry, Genetics and Molecular Biology, proteome-wide identification, Mitochondrial Proteins, stimulated gene-15, 03 medical and health sciences, Downregulation and upregulation, TARGETS, Autophagy, Animals, Secretion, Ubiquitins, PI3K/AKT/mTOR pathway, STIMULATED GENE-15, antiviral molecule, PROTEOME-WIDE IDENTIFICATION, COMPLEX, Lysine, Ubiquitination, ISGYLATION, General Chemistry, Listeria monocytogenes, ISG15, Mice, Mutant Strains, Mice, Inbred C57BL, Metabolic pathway, 030104 developmental biology, isgylation, CONJUGATION, General Biochemistry, lcsh:Q, Protein Processing, Post-Translational, 030217 neurology & neurosurgery, Post-translational modifications
Abstract

ISG15 is an interferon-stimulated, ubiquitin-like protein, with anti-viral and anti-bacterial activity. Here, we map the endogenous in vivo ISGylome in the liver following Listeria monocytogenes infection by combining murine models of reduced or enhanced ISGylation with quantitative proteomics. Our method identifies 930 ISG15 sites in 434 proteins and also detects changes in the host ubiquitylome. The ISGylated targets are enriched in proteins which alter cellular metabolic processes, including upstream modulators of the catabolic and antibacterial pathway of autophagy. Computational analysis of substrate structures reveals that a number of ISG15 modifications occur at catalytic sites or dimerization interfaces of enzymes. Finally, we demonstrate that animals and cells with enhanced ISGylation have increased basal and infection-induced autophagy through the modification of mTOR, WIPI2, AMBRA1, and RAB7. Taken together, these findings ascribe a role of ISGylation to temporally reprogram organismal metabolism following infection through direct modification of a subset of enzymes in the liver., ISG15 is a ubiquitin-like modifier that can be upregulated in response to bacterial infections. Here, the authors use proteomics to identify endogenous ISGylation substrates in the liver of Listeria monocytogenes infected mice and show that ISGylation alters basal and infection-induced autophagy.

Published
2019
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7. Human intracellular ISG15 prevents interferon-α/β over-amplification and auto-inflammation

