The M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles.
Identifieur interne : 001A77 ( PubMed/Corpus ); précédent : 001A76; suivant : 001A78The M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles.
Auteurs : Y L Siu ; K T Teoh ; J. Lo ; C M Chan ; F. Kien ; N. Escriou ; S W Tsao ; J M Nicholls ; R. Altmeyer ; J S M. Peiris ; R. Bruzzone ; B. NalSource :
- Journal of virology [ 1098-5514 ] ; 2008.
English descriptors
- KwdEn :
- Animals, Chlorocebus aethiops, Humans, Membrane Glycoproteins (metabolism), Microscopy, Electron, Transmission, Nucleocapsid Proteins (genetics), Nucleocapsid Proteins (metabolism), SARS Virus (physiology), Spike Glycoprotein, Coronavirus, Vero Cells, Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism), Virosomes (metabolism), Virosomes (ultrastructure), Virus Assembly.
- MESH :
- chemical , genetics : Nucleocapsid Proteins, Viral Envelope Proteins, Viral Matrix Proteins.
- chemical , metabolism : Membrane Glycoproteins, Nucleocapsid Proteins, Viral Envelope Proteins, Viral Matrix Proteins, Virosomes.
- physiology : SARS Virus.
- chemical , ultrastructure : Virosomes.
- Animals, Chlorocebus aethiops, Humans, Microscopy, Electron, Transmission, Spike Glycoprotein, Coronavirus, Vero Cells, Virus Assembly.
Abstract
The production of virus-like particles (VLPs) constitutes a relevant and safe model to study molecular determinants of virion egress. The minimal requirement for the assembly of VLPs for the coronavirus responsible for severe acute respiratory syndrome in humans (SARS-CoV) is still controversial. Recent studies have shown that SARS-CoV VLP formation depends on either M and E proteins or M and N proteins. Here we show that both E and N proteins must be coexpressed with M protein for the efficient production and release of VLPs by transfected Vero E6 cells. This suggests that the mechanism of SARS-CoV assembly differs from that of other studied coronaviruses, which only require M and E proteins for VLP formation. When coexpressed, the native envelope trimeric S glycoprotein is incorporated onto VLPs. Interestingly, when a fluorescent protein tag is added to the C-terminal end of N or S protein, but not M protein, the chimeric viral proteins can be assembled within VLPs and allow visualization of VLP production and trafficking in living cells by state-of-the-art imaging technologies. Fluorescent VLPs will be used further to investigate the role of cellular machineries during SARS-CoV egress.
DOI: 10.1128/JVI.01052-08
PubMed: 18753196
Links to Exploration step
pubmed:18753196Le document en format XML
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Nal</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18753196</idno><idno type="pmid">18753196</idno><idno type="doi">10.1128/JVI.01052-08</idno><idno type="wicri:Area/PubMed/Corpus">001A77</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001A77</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles.</title><author><name sortKey="Siu, Y L" sort="Siu, Y L" uniqKey="Siu Y" first="Y L" last="Siu">Y L Siu</name><affiliation><nlm:affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong SAR, China.</nlm:affiliation></affiliation></author><author><name sortKey="Teoh, K T" sort="Teoh, K T" uniqKey="Teoh K" first="K T" last="Teoh">K T Teoh</name></author><author><name sortKey="Lo, J" sort="Lo, J" uniqKey="Lo J" first="J" last="Lo">J. Lo</name></author><author><name sortKey="Chan, C M" sort="Chan, C M" uniqKey="Chan C" first="C M" last="Chan">C M Chan</name></author><author><name sortKey="Kien, F" sort="Kien, F" uniqKey="Kien F" first="F" last="Kien">F. Kien</name></author><author><name sortKey="Escriou, N" sort="Escriou, N" uniqKey="Escriou N" first="N" last="Escriou">N. Escriou</name></author><author><name sortKey="Tsao, S W" sort="Tsao, S W" uniqKey="Tsao S" first="S W" last="Tsao">S W Tsao</name></author><author><name sortKey="Nicholls, J M" sort="Nicholls, J M" uniqKey="Nicholls J" first="J M" last="Nicholls">J M Nicholls</name></author><author><name sortKey="Altmeyer, R" sort="Altmeyer, R" uniqKey="Altmeyer R" first="R" last="Altmeyer">R. Altmeyer</name></author><author><name sortKey="Peiris, J S M" sort="Peiris, J S M" uniqKey="Peiris J" first="J S M" last="Peiris">J S M. Peiris</name></author><author><name sortKey="Bruzzone, R" sort="Bruzzone, R" uniqKey="Bruzzone R" first="R" last="Bruzzone">R. Bruzzone</name></author><author><name sortKey="Nal, B" sort="Nal, B" uniqKey="Nal B" first="B" last="Nal">B. Nal</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Membrane Glycoproteins (metabolism)</term><term>Microscopy, Electron, Transmission</term><term>Nucleocapsid Proteins (genetics)</term><term>Nucleocapsid Proteins (metabolism)</term><term>SARS Virus (physiology)</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term><term>Viral Matrix Proteins (genetics)</term><term>Viral Matrix Proteins (metabolism)</term><term>Virosomes (metabolism)</term><term>Virosomes (ultrastructure)</term><term>Virus