Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus.
Identifieur interne : 001A69 ( PubMed/Corpus ); précédent : 001A68; suivant : 001A70Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus.
Auteurs : Yi-Ching Hsieh ; Hui-Chun Li ; Shih-Chi Chen ; Shih-Yen LoSource :
- Journal of biomedical science [ 1423-0127 ] ; 2008.
English descriptors
- KwdEn :
- Animals, Chlorocebus aethiops, Gene Deletion, Protein Binding, Protein Interaction Mapping, SARS Virus (genetics), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (metabolism), Severe Acute Respiratory Syndrome (virology), Vero Cells, Viral Matrix Proteins (metabolism), Viral Structural Proteins (metabolism).
- MESH :
- chemical , metabolism : Viral Matrix Proteins, Viral Structural Proteins.
- genetics : SARS Virus.
- metabolism : SARS Virus, Severe Acute Respiratory Syndrome.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Chlorocebus aethiops, Gene Deletion, Protein Binding, Protein Interaction Mapping, Vero Cells.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) structural proteins (S, E, M, and NC) localize in different subcellular positions when expressed individually. However, SARS-CoV M protein is co-localized almost entirely with S, E, or NC protein when co-expressed in the cells. On the other hand, only partial co-localization was observed when S and E, S and NC, or E and NC were co-expressed in the cells. Interactions between SARS-CoV M and other structural proteins but not interactions between S and E, S and NC, or E and NC were further demonstrated by co-immunoprecipitation assay. These results indicate that SARS-CoV M protein, similar to the M proteins of other coronaviruses, plays a pivotal role in virus assembly. The cytoplasmic C-terminus domain of SARS-CoV M protein was responsible for binding to NC protein. Multiple regions of M protein interacted with E and S proteins. A model for the interactions between SARS-CoV M protein and other structural proteins is proposed. This study helps us better understand protein-protein interactions during viral assembly of SARS-CoV.
DOI: 10.1007/s11373-008-9278-3
PubMed: 18792806
Links to Exploration step
pubmed:18792806Le document en format XML
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However, SARS-CoV M protein is co-localized almost entirely with S, E, or NC protein when co-expressed in the cells. On the other hand, only partial co-localization was observed when S and E, S and NC, or E and NC were co-expressed in the cells. Interactions between SARS-CoV M and other structural proteins but not interactions between S and E, S and NC, or E and NC were further demonstrated by co-immunoprecipitation assay. These results indicate that SARS-CoV M protein, similar to the M proteins of other coronaviruses, plays a pivotal role in virus assembly. The cytoplasmic C-terminus domain of SARS-CoV M protein was responsible for binding to NC protein. Multiple regions of M protein interacted with E and S proteins. A model for the interactions between SARS-CoV M protein and other structural proteins is proposed. This study helps us better understand protein-protein interactions during viral assembly of SARS-CoV.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18792806</PMID><DateCompleted><Year>2009</Year><Month>02</Month><Day>06</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1423-0127</ISSN><JournalIssue CitedMedium="Internet"><Volume>15</Volume><Issue>6</Issue><PubDate><Year>2008</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Journal of biomedical science</Title><ISOAbbreviation>J. Biomed. Sci.</ISOAbbreviation></Journal><ArticleTitle>Interactions between M protein and other structural proteins of severe, acute respiratory syndrome-associated coronavirus.</ArticleTitle><Pagination><MedlinePgn>707-17</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s11373-008-9278-3</ELocationID><Abstract><AbstractText>Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) structural proteins (S, E, M, and NC) localize in different subcellular positions when expressed individually. However, SARS-CoV M protein is co-localized almost entirely with S, E, or NC protein when co-expressed in the cells. On the other hand, only partial co-localization was observed when S and E, S and NC, or E and NC were co-expressed in the cells. Interactions between SARS-CoV M and other structural proteins but not interactions between S and E, S and NC, or E and NC were further demonstrated by co-immunoprecipitation assay. These results indicate that SARS-CoV M protein, similar to the M proteins of other coronaviruses, plays a pivotal role in virus assembly. The cytoplasmic C-terminus domain of SARS-CoV M protein was responsible for binding to NC protein. Multiple regions of M protein interacted with E and S proteins. A model for the interactions between SARS-CoV M protein and other structural proteins is proposed. This study helps us better understand protein-protein interactions during viral assembly of SARS-CoV.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hsieh</LastName><ForeName>Yi-Ching</ForeName><Initials>YC</Initials><AffiliationInfo><Affiliation>Graduate Institute of Molecular and Cellular Biology, Tzu Chi University, 701, Section 3, Chung Yang Road, Hualien, Taiwan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Hui-Chun</ForeName><Initials>HC</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Shih-Chi</ForeName><Initials>SC</Initials></Author><Author ValidYN="Y"><LastName>Lo</LastName><ForeName>Shih-Yen</ForeName><Initials>SY</Initials></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>2008</Year><Month>09</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Biomed Sci</MedlineTA><NlmUniqueID>9421567</NlmUniqueID><ISSNLinking>1021-7770</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014763">Viral Matrix Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015678">Viral Structural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>108502-71-2</RegistryNumber><NameOfSubstance UI="C067997">M protein, Coronavirus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002522" MajorTopicYN="N">Chlorocebus aethiops</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017353" 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