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Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus

Identifieur interne : 000206 ( PascalFrancis/Corpus ); précédent : 000205; suivant : 000207

Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus

Auteurs : Christel Schwegmann-Wessels ; Jörg Glende ; XIAOFENG REN ; XIUXIA OU ; HONGKUI DENG ; Luis Enjuanes ; Georg Herrler

Source :

RBID : Pascal:09-0295165

Descripteurs français

English descriptors

Abstract

The surface proteins S of severe acute respiratory syndrome coronavirus (SARS-CoV) and transmissible gastroenteritis virus (TGEV) were compared for their ability to mediate infection of viral pseudotypes based on vesicular stomatitis virus (VSV). The cell tropism of the respective pseudotypes corresponded to the tropism of the viruses from which the S protein was derived. Higher infectivity values were obtained with the SARS-CoV S protein than with the TGEV S protein. Differences were observed with respect to the importance of the cytoplasmic tail and the membrane anchor of the S proteins. In the case of the SARS-CoV S protein, truncation of the cytoplasmic tail resulted in increased infectivity. For the TGEV S protein, the inactivation of an intracellular retention signal in the cytoplasmic tail was required. Exchange of the membrane anchor of the S proteins led to a low infection efficiency. Our results indicate that related glycoproteins may show substantial differences in their ability to mediate pseudotype infection.

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 90
A06       @3 p. 7
A08 01  1  ENG  @1 Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus
A11 01  1    @1 SCHWEGMANN-WESSELS (Christel)
A11 02  1    @1 GLENDE (Jörg)
A11 03  1    @1 XIAOFENG REN
A11 04  1    @1 XIUXIA OU
A11 05  1    @1 HONGKUI DENG
A11 06  1    @1 ENJUANES (Luis)
A11 07  1    @1 HERRLER (Georg)
A14 01      @1 Institute of Virology, University of Veterinary Medicine Hannover @2 Hannover @3 DEU @Z 1 aut. @Z 2 aut. @Z 3 aut. @Z 7 aut.
A14 02      @1 College of Veterinary Medicine, Northeast Agricultural University, 59 Mucai Street @2 150030 Harbin @3 CHN @Z 3 aut.
A14 03      @1 Department of Cell Biology and Genetics, College of Life Sciences, Peking University @2 Beijing 100871 @3 CHN @Z 4 aut. @Z 5 aut.
A14 04      @1 Centro Nacional de Biotecnologia, CSIC, Department of Molecular and Cell Biology, Campus Universitario de Cantoblanco, Darwin 3 @2 28049 Madrid @3 ESP @Z 6 aut.
A20       @1 1724-1729
A21       @1 2009
A23 01      @0 ENG
A43 01      @1 INIST @2 13533 @5 354000187157980190
A44       @0 0000 @1 © 2009 INIST-CNRS. All rights reserved.
A45       @0 3/4 p.
A47 01  1    @0 09-0295165
A60       @1 P
A61       @0 A
A64 01  1    @0 Journal of general virology
A66 01      @0 GBR
C01 01    ENG  @0 The surface proteins S of severe acute respiratory syndrome coronavirus (SARS-CoV) and transmissible gastroenteritis virus (TGEV) were compared for their ability to mediate infection of viral pseudotypes based on vesicular stomatitis virus (VSV). The cell tropism of the respective pseudotypes corresponded to the tropism of the viruses from which the S protein was derived. Higher infectivity values were obtained with the SARS-CoV S protein than with the TGEV S protein. Differences were observed with respect to the importance of the cytoplasmic tail and the membrane anchor of the S proteins. In the case of the SARS-CoV S protein, truncation of the cytoplasmic tail resulted in increased infectivity. For the TGEV S protein, the inactivation of an intracellular retention signal in the cytoplasmic tail was required. Exchange of the membrane anchor of the S proteins led to a low infection efficiency. Our results indicate that related glycoproteins may show substantial differences in their ability to mediate pseudotype infection.
C02 01  X    @0 002A05C10
C03 01  X  FRE  @0 Virus stomatite vésiculeuse @2 NW @5 01
C03 01  X  ENG  @0 Vesicular stomatitis virus @2 NW @5 01
C03 01  X  SPA  @0 Vesicular stomatitis virus @2 NW @5 01
C03 02  X  FRE  @0 Porcin @5 02
C03 02  X  ENG  @0 Swine @5 02
C03 02  X  SPA  @0 Porcino @5 02
C03 03  X  FRE  @0 Porc @5 03
C03 03  X  ENG  @0 Pig @5 03
C03 03  X  SPA  @0 Cerdo @5 03
C03 04  X  FRE  @0 Homme @5 04
C03 04  X  ENG  @0 Human @5 04
C03 04  X  SPA  @0 Hombre @5 04
C03 05  X  FRE  @0 Etude comparative @5 05
C03 05  X  ENG  @0 Comparative study @5 05
C03 05  X  SPA  @0 Estudio comparativo @5 05
C03 06  X  FRE  @0 Protéine @5 06
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C03 06  X  SPA  @0 Proteína @5 06
C03 07  X  FRE  @0 Animal @5 07
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C03 08  X  ENG  @0 Coronavirus @2 NW @5 08
C03 08  X  SPA  @0 Coronavirus @2 NW @5 08
C03 09  X  FRE  @0 Microbiologie @5 09
C03 09  X  ENG  @0 Microbiology @5 09
C03 09  X  SPA  @0 Microbiología @5 09
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C07 01  X  SPA  @0 Vesiculovirus @2 NW
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C07 02  X  SPA  @0 Rhabdoviridae @2 NW
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C07 03  X  SPA  @0 Mononegavirales @2 NW
C07 04  X  FRE  @0 Virus @2 NW
C07 04  X  ENG  @0 Virus @2 NW
C07 04  X  SPA  @0 Virus @2 NW
C07 05  X  FRE  @0 Artiodactyla @2 NS
C07 05  X  ENG  @0 Artiodactyla @2 NS
C07 05  X  SPA  @0 Artiodactyla @2 NS
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C07 11  X  SPA  @0 Veterinario @5 13
N21       @1 215
N44 01      @1 OTO
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Format Inist (serveur)