Author

Nahal Mansouri, Bertrand Boisson, Xianqin Zhang, Qing Kenneth Wang, Gillian I. Rice, Xing Wang, Seyed Alireza Mahdaviani, Chao Yuan, Yuval Itan, Flore Rozenberg, Satoshi Okada, Gilles Uzé, Dusan Bogunovic, Mugen Liu, Tao Ma, Pierre Lebon, Lilliana Radoshevich, Jingyu Liu, Wenqiang Liu, Tiantian Han, Davood Mansouri, Delin Liu, Jean-Laurent Casanova, Béatrice Payelle-Brogard, Yanick J. Crow, Dilek Yalnizoglu, Stefano Volpi, Zhi Li, Ozden Sanal, Lu Zeng, Bo Wang, Chunyuan Chen, Sandra Pellegrini, Shen-Ying Zhang, Emmanuelle Jouanguy, Luigi D. Notarangelo, Adolfo García-Sastre, Philippe Gros, Hui Jiang, Stéphanie Boisson-Dupuis, Véronique Francois-Newton, Laurent Abel, Scott D. Speer, Ilhan Tezcan, Jacinta Bustamante, Li, Zhi, Host and microbial molecular dissection of pathogenesis and immunity in tuberculosis - HOMITB - - EC:FP7:HEALTH2008-11-01 - 2012-04-30 - 200732 - VALID, A system view on the differential activities of human type I interferons - IFNACTION - - EC:FP7:HEALTH2009-01-01 - 2012-12-31 - 223608 - VALID, Huazhong University of Science and Technology [Wuhan] (HUST), Signalisation des Cytokines, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Istituto Giannina Gaslini, Genova, Immunologia Clinica e Sperimentale, Ankara University School of Medicine [Turkey], University of Manchester [Manchester], Shahid Beheshti University of Medical Sciences [Tehran] (SBUMS), Shahid Beheshti University, St. Giles Laboratory of Human Genetics of Infectious Diseases, Rockefeller University [New York], Institut des sciences du végétal (ISV), Centre National de la Recherche Scientifique (CNRS), Department of Mathematics [Nanjing], Nanjing University of Aeronautics and Astronautics [Nanjing] (NUAA), Institut de Recherche en Communications Optiques et Microondes (IRCOM), Université de Limoges (UNILIM)-Centre National de la Recherche Scientifique (CNRS), Hunan Institute of Science and Technology, Interactions Bactéries-Cellules (UIBC), Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM), Dynamique des interactions membranaires normales et pathologiques (DIMNP), Université Montpellier 1 (UM1)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS), Département de Physique des Particules (ex SPP) (DPhP), Institut de Recherches sur les lois Fondamentales de l'Univers (IRFU), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Paris-Saclay, Laboratoire de Virologie, Hôpital Cochin [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Génétique Humaine des Maladies Infectieuses (Inserm U980), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), Imagine - Institut des maladies génétiques (IMAGINE - U1163), Icahn School of Medicine at Mount Sinai [New York] (MSSM), Service de virologie, Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Saint-Vincent de Paul, Università degli Studi di Brescia = University of Brescia (UniBs), The Laboratory of Human Genetics of Infectious Diseases is supported by grants from the French National Agency for Research (ANR), the EU grant HOMITB (HEALTH-F32008-200732), the St Giles Foundation, the National Center for Research Resources and the National Center for Advancing Sciences (NCATS), National Institutes of Health grant number 8UL1TR000043, the Rockefeller University, the National Institute of Allergy and Infectious Diseases grant number R37AI095983, Institut Merieux research grant and the Empire State Stem Cell fund through NYSDOH Contract #C023046 to Flow Cytometry Research Core at the Rockefeller University. The Cytokine Signaling Unit is supported by the Institut Pasteur, CNRS and INSERM. S.P. and G.U. received funding from the EU Seventh Framework Programme under grant agreement 223608. V.F.-N. was supported by the Ligue contre le Cancer. L.R. is a Human Frontier Science Program long-term fellow. L.D.N. was supported by the National Institute of Allergy and Infectious Diseases grant number 1PO1AI076210-01A1. Y.J.C. thanks the Manchester Biomedical Research Centre and the Greater Manchester Comprehensive Local Research Network, the European Union’s Seventh Framework Programme (FP7/2007-2013) under grant agreement 241779, and the European Research Council (GA 309449). A.G.-S. acknowledges NIAID grants U19AI083025 and P01AI090935 for support. We thank C. Daussy for technical assistance, E. Bianchi and F. Michel for discussions. We thank D. Zhang and the members of the Zhang laboratory for assistance, advice and discussions. This work was supported by Chinese National Natural Science Foundation grants (81000079, 81170165) to X.Z. D.B. is supported by the National Institute of Allergy and Infectious Diseases grant number R00AI106942-02., European Project: 200732,EC:FP7:HEALTH,FP7-HEALTH-2007-A,HOMITB(2008), European Project: 223608,EC:FP7:HEALTH,FP7-HEALTH-2007-B,IFNACTION(2009), Çocuk ve Ergen Ruh Sağlığı ve Hastalıkları, Institut Pasteur [Paris]-Centre National de la Recherche Scientifique (CNRS), Shahid Beheshti University of Medical Sciences, The Rockefeller University, St. Giles Laboratory of Human Genetics of Infectious Diseases, Rockefeller Branch, rockefeller university, Department of Mathematics (Nanjing University of Aeronautics and Astronautics), Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Pasteur [Paris]-Institut National de la Recherche Agronomique (INRA), Département de Physique des Particules (ex SPP) (DPP), CHU Cochin [AP-HP], Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris Descartes - Paris 5 (UPD5), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôpital Saint-Vincent de Paul, Department of Pediatrics and Institute for Molecular Medicine Angello Nocivelli, University of Brescia, Centre National de la Recherche Scientifique (CNRS)-Université de Limoges (UNILIM), Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris]-Institut National de la Santé et de la Recherche Médicale (INSERM), Università degli Studi di Brescia [Brescia], and Centre National de la Recherche Scientifique (CNRS)-Université de Montpellier (UM)-Université Montpellier 2 - Sciences et Techniques (UM2)-Université Montpellier 1 (UM1)

