SrasV1, Ncbi, Merge, bibRecord, 001801

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 : 001801 ( Ncbi/Merge ); précédent : 001800; suivant : 001802

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 ; Carolyn E. Machamer

Source :

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

RBID : pubmed:17166901

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs, Amino Acid Sequence, Cell Membrane (metabolism), Cell Membrane (virology), Coat Protein Complex I (metabolism), Cytoplasm (virology), Endoplasmic Reticulum (virology), Golgi Apparatus (virology), HeLa Cells, Humans, In Vitro Techniques, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (physiology), Membrane Proteins (metabolism), 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), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (physiology), Viral Matrix Proteins (genetics), Viral Matrix Proteins (metabolism).
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.

DOI: 10.1128/JVI.02146-06
PubMed: 17166901

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to stream PubMed, to step Corpus: 001F57
to stream PubMed, to step Curation: 001F57
to stream PubMed, to step Checkpoint: 001C63

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pubmed:17166901

Le document en format XML

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<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>
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<term>Membrane Glycoproteins (genetics)</term>
<term>Membrane Glycoproteins (physiology)</term>
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<term>Protein Binding</term>
<term>Protein Sorting Signals (genetics)</term>
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<term>Recombinant Fusion Proteins (genetics)</term>
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<term>SARS Virus (genetics)</term>
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<term>Spike Glycoprotein, Coronavirus</term>
<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
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<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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<term>Protéines de la matrice virale</term>
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<term>Protéines de la matrice virale</term>
<term>Protéines membranaires</term>
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<term>Protéines de l'enveloppe virale</term>
<term>Signaux de triage des protéines</term>
<term>Virus du SRAS</term>
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<term>Protein Sorting Signals</term>
<term>SARS Virus</term>
<term>Viral Envelope Proteins</term>
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<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>
</keywords>
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<term>Amino Acid Sequence</term>
<term>HeLa Cells</term>
<term>Humans</term>
<term>In Vitro Techniques</term>
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<term>Protein Binding</term>
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<term>Données de séquences moléculaires</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires</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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<Abstract><AbstractText>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.</AbstractText>
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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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