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GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry

Identifieur interne : 000652 ( PascalFrancis/Curation ); précédent : 000651; suivant : 000653

GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry

Auteurs : Jeroen Corver [Pays-Bas] ; Rene Broer [Pays-Bas] ; Puck Van Kasteren [Pays-Bas] ; Willy Spaan [Pays-Bas]

Source :

RBID : Pascal:07-0486287

Descripteurs français

English descriptors

Abstract

Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.
pA  
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A03   1    @0 J. virol.
A05       @2 81
A06       @2 15
A08 01  1  ENG  @1 GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry
A11 01  1    @1 CORVER (Jeroen)
A11 02  1    @1 BROER (Rene)
A11 03  1    @1 VAN KASTEREN (Puck)
A11 04  1    @1 SPAAN (Willy)
A14 01      @1 Department of Medical Microbiology, Center of Infectious Diseases, Leiden University Medical Center @2 2300 RC Leiden @3 NLD @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 4 aut.
A20       @1 8352-8355
A21       @1 2007
A23 01      @0 ENG
A43 01      @1 INIST @2 13592 @5 354000149980000540
A44       @0 0000 @1 © 2007 INIST-CNRS. All rights reserved.
A45       @0 13 ref.
A47 01  1    @0 07-0486287
A60       @1 P
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A64 01  1    @0 Journal of virology
A66 01      @0 USA
C01 01    ENG  @0 Recently, a paper was published in which it was proposed that the GxxxG motif of the severe acute respiratory syndrome (SARS) coronavirus spike (S) protein transmembrane domain plays a vital role in oligomerization of the protein (E. Arbely, Z. Granot, I. Kass, J. Orly, and I. T. Arkin, Biochemistry 45:11349-11356, 2006). Here, we show that the GxxxG motif is not involved in SARS S oligomerization by trimerization analysis of S GxxxG mutant proteins. In addition, the capability of S to mediate entry of SARS S-pseudotyped particles overall was affected moderately in the mutant proteins, also arguing for a nonvital role for the GxxxG motif in SARS coronavirus entry.
C02 01  X    @0 002A05C10
C03 01  X  FRE  @0 Coronavirus @2 NW @5 01
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 Aigu @5 05
C03 02  X  ENG  @0 Acute @5 05
C03 02  X  SPA  @0 Agudo @5 05
C03 03  X  FRE  @0 Glycoprotéine @5 06
C03 03  X  ENG  @0 Glycoprotein @5 06
C03 03  X  SPA  @0 Glicoproteína @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
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
N21       @1 316
N44 01      @1 OTO
N82       @1 OTO

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Pascal:07-0486287

Le document en format XML

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