NO : PASCAL 09-0295165 INIST
ET : Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus
AU : SCHWEGMANN-WESSELS (Christel); GLENDE (Jörg); XIAOFENG REN; XIUXIA OU; HONGKUI DENG; ENJUANES (Luis); HERRLER (Georg)
AF : Institute of Virology, University of Veterinary Medicine Hannover/Hannover/Allemagne (1 aut., 2 aut., 3 aut., 7 aut.); College of Veterinary Medicine, Northeast Agricultural University, 59 Mucai Street/150030 Harbin/Chine (3 aut.); Department of Cell Biology and Genetics, College of Life Sciences, Peking University/Beijing 100871/Chine (4 aut., 5 aut.); Centro Nacional de Biotecnologia, CSIC, Department of Molecular and Cell Biology, Campus Universitario de Cantoblanco, Darwin 3/28049 Madrid/Espagne (6 aut.)
DT : Publication en série; Niveau analytique
SO : Journal of general virology; ISSN 0022-1317; Coden JGVIAY; Royaume-Uni; Da. 2009; Vol. 90; No. p. 7; Pp. 1724-1729; Bibl. 3/4 p.
LA : Anglais
EA : The surface proteins S of severe acute respiratory syndrome coronavirus (SARS-CoV) and transmissible gastroenteritis virus (TGEV) were compared for their ability to mediate infection of viral pseudotypes based on vesicular stomatitis virus (VSV). The cell tropism of the respective pseudotypes corresponded to the tropism of the viruses from which the S protein was derived. Higher infectivity values were obtained with the SARS-CoV S protein than with the TGEV S protein. Differences were observed with respect to the importance of the cytoplasmic tail and the membrane anchor of the S proteins. In the case of the SARS-CoV S protein, truncation of the cytoplasmic tail resulted in increased infectivity. For the TGEV S protein, the inactivation of an intracellular retention signal in the cytoplasmic tail was required. Exchange of the membrane anchor of the S proteins led to a low infection efficiency. Our results indicate that related glycoproteins may show substantial differences in their ability to mediate pseudotype infection.
CC : 002A05C10
FD : Virus stomatite vésiculeuse; Porcin; Porc; Homme; Etude comparative; Protéine; Animal; Coronavirus; Microbiologie
FG : Vesiculovirus; Rhabdoviridae; Mononegavirales; Virus; Artiodactyla; Ungulata; Mammalia; Vertebrata; Coronaviridae; Nidovirales; Vétérinaire
ED : Vesicular stomatitis virus; Swine; Pig; Human; Comparative study; Protein; Animal; Coronavirus; Microbiology
EG : Vesiculovirus; Rhabdoviridae; Mononegavirales; Virus; Artiodactyla; Ungulata; Mammalia; Vertebrata; Coronaviridae; Nidovirales; Veterinary
SD : Vesicular stomatitis virus; Porcino; Cerdo; Hombre; Estudio comparativo; Proteína; Animal; Coronavirus; Microbiología
LO : INIST-13533.354000187157980190
ID : 09-0295165

