The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.
Identifieur interne : 000104 ( PubMed/Curation ); précédent : 000103; suivant : 000105The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.
Auteurs : Qingliang Shen [États-Unis] ; Jae-Hyun Cho [États-Unis]Source :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Mutant Proteins, Viral Nonstructural Proteins.
- metabolism : Influenza A virus, Viral Nonstructural Proteins.
- Influenza Pandemic, 1918-1919, Models, Molecular, Protein Conformation, Solutions.
Abstract
Nonstructural protein 1 (NS1) is a multifunctional virulence factor of influenza virus. The effector domain (ED) of influenza viruses is capable of binding to a variety of host factors, however, the molecular basis of the interactions remains to be investigated. The isolated NS1-ED exists in equilibrium between the monomer and homodimer. Although the structural diversity of the dimer interface has been well-characterized, limited information is available regarding the internal conformational heterogeneity of the monomeric NS1-ED. Here, we present the solution NMR structure of the NS1-ED W187R of the 1918 influenza A virus, which caused the "Spanish flu." Structural plasticity is an essential property to understand the molecular mechanism by which NS1-ED interacts with multiple host proteins. Structural comparison with the NS1-ED from influenza A/Udorn/1972 (Ud) strain revealed a similar overall structure but a distinct conformational variation and flexibility. Our results suggest that conformational flexibility of the NS1-ED might differ depending on the influenza strain.
DOI: 10.1016/j.bbrc.2019.08.027
PubMed: 31420169
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The effector domain (ED) of influenza viruses is capable of binding to a variety of host factors, however, the molecular basis of the interactions remains to be investigated. The isolated NS1-ED exists in equilibrium between the monomer and homodimer. Although the structural diversity of the dimer interface has been well-characterized, limited information is available regarding the internal conformational heterogeneity of the monomeric NS1-ED. Here, we present the solution NMR structure of the NS1-ED W187R of the 1918 influenza A virus, which caused the "Spanish flu." Structural plasticity is an essential property to understand the molecular mechanism by which NS1-ED interacts with multiple host proteins. Structural comparison with the NS1-ED from influenza A/Udorn/1972 (Ud) strain revealed a similar overall structure but a distinct conformational variation and flexibility. Our results suggest that conformational flexibility of the NS1-ED might differ depending on the influenza strain.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31420169</PMID><DateCompleted><Year>2020</Year><Month>06</Month><Day>01</Day></DateCompleted><DateRevised><Year>2020</Year><Month>06</Month><Day>01</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>518</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>10</Month><Day>08</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem. Biophys. Res. Commun.</ISOAbbreviation></Journal><ArticleTitle>The structure and conformational plasticity of the nonstructural protein 1 of the 1918 influenza A virus.</ArticleTitle><Pagination><MedlinePgn>178-182</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0006-291X(19)31538-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2019.08.027</ELocationID><Abstract><AbstractText>Nonstructural protein 1 (NS1) is a multifunctional virulence factor of influenza virus. The effector domain (ED) of influenza viruses is capable of binding to a variety of host factors, however, the molecular basis of the interactions remains to be investigated. The isolated NS1-ED exists in equilibrium between the monomer and homodimer. Although the structural diversity of the dimer interface has been well-characterized, limited information is available regarding the internal conformational heterogeneity of the monomeric NS1-ED. Here, we present the solution NMR structure of the NS1-ED W187R of the 1918 influenza A virus, which caused the "Spanish flu." Structural plasticity is an essential property to understand the molecular mechanism by which NS1-ED interacts with multiple host proteins. Structural comparison with the NS1-ED from influenza A/Udorn/1972 (Ud) strain revealed a similar overall structure but a distinct conformational variation and flexibility. Our results suggest that conformational flexibility of the NS1-ED might differ depending on the influenza strain.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Shen</LastName><ForeName>Qingliang</ForeName><Initials>Q</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cho</LastName><ForeName>Jae-Hyun</ForeName><Initials>JH</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX, 77843, USA. 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