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

Identifieur interne : 000687 ( PascalFrancis/Corpus ); précédent : 000686; suivant : 000688

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

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

Source :

RBID : Pascal:05-0229117

Descripteurs français

English descriptors

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.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

pA  
A01 01  1    @0 0022-1317
A02 01      @0 JGVIAY
A03   1    @0 J. gen. virol.
A05       @2 86
A06       @3 p.5
A08 01  1  ENG  @1 Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E
A11 01  1    @1 NAL (Baatrice)
A11 02  1    @1 CHAN (Cheman)
A11 03  1    @1 KIEN (Francois)
A11 04  1    @1 SIU (Lewis)
A11 05  1    @1 TSE (Jane)
A11 06  1    @1 CHU (Kid)
A11 07  1    @1 KAM (Jason)
A11 08  1    @1 STAROPOLI (Isabelle)
A11 09  1    @1 CRESCENZO-CHAIGNE (Bernadette)
A11 10  1    @1 ESCRIOU (Nicolas)
A11 11  1    @1 VAN DER WERF (Sylvie)
A11 12  1    @1 YUEN (Kwok-Yung)
A11 13  1    @1 ALTMEYER (Ralf)
A14 01      @1 HKU-Pasteur Research Centre, 8 Sassoon Road @3 HKG @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut. @Z 5 aut. @Z 6 aut. @Z 7 aut. @Z 13 aut.
A14 02      @1 Unité d'lmmunologie Virale, Institut Pasteur, 25 rue du Dr Roux @2 Paris @3 FRA @Z 8 aut.
A14 03      @1 Unité de Génétique Moléculaire des Virus Respiratoires, Institut Pasteur, 25 rue du Dr Roux @2 Paris @3 FRA @Z 9 aut. @Z 10 aut. @Z 11 aut.
A14 04      @1 Department of Microbiology, The University of Hong Kong @3 HKG @Z 12 aut.
A20       @1 1423-1434
A21       @1 2005
A23 01      @0 ENG
A43 01      @1 INIST @2 13533 @5 354000129444440210
A44       @0 0000 @1 © 2005 INIST-CNRS. All rights reserved.
A45       @0 2 p.1/4
A47 01  1    @0 05-0229117
A60       @1 P
A61       @0 A
A64 01  1    @0 Journal of general virology
A66 01      @0 GBR
C01 01    ENG  @0 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.
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C03 01  X  ENG  @0 Coronavirus @2 NW @5 01
C03 01  X  SPA  @0 Coronavirus @2 NW @5 01
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C03 03  X  SPA  @0 Proteína @5 06
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C03 04  X  SPA  @0 Microbiología @5 07
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C03 06  X  FRE  @0 Syndrome respiratoire aigu sévère @2 NM @5 14
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Format Inist (serveur)

NO : PASCAL 05-0229117 INIST
ET : Differential maturation and subcellular localization of severe acute respiratory syndrome coronavirus surface proteins S, M and E
AU : NAL (Baatrice); CHAN (Cheman); KIEN (Francois); SIU (Lewis); TSE (Jane); CHU (Kid); KAM (Jason); STAROPOLI (Isabelle); CRESCENZO-CHAIGNE (Bernadette); ESCRIOU (Nicolas); VAN DER WERF (Sylvie); YUEN (Kwok-Yung); ALTMEYER (Ralf)
AF : HKU-Pasteur Research Centre, 8 Sassoon Road/Hong-Kong (1 aut., 2 aut., 3 aut., 4 aut., 5 aut., 6 aut., 7 aut., 13 aut.); Unité d'lmmunologie Virale, Institut Pasteur, 25 rue du Dr Roux/Paris/France (8 aut.); Unité de Génétique Moléculaire des Virus Respiratoires, Institut Pasteur, 25 rue du Dr Roux/Paris/France (9 aut., 10 aut., 11 aut.); Department of Microbiology, The University of Hong Kong/Hong-Kong (12 aut.)
DT : Publication en série; Niveau analytique
SO : Journal of general virology; ISSN 0022-1317; Coden JGVIAY; Royaume-Uni; Da. 2005; Vol. 86; No. p.5; Pp. 1423-1434; Bibl. 2 p.1/4
LA : Anglais
EA : 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.
CC : 002A05C10
FD : Coronavirus; Localisation; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère
FG : Coronaviridae; Nidovirales; Virus; Appareil respiratoire pathologie; Virose; Infection; Poumon pathologie
ED : Coronavirus; Localization; Protein; Microbiology; Virology; Severe acute respiratory syndrome
EG : Coronaviridae; Nidovirales; Virus; Respiratory disease; Viral disease; Infection; Lung disease
SD : Coronavirus; Localización; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo
LO : INIST-13533.354000129444440210
ID : 05-0229117

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Pascal:05-0229117

Le document en format XML

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<AU>NAL (Baatrice); CHAN (Cheman); KIEN (Francois); SIU (Lewis); TSE (Jane); CHU (Kid); KAM (Jason); STAROPOLI (Isabelle); CRESCENZO-CHAIGNE (Bernadette); ESCRIOU (Nicolas); VAN DER WERF (Sylvie); YUEN (Kwok-Yung); ALTMEYER (Ralf)</AU>
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