Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.
Identifieur interne : 000E95 ( Ncbi/Curation ); précédent : 000E94; suivant : 000E96Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E.
Auteurs : Béatrice Nal [République populaire de Chine] ; Cheman Chan [République populaire de Chine] ; Francois Kien [République populaire de Chine] ; Lewis Siu [République populaire de Chine] ; Jane Tse [République populaire de Chine] ; Kid Chu [République populaire de Chine] ; Jason Kam [République populaire de Chine] ; Isabelle Staropoli [France] ; Bernadette Crescenzo-Chaigne [France] ; Nicolas Escriou [France] ; Sylvie Van Der Werf [France] ; Kwok-Yung Yuen [République populaire de Chine] ; Ralf Altmeyer [République populaire de Chine]Source :
- The Journal of general virology [ 0022-1317 ] ; 2005.
Descripteurs français
- KwdFr :
- Animaux, Appareil de Golgi (), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (analyse), Glycoprotéines membranaires (métabolisme), Glycosylation, Humains, Mannose (analyse), Maturation post-traductionnelle des protéines, Microscopie confocale, Polyosides (), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (analyse), Protéines de l'enveloppe virale (métabolisme), Protéines de la matrice virale (), Protéines de la matrice virale (analyse), Protéines de la matrice virale (métabolisme), Réticulum endoplasmique (), Transport de protéines, Virus du SRAS (croissance et développement), Vésicules cytoplasmiques ().
- MESH :
- analyse : Glycoprotéines membranaires, Mannose, Protéines de l'enveloppe virale, Protéines de la matrice virale.
- croissance et développement : Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale, Protéines de la matrice virale.
- Animaux, Appareil de Golgi, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Glycosylation, Humains, Maturation post-traductionnelle des protéines, Microscopie confocale, Polyosides, Protéines de l'enveloppe virale, Protéines de la matrice virale, Réticulum endoplasmique, Transport de protéines, Vésicules cytoplasmiques.
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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pubmed:15831954Le document en format XML
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<author><name sortKey="Kam, Jason" sort="Kam, Jason" uniqKey="Kam J" first="Jason" last="Kam">Jason Kam</name>
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<author><name sortKey="Staropoli, Isabelle" sort="Staropoli, Isabelle" uniqKey="Staropoli I" first="Isabelle" last="Staropoli">Isabelle Staropoli</name>
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<country xml:lang="fr">France</country>
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<placeName><region type="region">Île-de-France</region>
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<settlement type="city">Paris</settlement>
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<author><name sortKey="Crescenzo Chaigne, Bernadette" sort="Crescenzo Chaigne, Bernadette" uniqKey="Crescenzo Chaigne B" first="Bernadette" last="Crescenzo-Chaigne">Bernadette Crescenzo-Chaigne</name>
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<settlement type="city">Paris</settlement>
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<author><name sortKey="Escriou, Nicolas" sort="Escriou, Nicolas" uniqKey="Escriou N" first="Nicolas" last="Escriou">Nicolas Escriou</name>
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<country xml:lang="fr">France</country>
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<region type="old region">Île-de-France</region>
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<author><name sortKey="Van Der Werf, Sylvie" sort="Van Der Werf, Sylvie" uniqKey="Van Der Werf S" first="Sylvie" last="Van Der Werf">Sylvie Van Der Werf</name>
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<country xml:lang="fr">France</country>
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<author><name sortKey="Yuen, Kwok Yung" sort="Yuen, Kwok Yung" uniqKey="Yuen K" first="Kwok-Yung" last="Yuen">Kwok-Yung Yuen</name>
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<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Altmeyer, Ralf" sort="Altmeyer, Ralf" uniqKey="Altmeyer R" first="Ralf" last="Altmeyer">Ralf Altmeyer</name>
<affiliation wicri:level="1"><nlm:affiliation>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
<wicri:regionArea>HKU-Pasteur Research Centre, 8 Sassoon Road, Hong Kong</wicri:regionArea>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<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>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<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>
</TEI>
</record>
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