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Cell surface molecules involved in infection mediated by lymphocytic choriomeningitis virus glycoprotein.


ABSTRACT: The glycoprotein (GP) of lymphocytic choriomeningitis virus (LCMV), the prototype arenavirus, is a promising envelope protein of lentiviral pseudotype vectors for gene therapy. The distribution of dystroglycan, a known receptor for LCMV, cannot explain the narrow tropism of LCMV-GP-pseudotypes. Here, we examined whether infection of LCMV-GP-pseudotypes was affected by the expression of four cell surface molecules-Axl and Tyro3 (from the TAM family) and DC-SIGN and LSECtin (from the C-type lectin family)-that are known receptors of Lassa virus, another arenavirus. All four molecules enhanced LCMV-GP-pseudotype infection of cells. These results help explain the tropism of LCMV-GP-pseudotypes and further our understanding of LCMV infection in animals.

SUBMITTER: Shimojima M 

PROVIDER: S-EPMC6133296 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature

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Cell surface molecules involved in infection mediated by lymphocytic choriomeningitis virus glycoprotein.

Shimojima Masayuki M   Kawaoka Yoshihiro Y  

The Journal of veterinary medical science 20120601 10


The glycoprotein (GP) of lymphocytic choriomeningitis virus (LCMV), the prototype arenavirus, is a promising envelope protein of lentiviral pseudotype vectors for gene therapy. The distribution of dystroglycan, a known receptor for LCMV, cannot explain the narrow tropism of LCMV-GP-pseudotypes. Here, we examined whether infection of LCMV-GP-pseudotypes was affected by the expression of four cell surface molecules-Axl and Tyro3 (from the TAM family) and DC-SIGN and LSECtin (from the C-type lectin  ...[more]

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