Subjects
Male, MESH: Signal Transduction, MESH: Inflammation, MESH: Interferon Type I, Intracellular Space, 0302 clinical medicine, Interferon, MESH: Child, Child, MESH: Endopeptidases, S-Phase Kinase-Associated Proteins, 0303 health sciences, MESH: Cytokines, Multidisciplinary, Effector, MESH: Gene Expression Regulation, Pedigree, 3. Good health, Cell biology, 030220 oncology & carcinogenesis, Interferon Type I, Viruses, Cytokines, Science & Technology - Other Topics, MESH: Intracellular Space, [SDV.IMM]Life Sciences [q-bio]/Immunology, Female, Signal transduction, MESH: S-Phase Kinase-Associated Proteins, Ubiquitin Thiolesterase, Intracellular, Signal Transduction, medicine.drug, Adolescent, [SDV.IMM] Life Sciences [q-bio]/Immunology, MESH: Pedigree, Biology, [SDV.GEN.GH] Life Sciences [q-bio]/Genetics/Human genetics, MESH: Viruses, 03 medical and health sciences, Immunity, Endopeptidases, medicine, Humans, MESH: Ubiquitins, Ubiquitins, Alleles, 030304 developmental biology, Inflammation, MESH: Adolescent, MESH: Humans, MESH: Alleles, Ubiquitination, ISG15, MESH: Male, Neuroimmunology, Gene Expression Regulation, [SDV.GEN.GH]Life Sciences [q-bio]/Genetics/Human genetics, Immunology, MESH: Ubiquitination, MESH: Female, Interferon type I
Abstract

Intracellular ISG15 is an interferon (IFN)-alpha/beta-inducible ubiquitin-like modifier which can covalently bind other proteins in a process called ISGylation; it is an effector of IFN-alpha/beta-dependent antiviral immunity in mice(1-4). We previously published a study describing humans with inherited ISG15deficiency but without unusually severe viral diseases(5). We showed that these patients were prone to mycobacterial disease and that human ISG15 was non-redundant as an extracellular IFN-gamma-inducing molecule. We show here that ISG15-deficient patients also display unanticipated cellular, immunological and clinical signs of enhanced IFN-alpha/beta immunity, reminiscent of the Mendelian autoinflammatory interferonopathies Aicardi-Goutieres syndrome and spondyloenchondrodysplasia(6-9). We further show that an absence of intracellular ISG15 in the patients' cells prevents the accumulation of USP18(10,11), a potent negative regulator of IFN-alpha/beta signalling, resulting in the enhancement and amplification of IFN-alpha/beta responses. Human ISG15, therefore, is not only redundant for antiviral immunity, but is a key negative regulator of IFN-alpha/beta immunity. In humans, intracellular ISG15 is IFN-alpha/beta-inducible not to serve as a substrate for ISGylation-dependent antiviral immunity, but to ensure USP18-dependent regulation of IFN-alpha/beta and prevention of IFN-alpha/beta-dependent autoinflammation.

Published
2015
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8. Erratum: Human intracellular ISG15 prevents interferon-α/β over-amplification and auto-inflammation

Author

Xianqin Zhang, Seyed Alireza Mahdaviani, Chao Yuan, Tao Ma, Lilliana Radoshevich, Véronique Francois-Newton, Béatrice Payelle-Brogard, Davood Mansouri, Delin Liu, Nahal Mansouri, Stefano Volpi, Gilles Uzé, Philippe Gros, Hui Jiang, Bo Wang, Stéphanie Boisson-Dupuis, Ozden Sanal, Laurent Abel, Luigi D. Notarangelo, Dusan Bogunovic, Flore Rozenberg, Mugen Liu, Scott D. Speer, Yuval Itan, Jacinta Bustamante, Yanick J. Crow, Emmanuelle Jouanguy, Adolfo García-Sastre, Tiantian Han, Pierre Lebon, Dilek Yalnizoglu, Ilhan Tezcan, Sandra Pellegrini, Qing Kenneth Wang, Jean-Laurent Casanova, Wenqiang Liu, Xing Wang, Satoshi Okada, Chunyuan Chen, Shen-Ying Zhang, Lu Zeng, Jingyu Liu, Zhi Li, Bertrand Boisson, and Gillian I. Rice

Subjects
Multidisciplinary, Chemistry, Interferon α β, medicine, Inflammation, Erratum, medicine.symptom, error, ISG15, Molecular biology, Intracellular
Abstract

Nature 517, 89–93 (2015); doi:10.1038/nature13801In this Letter, author J.-L.C. was inadvertently missing one of their affiliations; they should also have been associated with affiliation number 2 (St. Giles Laboratory of Human Genetics of Infectious Diseases, Rockefeller Branch, The Rockefeller University, New York, New York 10065, USA). This has been corrected in the online versions of the paper.

Published
2015
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