Message in a bottle: lessons learned from antagonism of STING signalling during RNA virus infection.
Identifieur interne : 000F33 ( PubMed/Corpus ); précédent : 000F32; suivant : 000F34Message in a bottle: lessons learned from antagonism of STING signalling during RNA virus infection.
Auteurs : Kevin Maringer ; Ana Fernandez-SesmaSource :
- Cytokine & growth factor reviews [ 1879-0305 ] ; 2014.
English descriptors
- KwdEn :
- Animals, Coronavirus NL63, Human (genetics), Coronavirus NL63, Human (immunology), Dengue (genetics), Dengue (immunology), Dengue Virus (genetics), Dengue Virus (immunology), Humans, Membrane Proteins (genetics), Membrane Proteins (immunology), Mice, Nucleotidyltransferases (genetics), Nucleotidyltransferases (immunology), SARS Virus (genetics), SARS Virus (immunology), Severe Acute Respiratory Syndrome (genetics), Severe Acute Respiratory Syndrome (immunology), Signal Transduction (genetics), Signal Transduction (immunology), Viral Proteins (genetics), Viral Proteins (immunology).
- MESH :
- chemical , genetics : Membrane Proteins, Nucleotidyltransferases, Viral Proteins.
- genetics : Coronavirus NL63, Human, Dengue, Dengue Virus, SARS Virus, Severe Acute Respiratory Syndrome, Signal Transduction.
- immunology : Coronavirus NL63, Human, Dengue, Dengue Virus, Membrane Proteins, Nucleotidyltransferases, SARS Virus, Severe Acute Respiratory Syndrome, Signal Transduction, Viral Proteins.
- Animals, Humans, Mice.
Abstract
STING has emerged in recent years as an important signalling adaptor in the activation of type I interferon responses during infection with DNA viruses and bacteria. An increasing body of evidence suggests that STING also modulates responses to RNA viruses, though the mechanisms remain less clear. In this review, we give a brief overview of the ways in which STING facilitates sensing of RNA viruses. These include modulation of RIG-I-dependent responses through STING's interaction with MAVS, and more speculative mechanisms involving the DNA sensor cGAS and sensing of membrane remodelling events. We then provide an in-depth literature review to summarise the known mechanisms by which RNA viruses of the families Flaviviridae and Coronaviridae evade sensing through STING. Our own work has shown that the NS2B/3 protease complex of the flavivirus dengue virus binds and cleaves STING, and that an inability to degrade murine STING may contribute to host restriction in this virus. We contrast this to the mechanism employed by the distantly related hepacivirus hepatitis C virus, in which STING is bound and inactivated by the NS4B protein. Finally, we discuss STING antagonism in the coronaviruses SARS coronavirus and human coronavirus NL63, which disrupt K63-linked polyubiquitination and dimerisation of STING (both of which are required for STING-mediated activation of IRF-3) via their papain-like proteases. We draw parallels with less-well characterised mechanisms of STING antagonism in related viruses, and place our current knowledge in the context of species tropism restrictions that potentially affect the emergence of new human pathogens.
