Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2'-o-methyltransferase activity.
Identifieur interne : 001058 ( PubMed/Curation ); précédent : 001057; suivant : 001059Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2'-o-methyltransferase activity.
Auteurs : Vineet D. Menachery [États-Unis] ; Boyd L. Yount ; Laurence Josset ; Lisa E. Gralinski ; Trevor Scobey ; Sudhakar Agnihothram ; Michael G. Katze ; Ralph S. BaricSource :
- Journal of virology [ 1098-5514 ] ; 2014.
Descripteurs français
- KwdFr :
- Animaux, DEAD-box RNA helicases (génétique), DEAD-box RNA helicases (métabolisme), Femelle, Humains, Hélicase IFIH1 inductrice de l'interféron, Methyltransferases (), Methyltransferases (génétique), Methyltransferases (métabolisme), Motifs d'acides aminés, Mutation, Mâle, Protéines de liaison à l'ARN, Protéines de transport (génétique), Protéines de transport (métabolisme), Protéines virales non structurales (), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Réplication virale, Souris, Souris de lignée BALB C, Souris de lignée C57BL, Syndrome respiratoire aigu sévère (génétique), Syndrome respiratoire aigu sévère (métabolisme), Syndrome respiratoire aigu sévère (virologie), Virulence, Virus du SRAS (enzymologie), Virus du SRAS (génétique), Virus du SRAS (pathogénicité), Virus du SRAS (physiologie).
- MESH :
- enzymologie : Virus du SRAS.
- génétique : DEAD-box RNA helicases, Methyltransferases, Protéines de transport, Protéines virales non structurales, Syndrome respiratoire aigu sévère, Virus du SRAS.
- métabolisme : DEAD-box RNA helicases, Methyltransferases, Protéines de transport, Protéines virales non structurales, Syndrome respiratoire aigu sévère.
- pathogénicité : Virus du SRAS.
- physiologie : Virus du SRAS.
- virologie : Syndrome respiratoire aigu sévère.
- Animaux, Femelle, Humains, Hélicase IFIH1 inductrice de l'interféron, Methyltransferases, Motifs d'acides aminés, Mutation, Mâle, Protéines de liaison à l'ARN, Protéines virales non structurales, Réplication virale, Souris, Souris de lignée BALB C, Souris de lignée C57BL, Virulence.
English descriptors
- KwdEn :
- Amino Acid Motifs, Animals, Carrier Proteins (genetics), Carrier Proteins (metabolism), DEAD-box RNA Helicases (genetics), DEAD-box RNA Helicases (metabolism), Female, Humans, Interferon-Induced Helicase, IFIH1, Male, Methyltransferases (chemistry), Methyltransferases (genetics), Methyltransferases (metabolism), Mice, Mice, Inbred BALB C, Mice, Inbred C57BL, Mutation, RNA-Binding Proteins, SARS Virus (enzymology), SARS Virus (genetics), SARS Virus (pathogenicity), SARS Virus (physiology), Severe Acute Respiratory Syndrome (genetics), Severe Acute Respiratory Syndrome (metabolism), Severe Acute Respiratory Syndrome (virology), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Virulence, Virus Replication.
- MESH :
- chemical , chemistry : Methyltransferases, Viral Nonstructural Proteins.
- chemical , genetics : Carrier Proteins, DEAD-box RNA Helicases, Methyltransferases, Viral Nonstructural Proteins.
- chemical , metabolism : Carrier Proteins, DEAD-box RNA Helicases, Methyltransferases, Viral Nonstructural Proteins.
- enzymology : SARS Virus.
- genetics : SARS Virus, Severe Acute Respiratory Syndrome.
- metabolism : Severe Acute Respiratory Syndrome.
- pathogenicity : SARS Virus.
- physiology : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Motifs, Animals, Female, Humans, Interferon-Induced Helicase, IFIH1, Male, Mice, Mice, Inbred BALB C, Mice, Inbred C57BL, Mutation, RNA-Binding Proteins, Virulence, Virus Replication.
