Abstract
2'-5'-Oligoadenylate synthetase-like protein (OASL) is an interferon-inducible antiviral protein. Here we describe differential inhibitory activities of human OASL and the two mouse OASL homologs against respiratory syncytial virus (RSV) replication. Interestingly, nonstructural protein 1 (NS1) of RSV promoted proteasome-dependent degradation of specific OASL isoforms. We conclude that OASL acts as a cellular antiviral protein and that RSV NS1 suppresses this function to evade cellular innate immunity and allow virus growth.
Copyright © 2015, American Society for Microbiology. All Rights Reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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2',5'-Oligoadenylate Synthetase / immunology
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2',5'-Oligoadenylate Synthetase / physiology*
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Animals
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HEK293 Cells
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Host-Pathogen Interactions
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Humans
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Immune Evasion
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Immunity, Cellular
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Mice
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Proteasome Endopeptidase Complex / metabolism
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Proteolysis
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Respiratory Syncytial Virus Infections / immunology
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Respiratory Syncytial Virus Infections / virology
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Respiratory Syncytial Viruses / genetics
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Respiratory Syncytial Viruses / immunology
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Respiratory Syncytial Viruses / physiology*
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Viral Nonstructural Proteins / genetics
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Viral Nonstructural Proteins / physiology*
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Virus Replication / immunology
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Virus Replication / physiology*
Substances
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NS2 protein, human respiratory syncytial virus
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Viral Nonstructural Proteins
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OASL protein, human
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Oasl1 protein, mouse
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Oasl2 protein, mouse
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2',5'-Oligoadenylate Synthetase
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Proteasome Endopeptidase Complex