Lymphocytic choriomeningitis virus. VI. Isolation of a glycoprotein mediating neutralization

Virology. 1983 Oct 15;130(1):247-51. doi: 10.1016/0042-6822(83)90135-6.

Abstract

A structural glycoprotein of lymphocytic choriomeningitis virus was obtained in pure form by immunoaffinity chromatography using a monoclonal antibody with high neutralizing activity. It blocked neutralization of viral infectivity by antibody and in polyacrylamide gel electrophoresis it migrated with an apparent molecular weight of 44 X 10(3). We conclude that the isolated material is identical with the previously described gp44 (GP-1).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / analysis
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Glycoproteins / immunology
  • Glycoproteins / isolation & purification*
  • L Cells / microbiology
  • Lymphocytic choriomeningitis virus / immunology
  • Lymphocytic choriomeningitis virus / isolation & purification*
  • Mice
  • Molecular Weight
  • Neutralization Tests
  • Rabbits
  • Viral Proteins / immunology
  • Viral Proteins / isolation & purification*

Substances

  • Antibodies, Monoclonal
  • Glycoproteins
  • Viral Proteins