Abstract
The sudden emergence of severe acute respiratory syndrome coronavirus (SARS-CoV) in 2002 and, more recently, Middle Eastern respiratory syndrome CoV (MERS-CoV) underscores the importance of understanding critical aspects of CoV infection and pathogenesis. Despite significant insights into CoV cross-species transmission, replication, and virus-host interactions, successful therapeutic options for CoVs do not yet exist. Recent identification of SARS-CoV NSP16 as a viral 2'-O-methyltransferase (2'-O-MTase) led to the possibility of utilizing this pathway to both attenuate SARS-CoV infection and develop novel therapeutic treatment options. Mutations were introduced into SARS-CoV NSP16 within the conserved KDKE motif and effectively attenuated the resulting SARS-CoV mutant viruses both in vitro and in vivo. While viruses lacking 2'-O-MTase activity had enhanced sensitivity to type I interferon (IFN), they were not completely restored in their absence in vivo. However, the absence of either MDA5 or IFIT1, IFN-responsive genes that recognize unmethylated 2'-O RNA, resulted in restored replication and virulence of the dNSP16 mutant virus. Finally, using the mutant as a live-attenuated vaccine showed significant promise for possible therapeutic development against SARS-CoV. Together, the data underscore the necessity of 2'-O-MTase activity for SARS-CoV pathogenesis and identify host immune pathways that mediate this attenuation. In addition, we describe novel treatment avenues that exploit this pathway and could potentially be used against a diverse range of viral pathogens that utilize 2'-O-MTase activity to subvert the immune system.
DOI: 10.1128/JVI.03571-13
PubMed: 24478444
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pubmed:24478444Le document en format XML
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<term>Carrier Proteins (genetics)</term>
<term>Carrier Proteins (metabolism)</term>
<term>DEAD-box RNA Helicases (genetics)</term>
<term>DEAD-box RNA Helicases (metabolism)</term>
<term>Female</term>
<term>Humans</term>
<term>Interferon-Induced Helicase, IFIH1</term>
<term>Male</term>
<term>Methyltransferases (chemistry)</term>
<term>Methyltransferases (genetics)</term>
<term>Methyltransferases (metabolism)</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Mice, Inbred C57BL</term>
<term>Mutation</term>
<term>RNA-Binding Proteins</term>
<term>SARS Virus (enzymology)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (pathogenicity)</term>
<term>SARS Virus (physiology)</term>
<term>Severe Acute Respiratory Syndrome (genetics)</term>
<term>Severe Acute Respiratory Syndrome (metabolism)</term>
<term>Severe Acute Respiratory Syndrome (virology)</term>
<term>Viral Nonstructural Proteins (chemistry)</term>
<term>Viral Nonstructural Proteins (genetics)</term>
<term>Viral Nonstructural Proteins (metabolism)</term>
<term>Virulence</term>
<term>Virus Replication</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>DEAD-box RNA helicases (génétique)</term>
<term>DEAD-box RNA helicases (métabolisme)</term>
<term>Femelle</term>
<term>Humains</term>
<term>Hélicase IFIH1 inductrice de l'interféron</term>
<term>Methyltransferases ()</term>
<term>Methyltransferases (génétique)</term>
<term>Methyltransferases (métabolisme)</term>
<term>Motifs d'acides aminés</term>
<term>Mutation</term>
<term>Mâle</term>
<term>Protéines de liaison à l'ARN</term>
<term>Protéines de transport (génétique)</term>
<term>Protéines de transport (métabolisme)</term>
<term>Protéines virales non structurales ()</term>
<term>Protéines virales non structurales (génétique)</term>
<term>Protéines virales non structurales (métabolisme)</term>
<term>Réplication virale</term>
<term>Souris</term>
<term>Souris de lignée BALB C</term>
<term>Souris de lignée C57BL</term>
<term>Syndrome respiratoire aigu sévère (génétique)</term>
<term>Syndrome respiratoire aigu sévère (métabolisme)</term>
<term>Syndrome respiratoire aigu sévère (virologie)</term>
<term>Virulence</term>
<term>Virus du SRAS (enzymologie)</term>
<term>Virus du SRAS (génétique)</term>
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<term>Virus du SRAS (physiologie)</term>
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<term>Viral Nonstructural Proteins</term>
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<term>DEAD-box RNA Helicases</term>
<term>Methyltransferases</term>
<term>Viral Nonstructural Proteins</term>
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<term>DEAD-box RNA Helicases</term>
