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

J Vet Med Sci. 2012 Oct;74(10):1363-6. doi: 10.1292/jvms.12-0176. Epub 2012 Jun 1.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arenaviridae Infections / immunology*
  • Arenaviridae Infections / virology*
  • Cell Adhesion Molecules / immunology
  • Genetic Therapy / methods
  • Genetic Vectors / immunology
  • Glycoproteins / immunology*
  • Humans
  • Jurkat Cells
  • Lectins, C-Type / immunology
  • Lymphocytic choriomeningitis virus / immunology*
  • Receptor Protein-Tyrosine Kinases / immunology
  • Receptors, Cell Surface / immunology
  • Receptors, Virus / immunology*


  • CLEC4G protein, human
  • Cell Adhesion Molecules
  • DC-specific ICAM-3 grabbing nonintegrin
  • Glycoproteins
  • Lectins, C-Type
  • Receptors, Cell Surface
  • Receptors, Virus
  • Receptor Protein-Tyrosine Kinases
  • TYRO3 protein, human