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

Identifieur interne : 002F40 ( Main/Exploration ); précédent : 002F39; suivant : 002F41

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

Auteurs : Christel Schwegmann-Wessels [Allemagne] ; Jörg Glende [Allemagne] ; XIAOFENG REN [Allemagne, République populaire de Chine] ; XIUXIA OU [République populaire de Chine] ; HONGKUI DENG [République populaire de Chine] ; Luis Enjuanes [Espagne] ; Georg Herrler [Allemagne]

Source :

RBID : Pascal:09-0295165

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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.


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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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