SrasV1, PascalFrancis, Curation, bibRecord, 000589

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 : 000589 ( PascalFrancis/Curation ); précédent : 000588; suivant : 000590

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

Pascal (Inist)
- Coronavirus, Protéine membranaire, Réticulum endoplasmique, Virologie, Syndrome respiratoire aigu sévère.

English descriptors

KwdEn :
- Coronavirus, Endoplasmic reticulum, Membrane protein, Severe acute respiratory syndrome, Virology.

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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A06				`@2 5`
A08	`01`	`1`	`ENG`	`@1 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`
A11	`01`	`1`		`@1 MCBRIDE (Corrin E.)`
A11	`02`	`1`		`@1 JIE LI`
A11	`03`	`1`		`@1 MACHAMER (Carolyn E.)`
A14	`01`			`@1 Department of Cell Biology, The Johns Hopkins University School of Medicine @2 Baltimore, Maryland 21205 @3 USA @Z 1 aut. @Z 2 aut. @Z 3 aut.`
A20				`@1 2418-2428`
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C02	`01`	`X`		`@0 002A05C10`
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C03	`01`	`X`	`ENG`	`@0 Coronavirus @2 NW @5 01`
C03	`01`	`X`	`SPA`	`@0 Coronavirus @2 NW @5 01`
C03	`02`	`X`	`FRE`	`@0 Protéine membranaire @5 05`
C03	`02`	`X`	`ENG`	`@0 Membrane protein @5 05`
C03	`02`	`X`	`SPA`	`@0 Proteína membranar @5 05`
C03	`03`	`X`	`FRE`	`@0 Réticulum endoplasmique @5 06`
C03	`03`	`X`	`ENG`	`@0 Endoplasmic reticulum @5 06`
C03	`03`	`X`	`SPA`	`@0 Retículo endoplásmico @5 06`
C03	`04`	`X`	`FRE`	`@0 Virologie @5 07`
C03	`04`	`X`	`ENG`	`@0 Virology @5 07`
C03	`04`	`X`	`SPA`	`@0 Virología @5 07`
C03	`05`	`X`	`FRE`	`@0 Syndrome respiratoire aigu sévère @2 NM @5 14`
C03	`05`	`X`	`ENG`	`@0 Severe acute respiratory syndrome @2 NM @5 14`
C03	`05`	`X`	`SPA`	`@0 Síndrome respiratorio agudo severo @2 NM @5 14`
C07	`01`	`X`	`FRE`	`@0 Coronaviridae @2 NW`
C07	`01`	`X`	`ENG`	`@0 Coronaviridae @2 NW`
C07	`01`	`X`	`SPA`	`@0 Coronaviridae @2 NW`
C07	`02`	`X`	`FRE`	`@0 Nidovirales @2 NW`
C07	`02`	`X`	`ENG`	`@0 Nidovirales @2 NW`
C07	`02`	`X`	`SPA`	`@0 Nidovirales @2 NW`
C07	`03`	`X`	`FRE`	`@0 Virus @2 NW`
C07	`03`	`X`	`ENG`	`@0 Virus @2 NW`
C07	`03`	`X`	`SPA`	`@0 Virus @2 NW`
C07	`04`	`X`	`FRE`	`@0 Appareil respiratoire pathologie @5 13`
C07	`04`	`X`	`ENG`	`@0 Respiratory disease @5 13`
C07	`04`	`X`	`SPA`	`@0 Aparato respiratorio patología @5 13`
C07	`05`	`X`	`FRE`	`@0 Virose`
C07	`05`	`X`	`ENG`	`@0 Viral disease`
C07	`05`	`X`	`SPA`	`@0 Virosis`
C07	`06`	`X`	`FRE`	`@0 Infection`
C07	`06`	`X`	`ENG`	`@0 Infection`
C07	`06`	`X`	`SPA`	`@0 Infección`
C07	`07`	`X`	`FRE`	`@0 Poumon pathologie @5 16`
C07	`07`	`X`	`ENG`	`@0 Lung disease @5 16`
C07	`07`	`X`	`SPA`	`@0 Pulmón patología @5 16`
N21				`@1 092`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

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Le document en format XML

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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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Descripteurs français

English descriptors

Abstract

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Links to Exploration step

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