Immunoaffinity purification and characterization of the envelope protein E1 of hog cholera virus

Abstract

The envelope protein E1 of hog cholera virus (HCV) was isolated by immunoaffinity purification with monoclonal antibodies (MAbs) directed against HCV. E1 consisted of a doublet of glycoproteins which varied in size from 51K to 56K between the three strains tested. E1 contains major antigenic determinants of HCV which are conserved, and are involved in neutralization by MAbs. In infected cells, E1 was found always connected with a glycoprotein of 31K. When N-linked glycans were removed, E1 had a polypeptide backbone of approximately 47K. After proteolytic cleavage of E1 with Staphylococcus protease V8 and after electrophoresis and electrotransfer, peptide fragments containing different antigenic domains of E1 were detected with MAbs directed against HCV.