SrasV1, Main, Curation, bibRecord, 003B16

The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein

Identifieur interne : 003B16 ( Main/Curation ); précédent : 003B15; suivant : 003B17

The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein

Auteurs : Corrin E. Mcbride [États-Unis] ; JIE LI [États-Unis] ; Carolyn E. Machamer [États-Unis]

Source :

Journal of virology [ 0022-538X ] ; 2007.

RBID : Pascal:07-0143955

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Cell Membrane (metabolism), Cell Membrane (virology), Coat Protein Complex I (metabolism), Coronavirus, Cytoplasm (virology), Endoplasmic Reticulum (virology), Endoplasmic reticulum, Golgi Apparatus (virology), HeLa Cells, Humans, In Vitro Techniques, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (physiology), Membrane Proteins (metabolism), Membrane protein, Molecular Sequence Data, Protein Binding, Protein Sorting Signals (genetics), Protein Sorting Signals (physiology), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), SARS Virus (genetics), SARS Virus (pathogenicity), SARS Virus (physiology), Severe acute respiratory syndrome, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (physiology), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism), Virology.
MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Protein Sorting Signals, Recombinant Fusion Proteins, Viral Envelope Proteins, Viral Matrix Proteins.
- chemical , metabolism : Coat Protein Complex I, Membrane Proteins, Recombinant Fusion Proteins, Viral Matrix Proteins.
- genetics : SARS Virus.
- metabolism : Cell Membrane.
- pathogenicity : SARS Virus.
- chemical , physiology : Membrane Glycoproteins, Protein Sorting Signals, SARS Virus, Viral Envelope Proteins.
- virology : Cell Membrane, Cytoplasm, Endoplasmic Reticulum, Golgi Apparatus.
- Amino Acid Motifs, Amino Acid Sequence, HeLa Cells, Humans, In Vitro Techniques, Molecular Sequence Data, Protein Binding, Spike Glycoprotein, Coronavirus.

Abstract

Like other coronaviruses, severe acute respiratory syndrome coronavirus (SARS CoV) assembles at and buds into the lumen of the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC). Accumulation of the viral envelope proteins at this compartment is a prerequisite for virus assembly. Previously, we reported the identification of a dibasic motif (KxHxx) in the cytoplasmic tail of the SARS CoV spike (S) protein that was similar to a canonical dilysine ER retrieval signal. Here we demonstrate that this motif is a novel and functional ER retrieval signal which reduced the rate of traffic of the full-length S protein through the Golgi complex. The KxHxx motif also partially retained two different reporter proteins in the ERGIC region and reduced their rates of trafficking, although the motif was less potent than the canonical dilysine signal. The dibasic motif bound the coatomer complex I (COPI) in an in vitro binding assay, suggesting that ER retrieval may contribute to the accumulation of SARS CoV S protein near the virus assembly site for interaction with other viral structural proteins. In support of this, we found that the dibasic motif on the SARS S protein was required for its localization to the ERGIC/Golgi region when coexpressed with SARS membrane (M) protein. Thus, the cycling of SARS S through the ER-Golgi system may be required for its incorporation into assembling virions in the ERGIC.

