Structural model of the SARS coronavirus E channel in LMPG micelles.
Identifieur interne : 002F07 ( Ncbi/Merge ); précédent : 002F06; suivant : 002F08Structural model of the SARS coronavirus E channel in LMPG micelles.
Auteurs : Wahyu Surya [Singapour] ; Yan Li [Singapour] ; Jaume Torres [Singapour]Source :
- Biochimica et biophysica acta. Biomembranes [ 0005-2736 ] ; 2018.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Phosphatidylglycerols, Viral Envelope Proteins.
- chemical : Micelles.
- chemistry : SARS Virus.
- Electrophoresis, Polyacrylamide Gel, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Structure-Activity Relationship.
Abstract
Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.
DOI: 10.1016/j.bbamem.2018.02.017
PubMed: 29474890
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Electronic address: jtorres@ntu.edu.sg.</nlm:affiliation><country xml:lang="fr">Singapour</country><wicri:regionArea>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551</wicri:regionArea><wicri:noRegion>Singapore 637551</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. 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A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29474890</PMID><DateCompleted><Year>2018</Year><Month>08</Month><Day>14</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0005-2736</ISSN><JournalIssue CitedMedium="Print"><Volume>1860</Volume><Issue>6</Issue><PubDate><Year>2018</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Biomembranes</Title><ISOAbbreviation>Biochim Biophys Acta Biomembr</ISOAbbreviation></Journal><ArticleTitle>Structural model of the SARS coronavirus E channel in LMPG micelles.</ArticleTitle><Pagination><MedlinePgn>1309-1317</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0005-2736(18)30058-0</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbamem.2018.02.017</ELocationID><Abstract><AbstractText>Coronaviruses (CoV) cause common colds in humans, but are also responsible for the recent Severe Acute, and Middle East, respiratory syndromes (SARS and MERS, respectively). A promising approach for prevention are live attenuated vaccines (LAVs), some of which target the envelope (E) protein, which is a small membrane protein that forms ion channels. Unfortunately, detailed structural information is still limited for SARS-CoV E, and non-existent for other CoV E proteins. Herein, we report a structural model of a SARS-CoV E construct in LMPG micelles with, for the first time, unequivocal intermolecular NOEs. The model corresponding to the detergent-embedded region is consistent with previously obtained orientational restraints obtained in lipid bilayers and in vivo escape mutants. The C-terminal domain is mostly α-helical, and extramembrane intermolecular NOEs suggest interactions that may affect the TM channel conformation.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Surya</LastName><ForeName>Wahyu</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Yan</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Torres</LastName><ForeName>Jaume</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551, Singapore. Electronic address: jtorres@ntu.edu.sg.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>02</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Biomembr</MedlineTA><NlmUniqueID>101731713</NlmUniqueID><ISSNLinking>0005-2736</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008823">Micelles</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010715">Phosphatidylglycerols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope 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