Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus.
Identifieur interne : 002125 ( Main/Exploration ); précédent : 002124; suivant : 002126Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus.
Auteurs : I-Chueh Huang [États-Unis] ; Charles C. Bailey ; Jessica L. Weyer ; Sheli R. Radoshitzky ; Michelle M. Becker ; Jessica J. Chiang ; Abraham L. Brass ; Asim A. Ahmed ; Xiaoli Chi ; Lian Dong ; Lindsay E. Longobardi ; Dutch Boltz ; Jens H. Kuhn ; Stephen J. Elledge ; Sina Bavari ; Mark R. Denison ; Hyeryun Choe ; Michael FarzanSource :
- PLoS pathogens [ 1553-7374 ] ; 2011.
Descripteurs français
- KwdFr :
- Animaux, Antigènes de différenciation (immunologie), Antigènes de différenciation (métabolisme), Cellules Vero, Endothélium vasculaire, Femelle, Filoviridae (croissance et développement), Filoviridae (pathogénicité), Humains, Interactions hôte-pathogène, Lignée cellulaire tumorale, Maladies virales (immunologie), Maladies virales (métabolisme), Maladies virales (virologie), Pénétration virale, Réplication virale, Souris, Virus de la grippe A (croissance et développement), Virus de la grippe A (pathogénicité), Virus du SRAS (croissance et développement), Virus du SRAS (pathogénicité).
- MESH :
- croissance et développement : Filoviridae, Virus de la grippe A, Virus du SRAS.
- immunologie : Antigènes de différenciation, Maladies virales.
- métabolisme : Antigènes de différenciation, Maladies virales.
- pathogénicité : Filoviridae, Virus de la grippe A, Virus du SRAS.
- virologie : Maladies virales.
- Animaux, Cellules Vero, Endothélium vasculaire, Femelle, Humains, Interactions hôte-pathogène, Lignée cellulaire tumorale, Pénétration virale, Réplication virale, Souris.
English descriptors
- KwdEn :
- Animals, Antigens, Differentiation (immunology), Antigens, Differentiation (metabolism), Cell Line, Tumor, Chlorocebus aethiops, Endothelium, Vascular, Female, Filoviridae (growth & development), Filoviridae (pathogenicity), Host-Pathogen Interactions, Humans, Influenza A virus (growth & development), Influenza A virus (pathogenicity), Mice, SARS Virus (growth & development), SARS Virus (pathogenicity), Vero Cells, Virus Diseases (immunology), Virus Diseases (metabolism), Virus Diseases (virology), Virus Internalization, Virus Replication.
- MESH :
- chemical , immunology : Antigens, Differentiation.
- chemical , metabolism : Antigens, Differentiation.
- growth & development : Filoviridae, Influenza A virus, SARS Virus.
- immunology : Virus Diseases.
- metabolism : Virus Diseases.
- pathogenicity : Filoviridae, Influenza A virus, SARS Virus.
- virology : Virus Diseases.
- Animals, Cell Line, Tumor, Chlorocebus aethiops, Endothelium, Vascular, Female, Host-Pathogen Interactions, Humans, Mice, Vero Cells, Virus Internalization, Virus Replication.
Abstract
Interferon-inducible transmembrane proteins 1, 2, and 3 (IFITM1, 2, and 3) are recently identified viral restriction factors that inhibit infection mediated by the influenza A virus (IAV) hemagglutinin (HA) protein. Here we show that IFITM proteins restricted infection mediated by the entry glycoproteins (GP(1,2)) of Marburg and Ebola filoviruses (MARV, EBOV). Consistent with these observations, interferon-β specifically restricted filovirus and IAV entry processes. IFITM proteins also inhibited replication of infectious MARV and EBOV. We observed distinct patterns of IFITM-mediated restriction: compared with IAV, the entry processes of MARV and EBOV were less restricted by IFITM3, but more restricted by IFITM1. Moreover, murine Ifitm5 and 6 did not restrict IAV, but efficiently inhibited filovirus entry. We further demonstrate that replication of infectious SARS coronavirus (SARS-CoV) and entry mediated by the SARS-CoV spike (S) protein are restricted by IFITM proteins. The profile of IFITM-mediated restriction of SARS-CoV was more similar to that of filoviruses than to IAV. Trypsin treatment of receptor-associated SARS-CoV pseudovirions, which bypasses their dependence on lysosomal cathepsin L, also bypassed IFITM-mediated restriction. However, IFITM proteins did not reduce cellular cathepsin activity or limit access of virions to acidic intracellular compartments. Our data indicate that IFITM-mediated restriction is localized to a late stage in the endocytic pathway. They further show that IFITM proteins differentially restrict the entry of a broad range of enveloped viruses, and modulate cellular tropism independently of viral receptor expression.
DOI: 10.1371/journal.ppat.1001258
PubMed: 21253575
Affiliations:
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Le document en format XML
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<term>Chlorocebus aethiops</term>
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<term>Filoviridae (pathogenicity)</term>
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<front><div type="abstract" xml:lang="en">Interferon-inducible transmembrane proteins 1, 2, and 3 (IFITM1, 2, and 3) are recently identified viral restriction factors that inhibit infection mediated by the influenza A virus (IAV) hemagglutinin (HA) protein. Here we show that IFITM proteins restricted infection mediated by the entry glycoproteins (GP(1,2)) of Marburg and Ebola filoviruses (MARV, EBOV). Consistent with these observations, interferon-β specifically restricted filovirus and IAV entry processes. IFITM proteins also inhibited replication of infectious MARV and EBOV. We observed distinct patterns of IFITM-mediated restriction: compared with IAV, the entry processes of MARV and EBOV were less restricted by IFITM3, but more restricted by IFITM1. Moreover, murine Ifitm5 and 6 did not restrict IAV, but efficiently inhibited filovirus entry. We further demonstrate that replication of infectious SARS coronavirus (SARS-CoV) and entry mediated by the SARS-CoV spike (S) protein are restricted by IFITM proteins. The profile of IFITM-mediated restriction of SARS-CoV was more similar to that of filoviruses than to IAV. Trypsin treatment of receptor-associated SARS-CoV pseudovirions, which bypasses their dependence on lysosomal cathepsin L, also bypassed IFITM-mediated restriction. However, IFITM proteins did not reduce cellular cathepsin activity or limit access of virions to acidic intracellular compartments. Our data indicate that IFITM-mediated restriction is localized to a late stage in the endocytic pathway. They further show that IFITM proteins differentially restrict the entry of a broad range of enveloped viruses, and modulate cellular tropism independently of viral receptor expression.</div>
</front>
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