Assembly</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Nucleocapsid Proteins</term><term>Viral Envelope Proteins</term><term>Viral Matrix Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Nucleocapsid Proteins</term><term>Viral Envelope Proteins</term><term>Viral Matrix Proteins</term><term>Virosomes</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Virosomes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Chlorocebus aethiops</term><term>Humans</term><term>Microscopy, Electron, Transmission</term><term>Spike Glycoprotein, Coronavirus</term><term>Vero Cells</term><term>Virus Assembly</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The production of virus-like particles (VLPs) constitutes a relevant and safe model to study molecular determinants of virion egress. The minimal requirement for the assembly of VLPs for the coronavirus responsible for severe acute respiratory syndrome in humans (SARS-CoV) is still controversial. Recent studies have shown that SARS-CoV VLP formation depends on either M and E proteins or M and N proteins. Here we show that both E and N proteins must be coexpressed with M protein for the efficient production and release of VLPs by transfected Vero E6 cells. This suggests that the mechanism of SARS-CoV assembly differs from that of other studied coronaviruses, which only require M and E proteins for VLP formation. When coexpressed, the native envelope trimeric S glycoprotein is incorporated onto VLPs. Interestingly, when a fluorescent protein tag is added to the C-terminal end of N or S protein, but not M protein, the chimeric viral proteins can be assembled within VLPs and allow visualization of VLP production and trafficking in living cells by state-of-the-art imaging technologies. Fluorescent VLPs will be used further to investigate the role of cellular machineries during SARS-CoV egress.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18753196</PMID><DateCompleted><Year>2008</Year><Month>11</Month><Day>10</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>82</Volume><Issue>22</Issue><PubDate><Year>2008</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>The M, E, and N structural proteins of the severe acute respiratory syndrome coronavirus are required for efficient assembly, trafficking, and release of virus-like particles.</ArticleTitle><Pagination><MedlinePgn>11318-30</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.01052-08</ELocationID><Abstract><AbstractText>The production of virus-like particles (VLPs) constitutes a relevant and safe model to study molecular determinants of virion egress. The minimal requirement for the assembly of VLPs for the coronavirus responsible for severe acute respiratory syndrome in humans (SARS-CoV) is still controversial. Recent studies have shown that SARS-CoV VLP formation depends on either M and E proteins or M and N proteins. Here we show that both E and N proteins must be coexpressed with M protein for the efficient production and release of VLPs by transfected Vero E6 cells. This suggests that the mechanism of SARS-CoV assembly differs from that of other studied coronaviruses, which only require M and E proteins for VLP formation. When coexpressed, the native envelope trimeric S glycoprotein is incorporated onto VLPs. Interestingly, when a fluorescent protein tag is added to the C-terminal end of N or S protein, but not M protein, the chimeric viral proteins can be assembled within VLPs and allow visualization of VLP production and trafficking in living cells by state-of-the-art imaging technologies. Fluorescent VLPs will be used further to investigate the role of cellular machineries during SARS-CoV egress.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Siu</LastName><ForeName>Y L</ForeName><Initials>YL</Initials><AffiliationInfo><Affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong SAR, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Teoh</LastName><ForeName>K T</ForeName><Initials>KT</Initials></Author><Author ValidYN="Y"><LastName>Lo</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Chan</LastName><ForeName>C M</ForeName><Initials>CM</Initials></Author><Author ValidYN="Y"><LastName>Kien</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Escriou</LastName><ForeName>N</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Tsao</LastName><ForeName>S W</ForeName><Initials>SW</Initials></Author><Author ValidYN="Y"><LastName>Nicholls</LastName><ForeName>J M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Altmeyer</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Peiris</LastName><ForeName>J S M</ForeName><Initials>JS</Initials></Author><Author ValidYN="Y"><LastName>Bruzzone</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Nal</LastName><ForeName>B</ForeName><Initials>B</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>08</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J 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