MOLECULAR-BASIS OF ANTIGENIC VARIATION BETWEEN THE GLYCOPROTEINS-C OF RESPIRATORY BOVINE HERPESVIRUS-1 (BHV-1) AND NEUROVIRULENT BHV-5

Herpesvirus glycoprotein C (gC) functions as a major virus attachment protein. The gC sequence of the neurovirulent bovine herpesvirus type 5 (BHV-5) virus was determined and compared with the gC sequence of the nonneurovirulent BHV-1. Alignment of the predicted amino acid sequences of BHV-1 and BHV-5 gC ORFs showed that the amino-terminal third of the protein differed between the two viruses. Whole or subgenomic fragments of gC coding regions from both viruses were expressed as trpE-gC fusion proteins in Escherichia coli to map linear epitopes defined by type-specific murine monoclanal antibodies (MAbs). Based on the reactivity of BHV-1-specific MAbs with the recombinant proteins, two epitopes were mapped between BHV-1 gC residues 22 and 172. Unidirectional deletion of these residues at the carboxy end mapped one within residues 22-69 and the other within residues 103-122. Two BHV-5-specific MAbs identified an epitope coding region within BHV-5 gC residues 31-78. Bovine antisera against BHV-1 and BHV-5 showed specificity to BHV-1 gC residues 22-69 and to BHV-5 gC residues 31-78, respectively, in a type-specific manner. (C) 1995 Academic Press, Inc.