Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus.
Identifieur interne : 002B58 ( Main/Exploration ); précédent : 002B57; suivant : 002B59Comparison of vesicular stomatitis virus pseudotyped with the S proteins from a porcine and a human coronavirus.
Auteurs : Christel Schwegmann-We Els [Allemagne] ; Jörg Glende [Allemagne] ; Xiaofeng Ren [République populaire de Chine] ; Xiuxia Qu [République populaire de Chine] ; Hongkui Deng [République populaire de Chine] ; Luis Enjuanes [Espagne] ; Georg Herrler [Allemagne]Source :
- The Journal of general virology [ 0022-1317 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Cricetinae, Délétion de séquence, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (métabolisme), Humains, Lignée cellulaire, Protéines de l'enveloppe virale (métabolisme), Suidae, Vesiculovirus (génétique), Vesiculovirus (pathogénicité), Virulence, Virus de la gastroentérite transmissible (), Virus de la gastroentérite transmissible (génétique), Virus du SRAS (), Virus du SRAS (génétique).
- MESH :
- génétique : Vesiculovirus, Virus de la gastroentérite transmissible, Virus du SRAS.
- métabolisme : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- pathogénicité : Vesiculovirus.
- Animaux, Cricetinae, Délétion de séquence, Glycoprotéine de spicule des coronavirus, Humains, Lignée cellulaire, Suidae, Virulence, Virus de la gastroentérite transmissible, Virus du SRAS.
English descriptors
- KwdEn :
- Animals, Cell Line, Cricetinae, Humans, Membrane Glycoproteins (metabolism), SARS Virus (chemistry), SARS Virus (genetics), Sequence Deletion, Spike Glycoprotein, Coronavirus, Swine, Transmissible gastroenteritis virus (chemistry), Transmissible gastroenteritis virus (genetics), Vesiculovirus (genetics), Vesiculovirus (pathogenicity), Viral Envelope Proteins (metabolism), Virulence.
- MESH :
- chemical , metabolism : Membrane Glycoproteins, Viral Envelope Proteins.
- chemistry : SARS Virus, Transmissible gastroenteritis virus.
- genetics : SARS Virus, Transmissible gastroenteritis virus, Vesiculovirus.
- pathogenicity : Vesiculovirus.
- Animals, Cell Line, Cricetinae, Humans, Sequence Deletion, Spike Glycoprotein, Coronavirus, Swine, Virulence.
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.
DOI: 10.1099/vir.0.009704-0
PubMed: 19264610
Affiliations:
- Allemagne, Espagne, République populaire de Chine
- Basse-Saxe, Communauté de Madrid, Pékin
- Hanovre, Pékin
- Université de Pékin
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Le document en format XML
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<term>Glycoprotéines membranaires (métabolisme)</term>
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<term>Lignée cellulaire</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
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<term>Vesiculovirus (pathogénicité)</term>
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<front><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>
</front>
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