Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.
Identifieur interne : 002790 ( PubMed/Corpus ); précédent : 002789; suivant : 002791Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.
Auteurs : Béatrice Nal ; Cheman Chan ; Francois Kien ; Lewis Siu ; Jane Tse ; Kid Chu ; Jason Kam ; Isabelle Staropoli ; Bernadette Crescenzo-Chaigne ; Nicolas Escriou ; Sylvie Van Der Werf ; Kwok-Yung Yuen ; Ralf AltmeyerSource :
- The Journal of general virology [ 0022-1317 ] ; 2005.
English descriptors
- KwdEn :
- Animals, Cytoplasmic Vesicles (chemistry), Endoplasmic Reticulum (chemistry), Glycosylation, Golgi Apparatus (chemistry), Humans, Mannose (analysis), Membrane Glycoproteins (analysis), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (metabolism), Microscopy, Confocal, Polysaccharides (chemistry), Protein Processing, Post-Translational, Protein Transport, SARS Virus (growth & development), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (analysis), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism), Viral Matrix Proteins (analysis), Viral Matrix Proteins (chemistry), Viral Matrix Proteins (metabolism).
- MESH :
- chemical , analysis : Mannose, Membrane Glycoproteins, Viral Envelope Proteins, Viral Matrix Proteins.
- chemistry : Cytoplasmic Vesicles, Endoplasmic Reticulum, Golgi Apparatus, Membrane Glycoproteins, Polysaccharides, Viral Envelope Proteins, Viral Matrix Proteins.
- growth & development : SARS Virus.
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins, Viral Matrix Proteins.
- Animals, Glycosylation, Humans, Microscopy, Confocal, Protein Processing, Post-Translational, Protein Transport, Spike Glycoprotein, Coronavirus.
Abstract
Post-translational modifications and correct subcellular localization of viral structural proteins are prerequisites for assembly and budding of enveloped viruses. Coronaviruses, like the severe acute respiratory syndrome-associated virus (SARS-CoV), bud from the endoplasmic reticulum-Golgi intermediate compartment. In this study, the subcellular distribution and maturation of SARS-CoV surface proteins S, M and E were analysed by using C-terminally tagged proteins. As early as 30 min post-entry into the endoplasmic reticulum, high-mannosylated S assembles into trimers prior to acquisition of complex N-glycans in the Golgi. Like S, M acquires high-mannose N-glycans that are subsequently modified into complex N-glycans in the Golgi. The N-glycosylation profile and the absence of O-glycosylation on M protein relate SARS-CoV to the previously described group 1 and 3 coronaviruses. Immunofluorescence analysis shows that S is detected in several compartments along the secretory pathway from the endoplasmic reticulum to the plasma membrane while M predominantly localizes in the Golgi, where it accumulates, and in trafficking vesicles. The E protein is not glycosylated. Pulse-chase labelling and confocal microscopy in the presence of protein translation inhibitor cycloheximide revealed that the E protein has a short half-life of 30 min. E protein is found in bright perinuclear patches colocalizing with endoplasmic reticulum markers. In conclusion, SARS-CoV surface proteins S, M and E show differential subcellular localizations when expressed alone suggesting that additional cellular or viral factors might be required for coordinated trafficking to the virus assembly site in the endoplasmic reticulum-Golgi intermediate compartment.
DOI: 10.1099/vir.0.80671-0
PubMed: 15831954
Links to Exploration step
pubmed:15831954Le document en format XML
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<term>Endoplasmic Reticulum (chemistry)</term>
<term>Glycosylation</term>
<term>Golgi Apparatus (chemistry)</term>
<term>Humans</term>
<term>Mannose (analysis)</term>
<term>Membrane Glycoproteins (analysis)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Microscopy, Confocal</term>
<term>Polysaccharides (chemistry)</term>
<term>Protein Processing, Post-Translational</term>
<term>Protein Transport</term>
<term>SARS Virus (growth & development)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (analysis)</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (metabolism)</term>
<term>Viral Matrix Proteins (analysis)</term>
<term>Viral Matrix Proteins (chemistry)</term>
<term>Viral Matrix Proteins (metabolism)</term>
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<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Mannose</term>
<term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Matrix Proteins</term>
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<term>Endoplasmic Reticulum</term>
<term>Golgi Apparatus</term>
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<term>Viral Envelope Proteins</term>
<term>Viral Matrix Proteins</term>
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<term>Viral Envelope Proteins</term>
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<term>Glycosylation</term>
<term>Humans</term>
<term>Microscopy, Confocal</term>
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<front><div type="abstract" xml:lang="en">Post-translational modifications and correct subcellular localization of viral structural proteins are prerequisites for assembly and budding of enveloped viruses. Coronaviruses, like the severe acute respiratory syndrome-associated virus (SARS-CoV), bud from the endoplasmic reticulum-Golgi intermediate compartment. In this study, the subcellular distribution and maturation of SARS-CoV surface proteins S, M and E were analysed by using C-terminally tagged proteins. As early as 30 min post-entry into the endoplasmic reticulum, high-mannosylated S assembles into trimers prior to acquisition of complex N-glycans in the Golgi. Like S, M acquires high-mannose N-glycans that are subsequently modified into complex N-glycans in the Golgi. The N-glycosylation profile and the absence of O-glycosylation on M protein relate SARS-CoV to the previously described group 1 and 3 coronaviruses. Immunofluorescence analysis shows that S is detected in several compartments along the secretory pathway from the endoplasmic reticulum to the plasma membrane while M predominantly localizes in the Golgi, where it accumulates, and in trafficking vesicles. The E protein is not glycosylated. Pulse-chase labelling and confocal microscopy in the presence of protein translation inhibitor cycloheximide revealed that the E protein has a short half-life of 30 min. E protein is found in bright perinuclear patches colocalizing with endoplasmic reticulum markers. In conclusion, SARS-CoV surface proteins S, M and E show differential subcellular localizations when expressed alone suggesting that additional cellular or viral factors might be required for coordinated trafficking to the virus assembly site in the endoplasmic reticulum-Golgi intermediate compartment.</div>