DOI: 10.1016/j.cytogfr.2014.08.004
PubMed: 25212897
Links to Exploration step
pubmed:25212897Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Message in a bottle: lessons learned from antagonism of STING signalling during RNA virus infection.</title><author><name sortKey="Maringer, Kevin" sort="Maringer, Kevin" uniqKey="Maringer K" first="Kevin" last="Maringer">Kevin Maringer</name><affiliation><nlm:affiliation>Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA; School of Cellular and Molecular Medicine, School of Medical Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom.</nlm:affiliation></affiliation></author><author><name sortKey="Fernandez Sesma, Ana" sort="Fernandez Sesma, Ana" uniqKey="Fernandez Sesma A" first="Ana" last="Fernandez-Sesma">Ana Fernandez-Sesma</name><affiliation><nlm:affiliation>Department of Microbiology, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA. 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Electronic address: ana.sesma@mssm.edu.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Cytokine & growth factor reviews</title><idno type="eISSN">1879-0305</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Coronavirus NL63, Human (genetics)</term><term>Coronavirus NL63, Human (immunology)</term><term>Dengue (genetics)</term><term>Dengue (immunology)</term><term>Dengue Virus (genetics)</term><term>Dengue Virus (immunology)</term><term>Humans</term><term>Membrane Proteins (genetics)</term><term>Membrane Proteins (immunology)</term><term>Mice</term><term>Nucleotidyltransferases (genetics)</term><term>Nucleotidyltransferases (immunology)</term><term>SARS Virus (genetics)</term><term>SARS Virus (immunology)</term><term>Severe Acute Respiratory Syndrome (genetics)</term><term>Severe Acute Respiratory Syndrome (immunology)</term><term>Signal Transduction (genetics)</term><term>Signal Transduction (immunology)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (immunology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Proteins</term><term>Nucleotidyltransferases</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coronavirus NL63, Human</term><term>Dengue</term><term>Dengue Virus</term><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Coronavirus NL63, Human</term><term>Dengue</term><term>Dengue Virus</term><term>Membrane Proteins</term><term>Nucleotidyltransferases</term><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term><term>Signal Transduction</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Mice</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">STING has emerged in recent years as an important signalling adaptor in the activation of type I interferon responses during infection with DNA viruses and bacteria. An increasing body of evidence suggests that STING also modulates responses to RNA viruses, though the mechanisms remain less clear. In this review, we give a brief overview of the ways in which STING facilitates sensing of RNA viruses. These include modulation of RIG-I-dependent responses through STING's interaction with MAVS, and more speculative mechanisms involving the DNA sensor cGAS and sensing of membrane remodelling events. We then provide an in-depth literature review to summarise the known mechanisms by which RNA viruses of the families Flaviviridae and Coronaviridae evade sensing through STING. Our own work has shown that the NS2B/3 protease complex of the flavivirus dengue virus binds and cleaves STING, and that an inability to degrade murine STING may contribute to host restriction in this virus. We contrast this to the mechanism employed by the distantly related hepacivirus hepatitis C virus, in which STING is bound and inactivated by the NS4B protein. Finally, we discuss STING antagonism in the coronaviruses SARS coronavirus and human coronavirus NL63, which disrupt K63-linked polyubiquitination and dimerisation of STING (both of which are required for STING-mediated activation of IRF-3) via their papain-like proteases. We draw parallels with less-well characterised mechanisms of STING antagonism in related viruses, and place our current knowledge in the context of species tropism restrictions that potentially affect the emergence of new human pathogens. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25212897</PMID><DateCompleted><Year>2015</Year><Month>07</Month><Day>29</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>27</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0305</ISSN><JournalIssue CitedMedium="Internet"><Volume>25</Volume><Issue>6</Issue><PubDate><Year>2014</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Cytokine & growth factor reviews</Title><ISOAbbreviation>Cytokine Growth Factor Rev.</ISOAbbreviation></Journal><ArticleTitle>Message in a bottle: lessons learned from antagonism of STING signalling during RNA virus infection.</ArticleTitle><Pagination><MedlinePgn>669-79</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.cytogfr.2014.08.004</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S1359-6101(14)00087-2</ELocationID><Abstract><AbstractText>STING has emerged in recent years as an important signalling adaptor in the activation of type I interferon responses during infection with DNA viruses and bacteria. An increasing body of evidence suggests that STING also modulates responses to RNA viruses, though the mechanisms remain less clear. In this review, we give a brief overview of the ways in which STING facilitates sensing of RNA viruses. These include modulation of RIG-I-dependent responses through STING's interaction with MAVS, and more speculative mechanisms involving the DNA sensor cGAS and sensing of membrane remodelling events. We then provide an in-depth literature review to summarise the known mechanisms by which RNA viruses of the families Flaviviridae and Coronaviridae evade sensing through STING. Our own work has shown that the NS2B/3 protease complex of the flavivirus dengue virus binds and cleaves STING, and that an inability to degrade murine STING may contribute to host restriction in this virus. We contrast this to the mechanism employed by the distantly related hepacivirus hepatitis C virus, in which STING is bound and inactivated by the NS4B protein. Finally, we discuss STING antagonism in the coronaviruses SARS coronavirus and human coronavirus NL63, which disrupt K63-linked polyubiquitination and dimerisation of STING (both of which are required for STING-mediated activation of IRF-3) via their papain-like proteases. We draw parallels with less-well characterised mechanisms of STING antagonism in related viruses, and place our current knowledge in the context of species tropism restrictions that potentially affect the emergence of new human pathogens. </AbstractText><CopyrightInformation>Copyright © 2014 The Authors. Published by Elsevier Ltd.. 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