Coronavirus non-structural protein 16: evasion, attenuation, and possible treatments.
Identifieur interne : 001828 ( PubMed/Corpus ); précédent : 001827; suivant : 001829Coronavirus non-structural protein 16: evasion, attenuation, and possible treatments.
Auteurs : Vineet D. Menachery ; Kari Debbink ; Ralph S. BaricSource :
- Virus research [ 1872-7492 ] ; 2014.
English descriptors
- KwdEn :
- Coronavirus Infections (immunology), Coronavirus Infections (virology), Humans, Methyltransferases (genetics), Methyltransferases (immunology), Methyltransferases (metabolism), Middle East Respiratory Syndrome Coronavirus (enzymology), Middle East Respiratory Syndrome Coronavirus (genetics), Middle East Respiratory Syndrome Coronavirus (physiology), SARS Virus (enzymology), SARS Virus (genetics), SARS Virus (physiology), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (immunology), Viral Nonstructural Proteins (metabolism), Virus Replication.
- MESH :
- chemical , genetics : Methyltransferases, Viral Nonstructural Proteins.
- enzymology : Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- genetics : Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- immunology : Coronavirus Infections, Methyltransferases, Viral Nonstructural Proteins.
- chemical , metabolism : Methyltransferases, Viral Nonstructural Proteins.
- physiology : Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- virology : Coronavirus Infections.
- Humans, Virus Replication.
Abstract
The recent emergence of Middle East Respiratory Syndrome Coronavirus (MERS-CoV), nearly a decade after the Severe Acute Respiratory Syndrome (SARS) CoV, highlights the importance of understanding and developing therapeutic treatment for current and emergent CoVs. This manuscript explores the role of NSP16, a 2'O-methyl-transferase (2'O-MTase), in CoV infection and the host immune response. The review highlights conserved motifs, required interaction partners, as well as the attenuation of NSP16 mutants, and restoration of these mutants in specific immune knockouts. Importantly, the work also identifies a number of approaches to exploit this understanding for therapeutic treatment and the data clearly illustrate the importance of NSP16 2'O-MTase activity for CoV infection and pathogenesis.
DOI: 10.1016/j.virusres.2014.09.009
PubMed: 25278144
Links to Exploration step
pubmed:25278144Le document en format XML
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Electronic address: vineet@email.unc.edu.</nlm:affiliation></affiliation></author><author><name sortKey="Debbink, Kari" sort="Debbink, Kari" uniqKey="Debbink K" first="Kari" last="Debbink">Kari Debbink</name><affiliation><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599, USA; Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, NC 27599, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. 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Menachery</name><affiliation><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599, USA. Electronic address: vineet@email.unc.edu.</nlm:affiliation></affiliation></author><author><name sortKey="Debbink, Kari" sort="Debbink, Kari" uniqKey="Debbink K" first="Kari" last="Debbink">Kari Debbink</name><affiliation><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, NC 27599, USA; Department of Microbiology and Immunology, University of North Carolina, Chapel Hill, NC 27599, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. 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This manuscript explores the role of NSP16, a 2'O-methyl-transferase (2'O-MTase), in CoV infection and the host immune response. The review highlights conserved motifs, required interaction partners, as well as the attenuation of NSP16 mutants, and restoration of these mutants in specific immune knockouts. Importantly, the work also identifies a number of approaches to exploit this understanding for therapeutic treatment and the data clearly illustrate the importance of NSP16 2'O-MTase activity for CoV infection and pathogenesis. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25278144</PMID><DateCompleted><Year>2015</Year><Month>07</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-7492</ISSN><JournalIssue CitedMedium="Internet"><Volume>194</Volume><PubDate><Year>2014</Year><Month>Dec</Month><Day>19</Day></PubDate></JournalIssue><Title>Virus research</Title><ISOAbbreviation>Virus Res.</ISOAbbreviation></Journal><ArticleTitle>Coronavirus non-structural protein 16: evasion, attenuation, and possible treatments.</ArticleTitle><Pagination><MedlinePgn>191-9</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virusres.2014.09.009</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0168-1702(14)00396-7</ELocationID><Abstract><AbstractText>The recent emergence of Middle East Respiratory Syndrome Coronavirus (MERS-CoV), nearly a decade after the Severe Acute Respiratory Syndrome (SARS) CoV, highlights the importance of understanding and developing therapeutic treatment for current and emergent CoVs. This manuscript explores the role of NSP16, a 2'O-methyl-transferase (2'O-MTase), in CoV infection and the host immune response. The review highlights conserved motifs, required interaction partners, as well as the attenuation of NSP16 mutants, and restoration of these mutants in specific immune knockouts. Importantly, the work also identifies a number of approaches to exploit this understanding for therapeutic treatment and the data clearly illustrate the importance of NSP16 2'O-MTase activity for CoV infection and pathogenesis. </AbstractText><CopyrightInformation>Copyright © 2014. Published by Elsevier B.V.</CopyrightInformation></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, NC 27599, USA. 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