SrasV1, PubMed, Curation, bibRecord, 002790

Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.

Identifieur interne : 002790 ( PubMed/Curation ); précédent : 002789; suivant : 002791

Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.

Source :

The Journal of general virology [ 0022-1317 ] ; 2005.

RBID : pubmed:15831954

Descripteurs français

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

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<term>Cytoplasmic Vesicles (chemistry)</term>
<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>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Appareil de Golgi ()</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (analyse)</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Glycosylation</term>
<term>Humains</term>
<term>Mannose (analyse)</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Microscopie confocale</term>
<term>Polyosides ()</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (analyse)</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Protéines de la matrice virale ()</term>
<term>Protéines de la matrice virale (analyse)</term>
<term>Protéines de la matrice virale (métabolisme)</term>
<term>Réticulum endoplasmique ()</term>
<term>Transport de protéines</term>
<term>Virus du SRAS (croissance et développement)</term>
<term>Vésicules cytoplasmiques ()</term>
</keywords>
<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>
</keywords>
<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Mannose</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines de la matrice virale</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cytoplasmic Vesicles</term>
<term>Endoplasmic Reticulum</term>
<term>Golgi Apparatus</term>
<term>Membrane Glycoproteins</term>
<term>Polysaccharides</term>
<term>Viral Envelope Proteins</term>
<term>Viral Matrix Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term>
<term>Viral Envelope Proteins</term>
<term>Viral Matrix Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines de la matrice virale</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Glycosylation</term>
<term>Humans</term>
<term>Microscopy, Confocal</term>
<term>Protein Processing, Post-Translational</term>
<term>Protein Transport</term>
<term>Spike Glycoprotein, Coronavirus</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Appareil de Golgi</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Glycosylation</term>
<term>Humains</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Microscopie confocale</term>
<term>Polyosides</term>
<term>Protéines de l'enveloppe virale</term>
<term>Protéines de la matrice virale</term>
<term>Réticulum endoplasmique</term>
<term>Transport de protéines</term>
<term>Vésicules cytoplasmiques</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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<Month>05</Month>
<Day>31</Day>
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<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>06</Day>
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<Month>May</Month>
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<Title>The Journal of general virology</Title>
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<ArticleTitle>Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.</ArticleTitle>
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</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>
</Author>
<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>
</Author>
<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>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Siu</LastName>
<ForeName>Lewis</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong, China.</Affiliation>
</AffiliationInfo>
</Author>
<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>
</AffiliationInfo>
</Author>
<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>
</Author>
<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>
</Author>
<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>
</Author>
<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>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>J Gen Virol</MedlineTA>
<NlmUniqueID>0077340</NlmUniqueID>
<ISSNLinking>0022-1317</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014763">Viral Matrix Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>108502-71-2</RegistryNumber>
<NameOfSubstance UI="C067997">M protein, Coronavirus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>PHA4727WTP</RegistryNumber>
<NameOfSubstance UI="D008358">Mannose</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D022162" MajorTopicYN="N">Cytoplasmic Vesicles</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004721" MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006056" MajorTopicYN="N">Golgi Apparatus</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008358" MajorTopicYN="N">Mannose</DescriptorName>
<QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName>
<QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018613" MajorTopicYN="N">Microscopy, Confocal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011499" MajorTopicYN="Y">Protein Processing, Post-Translational</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021381" MajorTopicYN="Y">Protein Transport</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName>
<QualifierName UI="Q000254" MajorTopicYN="Y">growth & development</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D064370" MajorTopicYN="N">Spike Glycoprotein, Coronavirus</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014759" MajorTopicYN="N">Viral Envelope Proteins</DescriptorName>
<QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014763" MajorTopicYN="N">Viral Matrix Proteins</DescriptorName>
<QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year>
<Month>4</Month>
<Day>16</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2005</Year>
<Month>6</Month>
<Day>1</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2005</Year>
<Month>4</Month>
<Day>16</Day>
<Hour>9</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">15831954</ArticleId>
<ArticleId IdType="doi">10.1099/vir.0.80671-0</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
</record>

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Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.

Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.

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