<term>Methyltransferases</term>
<term>Viral Nonstructural Proteins</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term>
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<term>Methyltransferases</term>
<term>Protéines de transport</term>
<term>Protéines virales non structurales</term>
<term>Syndrome respiratoire aigu sévère</term>
<term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>DEAD-box RNA helicases</term>
<term>Methyltransferases</term>
<term>Protéines de transport</term>
<term>Protéines virales non structurales</term>
<term>Syndrome respiratoire aigu sévère</term>
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<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Virus du SRAS</term>
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<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term>
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<keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Syndrome respiratoire aigu sévère</term>
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<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term>
<term>Animals</term>
<term>Female</term>
<term>Humans</term>
<term>Interferon-Induced Helicase, IFIH1</term>
<term>Male</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
<term>Mice, Inbred C57BL</term>
<term>Mutation</term>
<term>RNA-Binding Proteins</term>
<term>Virulence</term>
<term>Virus Replication</term>
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<term>Femelle</term>
<term>Humains</term>
<term>Hélicase IFIH1 inductrice de l'interféron</term>
<term>Methyltransferases</term>
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<front><div type="abstract" xml:lang="en">The sudden emergence of severe acute respiratory syndrome coronavirus (SARS-CoV) in 2002 and, more recently, Middle Eastern respiratory syndrome CoV (MERS-CoV) underscores the importance of understanding critical aspects of CoV infection and pathogenesis. Despite significant insights into CoV cross-species transmission, replication, and virus-host interactions, successful therapeutic options for CoVs do not yet exist. Recent identification of SARS-CoV NSP16 as a viral 2'-O-methyltransferase (2'-O-MTase) led to the possibility of utilizing this pathway to both attenuate SARS-CoV infection and develop novel therapeutic treatment options. Mutations were introduced into SARS-CoV NSP16 within the conserved KDKE motif and effectively attenuated the resulting SARS-CoV mutant viruses both in vitro and in vivo. While viruses lacking 2'-O-MTase activity had enhanced sensitivity to type I interferon (IFN), they were not completely restored in their absence in vivo. However, the absence of either MDA5 or IFIT1, IFN-responsive genes that recognize unmethylated 2'-O RNA, resulted in restored replication and virulence of the dNSP16 mutant virus. Finally, using the mutant as a live-attenuated vaccine showed significant promise for possible therapeutic development against SARS-CoV. Together, the data underscore the necessity of 2'-O-MTase activity for SARS-CoV pathogenesis and identify host immune pathways that mediate this attenuation. In addition, we describe novel treatment avenues that exploit this pathway and could potentially be used against a diverse range of viral pathogens that utilize 2'-O-MTase activity to subvert the immune system.</div>
</front>
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<DateCompleted><Year>2014</Year>
<Month>06</Month>
<Day>24</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>04</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>88</Volume>
<Issue>8</Issue>
<PubDate><Year>2014</Year>
<Month>Apr</Month>
</PubDate>
</JournalIssue>
<Title>Journal of virology</Title>
<ISOAbbreviation>J. Virol.</ISOAbbreviation>
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<ArticleTitle>Attenuation and restoration of severe acute respiratory syndrome coronavirus mutant lacking 2'-o-methyltransferase activity.</ArticleTitle>
<Pagination><MedlinePgn>4251-64</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.03571-13</ELocationID>