</front>
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<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15831954</PMID>
<DateCompleted><Year>2005</Year>
<Month>05</Month>
<Day>31</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>06</Day>
</DateRevised>
<Article PubModel="Print"><Journal><ISSN IssnType="Print">0022-1317</ISSN>
<JournalIssue CitedMedium="Print"><Volume>86</Volume>
<Issue>Pt 5</Issue>
<PubDate><Year>2005</Year>
<Month>May</Month>
</PubDate>
</JournalIssue>
<Title>The Journal of general virology</Title>
<ISOAbbreviation>J. Gen. Virol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.</ArticleTitle>
<Pagination><MedlinePgn>1423-1434</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1099/vir.0.80671-0</ELocationID>
<Abstract><AbstractText>Post-translational modifications and correct subcellular localization of viral structural proteins are prerequisites for assembly and budding of enveloped viruses. Coronaviruses, like the severe acute respiratory syndrome-associated virus (SARS-CoV), bud from the endoplasmic reticulum-Golgi intermediate compartment. In this study, the subcellular distribution and maturation of SARS-CoV surface proteins S, M and E were analysed by using C-terminally tagged proteins. As early as 30 min post-entry into the endoplasmic reticulum, high-mannosylated S assembles into trimers prior to acquisition of complex N-glycans in the Golgi. Like S, M acquires high-mannose N-glycans that are subsequently modified into complex N-glycans in the Golgi. The N-glycosylation profile and the absence of O-glycosylation on M protein relate SARS-CoV to the previously described group 1 and 3 coronaviruses. Immunofluorescence analysis shows that S is detected in several compartments along the secretory pathway from the endoplasmic reticulum to the plasma membrane while M predominantly localizes in the Golgi, where it accumulates, and in trafficking vesicles. The E protein is not glycosylated. Pulse-chase labelling and confocal microscopy in the presence of protein translation inhibitor cycloheximide revealed that the E protein has a short half-life of 30 min. E protein is found in bright perinuclear patches colocalizing with endoplasmic reticulum markers. In conclusion, SARS-CoV surface proteins S, M and E show differential subcellular localizations when expressed alone suggesting that additional cellular or viral factors might be required for coordinated trafficking to the virus assembly site in the endoplasmic reticulum-Golgi intermediate compartment.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nal</LastName>
<ForeName>Béatrice</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Chan</LastName>
<ForeName>Cheman</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Kien</LastName>
<ForeName>Francois</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong, China.</Affiliation>
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<Author ValidYN="Y"><LastName>Siu</LastName>
<ForeName>Lewis</ForeName>
<Initials>L</Initials>
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</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Tse</LastName>
<ForeName>Jane</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong, China.</Affiliation>
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<Author ValidYN="Y"><LastName>Chu</LastName>
<ForeName>Kid</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Kam</LastName>
<ForeName>Jason</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Staropoli</LastName>
<ForeName>Isabelle</ForeName>
<Initials>I</Initials>
<AffiliationInfo><Affiliation>Unité d'Immunologie Virale, Institut Pasteur, 25 rue du Dr Roux, Paris, France.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Crescenzo-Chaigne</LastName>
<ForeName>Bernadette</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>Unité de Génétique Moléculaire des Virus Respiratoires, Institut Pasteur, 25 rue du Dr Roux, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Escriou</LastName>
<ForeName>Nicolas</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Unité de Génétique Moléculaire des Virus Respiratoires, Institut Pasteur, 25 rue du Dr Roux, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>van der Werf</LastName>
<ForeName>Sylvie</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Unité de Génétique Moléculaire des Virus Respiratoires, Institut Pasteur, 25 rue du Dr Roux, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yuen</LastName>
<ForeName>Kwok-Yung</ForeName>
<Initials>KY</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, The University of Hong Kong, Hong Kong, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Altmeyer</LastName>
<ForeName>Ralf</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong, China.</Affiliation>
</AffiliationInfo>
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<MedlineTA>J Gen Virol</MedlineTA>
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<MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName>
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</MeshHeading>
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