Links to Exploration step

Pascal:09-0295165

Le document en format XML

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<div type="abstract" xml:lang="en">The surface proteins S of severe acute respiratory syndrome coronavirus (SARS-CoV) and transmissible gastroenteritis virus (TGEV) were compared for their ability to mediate infection of viral pseudotypes based on vesicular stomatitis virus (VSV). The cell tropism of the respective pseudotypes corresponded to the tropism of the viruses from which the S protein was derived. Higher infectivity values were obtained with the SARS-CoV S protein than with the TGEV S protein. Differences were observed with respect to the importance of the cytoplasmic tail and the membrane anchor of the S proteins. In the case of the SARS-CoV S protein, truncation of the cytoplasmic tail resulted in increased infectivity. For the TGEV S protein, the inactivation of an intracellular retention signal in the cytoplasmic tail was required. Exchange of the membrane anchor of the S proteins led to a low infection efficiency. Our results indicate that related glycoproteins may show substantial differences in their ability to mediate pseudotype infection.</div>
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<s0>A</s0>
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<s0>Journal of general virology</s0>
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<s0>The surface proteins S of severe acute respiratory syndrome coronavirus (SARS-CoV) and transmissible gastroenteritis virus (TGEV) were compared for their ability to mediate infection of viral pseudotypes based on vesicular stomatitis virus (VSV). The cell tropism of the respective pseudotypes corresponded to the tropism of the viruses from which the S protein was derived. Higher infectivity values were obtained with the SARS-CoV S protein than with the TGEV S protein. Differences were observed with respect to the importance of the cytoplasmic tail and the membrane anchor of the S proteins. In the case of the SARS-CoV S protein, truncation of the cytoplasmic tail resulted in increased infectivity. For the TGEV S protein, the inactivation of an intracellular retention signal in the cytoplasmic tail was required. Exchange of the membrane anchor of the S proteins led to a low infection efficiency. Our results indicate that related glycoproteins may show substantial differences in their ability to mediate pseudotype infection.</s0>
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<s5>04</s5>
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<s5>05</s5>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NS</s2>
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<s0>Artiodactyla</s0>
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<s0>Artiodactyla</s0>
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<s0>Vertebrata</s0>
<s2>NS</s2>
</fC07>
<fC07 i1="08" i2="X" l="SPA">
<s0>Vertebrata</s0>
<s2>NS</s2>
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<fC07 i1="09" i2="X" l="FRE">
<s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="09" i2="X" l="ENG">
<s0>Coronaviridae</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="09" i2="X" l="SPA">
<s0>Coronaviridae</s0>
<s2>NW</s2>
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<fC07 i1="10" i2="X" l="FRE">