<Abstract><AbstractText Label="UNLABELLED">The sudden emergence of severe acute respiratory syndrome coronavirus (SARS-CoV) in 2002 and, more recently, Middle Eastern respiratory syndrome CoV (MERS-CoV) underscores the importance of understanding critical aspects of CoV infection and pathogenesis. Despite significant insights into CoV cross-species transmission, replication, and virus-host interactions, successful therapeutic options for CoVs do not yet exist. Recent identification of SARS-CoV NSP16 as a viral 2'-O-methyltransferase (2'-O-MTase) led to the possibility of utilizing this pathway to both attenuate SARS-CoV infection and develop novel therapeutic treatment options. Mutations were introduced into SARS-CoV NSP16 within the conserved KDKE motif and effectively attenuated the resulting SARS-CoV mutant viruses both in vitro and in vivo. While viruses lacking 2'-O-MTase activity had enhanced sensitivity to type I interferon (IFN), they were not completely restored in their absence in vivo. However, the absence of either MDA5 or IFIT1, IFN-responsive genes that recognize unmethylated 2'-O RNA, resulted in restored replication and virulence of the dNSP16 mutant virus. Finally, using the mutant as a live-attenuated vaccine showed significant promise for possible therapeutic development against SARS-CoV. Together, the data underscore the necessity of 2'-O-MTase activity for SARS-CoV pathogenesis and identify host immune pathways that mediate this attenuation. In addition, we describe novel treatment avenues that exploit this pathway and could potentially be used against a diverse range of viral pathogens that utilize 2'-O-MTase activity to subvert the immune system.</AbstractText>
<AbstractText Label="IMPORTANCE" NlmCategory="OBJECTIVE">Preventing recognition by the host immune response represents a critical aspect necessary for successful viral infection. Several viruses, including SARS-CoV, utilize virally encoded 2'-O-MTases to camouflage and obscure their viral RNA from host cell sensing machinery, thus preventing recognition and activation of cell intrinsic defense pathways. For SARS-CoV, the absence of this 2'-O-MTase activity results in significant attenuation characterized by decreased viral replication, reduced weight loss, and limited breathing dysfunction in mice. The results indicate that both MDA5, a recognition molecule, and the IFIT family play an important role in mediating this attenuation with restored virulence observed in their absence. Understanding this virus-host interaction provided an opportunity to design a successful live-attenuated vaccine for SARS-CoV and opens avenues for treatment and prevention of emerging CoVs and other RNA virus infections.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Menachery</LastName>
<ForeName>Vineet D</ForeName>
<Initials>VD</Initials>
<AffiliationInfo><Affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yount</LastName>
<ForeName>Boyd L</ForeName>
<Initials>BL</Initials>
<Suffix>Jr</Suffix>
</Author>
<Author ValidYN="Y"><LastName>Josset</LastName>
<ForeName>Laurence</ForeName>
<Initials>L</Initials>
</Author>
<Author ValidYN="Y"><LastName>Gralinski</LastName>
<ForeName>Lisa E</ForeName>
<Initials>LE</Initials>
</Author>
<Author ValidYN="Y"><LastName>Scobey</LastName>
<ForeName>Trevor</ForeName>
<Initials>T</Initials>
</Author>
<Author ValidYN="Y"><LastName>Agnihothram</LastName>
<ForeName>Sudhakar</ForeName>
<Initials>S</Initials>
</Author>
<Author ValidYN="Y"><LastName>Katze</LastName>
<ForeName>Michael G</ForeName>
<Initials>MG</Initials>
</Author>
<Author ValidYN="Y"><LastName>Baric</LastName>
<ForeName>Ralph S</ForeName>
<Initials>RS</Initials>
</Author>
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<Language>eng</Language>
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<MedlineTA>J Virol</MedlineTA>
<NlmUniqueID>0113724</NlmUniqueID>
<ISSNLinking>0022-538X</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D002352">Carrier Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C092573">Ifit1 protein, mouse</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D016601">RNA-Binding Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber>
<NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance>
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<Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber>
<NameOfSubstance UI="C558879">Nsp16 protein, SARS virus</NameOfSubstance>
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<Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber>
<NameOfSubstance UI="C510592">Ifih1 protein, mouse</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.6.4.13</RegistryNumber>
<NameOfSubstance UI="D053487">DEAD-box RNA Helicases</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.6.4.13</RegistryNumber>
<NameOfSubstance UI="D000072640">Interferon-Induced Helicase, IFIH1</NameOfSubstance>
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