SrasV1, France, Analysis, bibRecord, 000348

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

Identifieur interne : 000348 ( France/Analysis ); précédent : 000347; suivant : 000349

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

Auteurs : Baatrice Nal [Hong Kong] ; Cheman Chan [Hong Kong] ; Francois Kien [Hong Kong] ; Lewis Siu [Hong Kong] ; Jane Tse [Hong Kong] ; Kid Chu [Hong Kong] ; Jason Kam [Hong Kong] ; Isabelle Staropoli [France] ; Bernadette Crescenzo-Chaigne [France] ; Nicolas Escriou [France] ; Sylvie Van Der Werf [France] ; Kwok-Yung Yuen [Hong Kong] ; Ralf Altmeyer [Hong Kong]

Source :

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

RBID : Pascal:05-0229117

Descripteurs français

English descriptors

KwdEn :
- Animals, Coronavirus, Cytoplasmic Vesicles (chemistry), Endoplasmic Reticulum (chemistry), Glycosylation, Golgi Apparatus (chemistry), Humans, Localization, Mannose (analysis), Membrane Glycoproteins (analysis), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (metabolism), Microbiology, Microscopy, Confocal, Polysaccharides (chemistry), Protein, Protein Processing, Post-Translational, Protein Transport, SARS Virus (growth & development), Severe acute respiratory syndrome, 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), Virology.
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.

Affiliations:

Links to Exploration step

Pascal:05-0229117

Le document en format XML

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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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</affiliation>
</author>
<author><name sortKey="Altmeyer, Ralf" sort="Altmeyer, Ralf" uniqKey="Altmeyer R" first="Ralf" last="Altmeyer">Ralf Altmeyer</name>
<affiliation wicri:level="1"><inist:fA14 i1="01"><s1>HKU-Pasteur Research Centre, 8 Sassoon Road</s1>
<s3>HKG</s3>
<sZ>1 aut.</sZ>
<sZ>2 aut.</sZ>
<sZ>3 aut.</sZ>
<sZ>4 aut.</sZ>
<sZ>5 aut.</sZ>
<sZ>6 aut.</sZ>
<sZ>7 aut.</sZ>
<sZ>13 aut.</sZ>
</inist:fA14>
<country>Hong Kong</country>
<wicri:noRegion>HKU-Pasteur Research Centre, 8 Sassoon Road</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series><title level="j" type="main">Journal of general virology</title>
<title level="j" type="abbreviated">J. gen. virol.</title>
<idno type="ISSN">0022-1317</idno>
<imprint><date when="2005">2005</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><title level="j" type="main">Journal of general virology</title>
<title level="j" type="abbreviated">J. gen. virol.</title>
<idno type="ISSN">0022-1317</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Coronavirus</term>
<term>Cytoplasmic Vesicles (chemistry)</term>
<term>Endoplasmic Reticulum (chemistry)</term>
<term>Glycosylation</term>
<term>Golgi Apparatus (chemistry)</term>
<term>Humans</term>
<term>Localization</term>
<term>Mannose (analysis)</term>
<term>Membrane Glycoproteins (analysis)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Microbiology</term>
<term>Microscopy, Confocal</term>
<term>Polysaccharides (chemistry)</term>
<term>Protein</term>
<term>Protein Processing, Post-Translational</term>
<term>Protein Transport</term>
<term>SARS Virus (growth & development)</term>
<term>Severe acute respiratory syndrome</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>
<term>Virology</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="Pascal" xml:lang="fr"><term>Animaux</term>
<term>Appareil de Golgi</term>
<term>Coronavirus</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Glycosylation</term>
<term>Humains</term>
<term>Localisation</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Microscopie confocale</term>
<term>Polyosides</term>
<term>Protéine</term>
<term>Microbiologie</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>Virologie</term>
<term>Syndrome respiratoire aigu sévère</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>
<affiliations><list><country><li>France</li>
<li>Hong Kong</li>
</country>
<region><li>Île-de-France</li>
</region>
<settlement><li>Paris</li>
</settlement>
</list>
<tree><country name="Hong Kong"><noRegion><name sortKey="Nal, Baatrice" sort="Nal, Baatrice" uniqKey="Nal B" first="Baatrice" last="Nal">Baatrice Nal</name>
</noRegion>
<name sortKey="Altmeyer, Ralf" sort="Altmeyer, Ralf" uniqKey="Altmeyer R" first="Ralf" last="Altmeyer">Ralf Altmeyer</name>
<name sortKey="Chan, Cheman" sort="Chan, Cheman" uniqKey="Chan C" first="Cheman" last="Chan">Cheman Chan</name>
<name sortKey="Chu, Kid" sort="Chu, Kid" uniqKey="Chu K" first="Kid" last="Chu">Kid Chu</name>
<name sortKey="Kam, Jason" sort="Kam, Jason" uniqKey="Kam J" first="Jason" last="Kam">Jason Kam</name>
<name sortKey="Kien, Francois" sort="Kien, Francois" uniqKey="Kien F" first="Francois" last="Kien">Francois Kien</name>
<name sortKey="Siu, Lewis" sort="Siu, Lewis" uniqKey="Siu L" first="Lewis" last="Siu">Lewis Siu</name>
<name sortKey="Tse, Jane" sort="Tse, Jane" uniqKey="Tse J" first="Jane" last="Tse">Jane Tse</name>
<name sortKey="Yuen, Kwok Yung" sort="Yuen, Kwok Yung" uniqKey="Yuen K" first="Kwok-Yung" last="Yuen">Kwok-Yung Yuen</name>
</country>
<country name="France"><region name="Île-de-France"><name sortKey="Staropoli, Isabelle" sort="Staropoli, Isabelle" uniqKey="Staropoli I" first="Isabelle" last="Staropoli">Isabelle Staropoli</name>
</region>
<name sortKey="Crescenzo Chaigne, Bernadette" sort="Crescenzo Chaigne, Bernadette" uniqKey="Crescenzo Chaigne B" first="Bernadette" last="Crescenzo-Chaigne">Bernadette Crescenzo-Chaigne</name>
<name sortKey="Escriou, Nicolas" sort="Escriou, Nicolas" uniqKey="Escriou N" first="Nicolas" last="Escriou">Nicolas Escriou</name>
<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>
</country>
</tree>
</affiliations>
</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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