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Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes.

Authors
  • C Lindqvist
  • M Schmidt
  • J Heinola
  • R Jaatinen
  • M Osterblad
  • A Salmi
  • S Keränen
  • K Akerman
  • C Oker-Blom
Publication Date
Sep 01, 1994
Source
PMC
Keywords
Disciplines
  • Biology
  • Medicine
License
Unknown

Abstract

Three monoclonal antibodies, termed 4E10, 1E11:10, and 2D9:1, were generated against rubella virus. Immunoblot analysis with purified authentic rubella virus or recombinant baculovirus-expressed rubella virus structural proteins E1, E2, and C demonstrated that they were directed against the E1 envelope glycoprotein of the rubella virus particle. By using the yeast Ty virus-like particle system, it was possible to map the binding site of 1E11:10 within amino acids 236 to 286 of the E1 protein and the binding sites of 2D9:1 and 4E10 outside this region. Immunoaffinity purification with these monoclonal antibodies made it evident that they are useful for obtaining large quantities of pure baculovirus-expressed rubella virus envelope protein E1. The diagnostic potential of this immunoaffinity-purified recombinant rubella virus E1 protein compared with that of authentic rubella virus is demonstrated.

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