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Le document en format XML

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<term>Cell Membrane (virology)</term>
<term>Coat Protein Complex I (metabolism)</term>
<term>Coronavirus</term>
<term>Cytoplasm (virology)</term>
<term>Endoplasmic Reticulum (virology)</term>
<term>Endoplasmic reticulum</term>
<term>Golgi Apparatus (virology)</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>In Vitro Techniques</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (physiology)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Membrane protein</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Sorting Signals (genetics)</term>
<term>Protein Sorting Signals (physiology)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
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<term>Viral Envelope Proteins (genetics)</term>
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<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
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<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (physiologie)</term>
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<term>Protéines de fusion recombinantes (métabolisme)</term>
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<term>Protéines de l'enveloppe virale (physiologie)</term>
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<term>Signaux de triage des protéines (génétique)</term>
<term>Signaux de triage des protéines (physiologie)</term>
<term>Séquence d'acides aminés</term>
<term>Techniques in vitro</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (pathogénicité)</term>
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<term>HeLa Cells</term>
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<term>Protein Binding</term>
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<term>Glycoprotéines membranaires</term>
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<term>Protéines de l'enveloppe virale</term>
<term>Réticulum endoplasmique</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Like other coronaviruses, severe acute respiratory syndrome coronavirus (SARS CoV) assembles at and buds into the lumen of the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC). Accumulation of the viral envelope proteins at this compartment is a prerequisite for virus assembly. Previously, we reported the identification of a dibasic motif (KxHxx) in the cytoplasmic tail of the SARS CoV spike (S) protein that was similar to a canonical dilysine ER retrieval signal. Here we demonstrate that this motif is a novel and functional ER retrieval signal which reduced the rate of traffic of the full-length S protein through the Golgi complex. The KxHxx motif also partially retained two different reporter proteins in the ERGIC region and reduced their rates of trafficking, although the motif was less potent than the canonical dilysine signal. The dibasic motif bound the coatomer complex I (COPI) in an in vitro binding assay, suggesting that ER retrieval may contribute to the accumulation of SARS CoV S protein near the virus assembly site for interaction with other viral structural proteins. In support of this, we found that the dibasic motif on the SARS S protein was required for its localization to the ERGIC/Golgi region when coexpressed with SARS membrane (M) protein. Thus, the cycling of SARS S through the ER-Golgi system may be required for its incorporation into assembling virions in the ERGIC.</div>
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<title level="j" type="abbreviated">J. virol.</title>
<idno type="ISSN">0022-538X</idno>
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<term>Severe acute respiratory syndrome</term>
<term>Virology</term>
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<term>Protéine membranaire</term>
<term>Réticulum endoplasmique</term>
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<front><div type="abstract" xml:lang="en">Like other coronaviruses, severe acute respiratory syndrome coronavirus (SARS CoV) assembles at and buds into the lumen of the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC). Accumulation of the viral envelope proteins at this compartment is a prerequisite for virus assembly. Previously, we reported the identification of a dibasic motif (KxHxx) in the cytoplasmic tail of the SARS CoV spike (S) protein that was similar to a canonical dilysine ER retrieval signal. Here we demonstrate that this motif is a novel and functional ER retrieval signal which reduced the rate of traffic of the full-length S protein through the Golgi complex. The KxHxx motif also partially retained two different reporter proteins in the ERGIC region and reduced their rates of trafficking, although the motif was less potent than the canonical dilysine signal. The dibasic motif bound the coatomer complex I (COPI) in an in vitro binding assay, suggesting that ER retrieval may contribute to the accumulation of SARS CoV S protein near the virus assembly site for interaction with other viral structural proteins. In support of this, we found that the dibasic motif on the SARS S protein was required for its localization to the ERGIC/Golgi region when coexpressed with SARS membrane (M) protein. Thus, the cycling of SARS S through the ER-Golgi system may be required for its incorporation into assembling virions in the ERGIC.</div>
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<PubMed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein.</title>
<author><name sortKey="Mcbride, Corrin E" sort="Mcbride, Corrin E" uniqKey="Mcbride C" first="Corrin E" last="Mcbride">Corrin E. Mcbride</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Cell Biology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Cell Biology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205</wicri:regionArea>
<placeName><region type="state">Maryland</region>
</placeName>
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<author><name sortKey="Li, Jie" sort="Li, Jie" uniqKey="Li J" first="Jie" last="Li">Jie Li</name>
</author>
<author><name sortKey="Machamer, Carolyn E" sort="Machamer, Carolyn E" uniqKey="Machamer C" first="Carolyn E" last="Machamer">Carolyn E. Machamer</name>
</author>
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<date when="2007">2007</date>
<idno type="RBID">pubmed:17166901</idno>
<idno type="pmid">17166901</idno>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein.</title>
<author><name sortKey="Mcbride, Corrin E" sort="Mcbride, Corrin E" uniqKey="Mcbride C" first="Corrin E" last="Mcbride">Corrin E. Mcbride</name>