<s0>Nidovirales</s0>
<s2>NW</s2>
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<fC07 i1="10" i2="X" l="ENG">
<s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="10" i2="X" l="SPA">
<s0>Nidovirales</s0>
<s2>NW</s2>
</fC07>
<fC07 i1="11" i2="X" l="FRE">
<s0>Vétérinaire</s0>
<s5>13</s5>
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<s0>Veterinary</s0>
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<fN21>
<s1>215</s1>
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<NO>PASCAL 09-0295165 INIST</NO>
<ET>Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus</ET>
<AU>SCHWEGMANN-WESSELS (Christel); GLENDE (Jörg); XIAOFENG REN; XIUXIA OU; HONGKUI DENG; ENJUANES (Luis); HERRLER (Georg)</AU>
<AF>Institute of Virology, University of Veterinary Medicine Hannover/Hannover/Allemagne (1 aut., 2 aut., 3 aut., 7 aut.); College of Veterinary Medicine, Northeast Agricultural University, 59 Mucai Street/150030 Harbin/Chine (3 aut.); Department of Cell Biology and Genetics, College of Life Sciences, Peking University/Beijing 100871/Chine (4 aut., 5 aut.); Centro Nacional de Biotecnologia, CSIC, Department of Molecular and Cell Biology, Campus Universitario de Cantoblanco, Darwin 3/28049 Madrid/Espagne (6 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of general virology; ISSN 0022-1317; Coden JGVIAY; Royaume-Uni; Da. 2009; Vol. 90; No. p. 7; Pp. 1724-1729; Bibl. 3/4 p.</SO>
<LA>Anglais</LA>
<EA>The surface proteins S of severe acute respiratory syndrome coronavirus (SARS-CoV) and transmissible gastroenteritis virus (TGEV) were compared for their ability to mediate infection of viral pseudotypes based on vesicular stomatitis virus (VSV). The cell tropism of the respective pseudotypes corresponded to the tropism of the viruses from which the S protein was derived. Higher infectivity values were obtained with the SARS-CoV S protein than with the TGEV S protein. Differences were observed with respect to the importance of the cytoplasmic tail and the membrane anchor of the S proteins. In the case of the SARS-CoV S protein, truncation of the cytoplasmic tail resulted in increased infectivity. For the TGEV S protein, the inactivation of an intracellular retention signal in the cytoplasmic tail was required. Exchange of the membrane anchor of the S proteins led to a low infection efficiency. Our results indicate that related glycoproteins may show substantial differences in their ability to mediate pseudotype infection.</EA>
<CC>002A05C10</CC>
<FD>Virus stomatite vésiculeuse; Porcin; Porc; Homme; Etude comparative; Protéine; Animal; Coronavirus; Microbiologie</FD>
<FG>Vesiculovirus; Rhabdoviridae; Mononegavirales; Virus; Artiodactyla; Ungulata; Mammalia; Vertebrata; Coronaviridae; Nidovirales; Vétérinaire</FG>
<ED>Vesicular stomatitis virus; Swine; Pig; Human; Comparative study; Protein; Animal; Coronavirus; Microbiology</ED>
<EG>Vesiculovirus; Rhabdoviridae; Mononegavirales; Virus; Artiodactyla; Ungulata; Mammalia; Vertebrata; Coronaviridae; Nidovirales; Veterinary</EG>
<SD>Vesicular stomatitis virus; Porcino; Cerdo; Hombre; Estudio comparativo; Proteína; Animal; Coronavirus; Microbiología</SD>
<LO>INIST-13533.354000187157980190</LO>
<ID>09-0295165</ID>
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