<affiliation wicri:level="2"><nlm:affiliation>Department of Cell Biology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205, USA.</nlm:affiliation>
<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Cell Biology, The Johns Hopkins University School of Medicine, 725 N. Wolfe Street, Baltimore, MD 21205</wicri:regionArea>
<placeName><region type="state">Maryland</region>
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<author><name sortKey="Li, Jie" sort="Li, Jie" uniqKey="Li J" first="Jie" last="Li">Jie Li</name>
</author>
<author><name sortKey="Machamer, Carolyn E" sort="Machamer, Carolyn E" uniqKey="Machamer C" first="Carolyn E" last="Machamer">Carolyn E. Machamer</name>
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<series><title level="j">Journal of virology</title>
<idno type="ISSN">0022-538X</idno>
<imprint><date when="2007" type="published">2007</date>
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<term>Amino Acid Sequence</term>
<term>Cell Membrane (metabolism)</term>
<term>Cell Membrane (virology)</term>
<term>Coat Protein Complex I (metabolism)</term>
<term>Cytoplasm (virology)</term>
<term>Endoplasmic Reticulum (virology)</term>
<term>Golgi Apparatus (virology)</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>In Vitro Techniques</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (physiology)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Sorting Signals (genetics)</term>
<term>Protein Sorting Signals (physiology)</term>
<term>Recombinant Fusion Proteins (genetics)</term>
<term>Recombinant Fusion Proteins (metabolism)</term>
<term>SARS Virus (genetics)</term>
<term>SARS Virus (pathogenicity)</term>
<term>SARS Virus (physiology)</term>
<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (physiology)</term>
<term>Viral Matrix Proteins (genetics)</term>
<term>Viral Matrix Proteins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Appareil de Golgi (virologie)</term>
<term>Cellules HeLa</term>
<term>Complexe I de protéines de revêtement (métabolisme)</term>
<term>Cytoplasme (virologie)</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (génétique)</term>
<term>Glycoprotéines membranaires (physiologie)</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Membrane cellulaire (métabolisme)</term>
<term>Membrane cellulaire (virologie)</term>
<term>Motifs d'acides aminés</term>
<term>Protéines de fusion recombinantes (génétique)</term>
<term>Protéines de fusion recombinantes (métabolisme)</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (génétique)</term>
<term>Protéines de l'enveloppe virale (physiologie)</term>
<term>Protéines de la matrice virale (génétique)</term>
<term>Protéines de la matrice virale (métabolisme)</term>
<term>Protéines membranaires (métabolisme)</term>
<term>Réticulum endoplasmique (virologie)</term>
<term>Signaux de triage des protéines (génétique)</term>
<term>Signaux de triage des protéines (physiologie)</term>
<term>Séquence d'acides aminés</term>
<term>Techniques in vitro</term>
<term>Virus du SRAS (génétique)</term>
<term>Virus du SRAS (pathogénicité)</term>
<term>Virus du SRAS (physiologie)</term>
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<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term>
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<term>Recombinant Fusion Proteins</term>
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<term>Viral Matrix Proteins</term>
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<term>Recombinant Fusion Proteins</term>
<term>Viral Matrix Proteins</term>
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<term>Protéines de l'enveloppe virale</term>
<term>Protéines de la matrice virale</term>
<term>Signaux de triage des protéines</term>
<term>Virus du SRAS</term>
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<term>Protéines de la matrice virale</term>
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<term>Signaux de triage des protéines</term>
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<term>SARS Virus</term>
<term>Viral Envelope Proteins</term>
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<term>Cytoplasme</term>
<term>Membrane cellulaire</term>
<term>Réticulum endoplasmique</term>
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<keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Cell Membrane</term>
<term>Cytoplasm</term>
<term>Endoplasmic Reticulum</term>
<term>Golgi Apparatus</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term>
<term>Amino Acid Sequence</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>In Vitro Techniques</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Spike Glycoprotein, Coronavirus</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term>
<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</term>
<term>Humains</term>
<term>Liaison aux protéines</term>
<term>Motifs d'acides aminés</term>
<term>Protéines de l'enveloppe virale</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Like other coronaviruses, severe acute respiratory syndrome coronavirus (SARS CoV) assembles at and buds into the lumen of the endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC). Accumulation of the viral envelope proteins at this compartment is a prerequisite for virus assembly. Previously, we reported the identification of a dibasic motif (KxHxx) in the cytoplasmic tail of the SARS CoV spike (S) protein that was similar to a canonical dilysine ER retrieval signal. Here we demonstrate that this motif is a novel and functional ER retrieval signal which reduced the rate of traffic of the full-length S protein through the Golgi complex. The KxHxx motif also partially retained two different reporter proteins in the ERGIC region and reduced their rates of trafficking, although the motif was less potent than the canonical dilysine signal. The dibasic motif bound the coatomer complex I (COPI) in an in vitro binding assay, suggesting that ER retrieval may contribute to the accumulation of SARS CoV S protein near the virus assembly site for interaction with other viral structural proteins. In support of this, we found that the dibasic motif on the SARS S protein was required for its localization to the ERGIC/Golgi region when coexpressed with SARS membrane (M) protein. Thus, the cycling of SARS S through the ER-Golgi system may be required for its incorporation into assembling virions in the ERGIC.</div>
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The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein

The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein

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