Interactions of monoclonal antibodies and bovine herpesvirus type 1 (BHV-1) glycoproteins: characterization of their biochemical and immunological properties.

Hybridoma cell lines producing monoclonal antibodies to bovine herpes virus type 1 (BHV-1) were established. The monoclonal antibodies were characterized with respect to their antigen specificities and biological activities. One group of eight monoclonal antibodies precipitated the glycoproteins GVP 3 (180K) and GVP 9 (91K), a second group of thirteen monoclonal antibodies precipitated GVP 6 (130K), GVP 11 (74K) and GVP 16 (55K), and one monoclone secreted antibodies specific for GVP 7 (105K). Analysis of the immune precipitates by electrophoresis under nonreducing conditions suggested that GVP 3 is a dimer of GVP 9. It also indicated that GVP 11 and GVP 16 are components of a disulfide-linked complex, GVP 6. The results, obtained by immunoprecipitation were confirmed by Western blot analysis and an enzyme-linked immunosorbent assay (ELISA), using electrophoretically separated viral glycoproteins. In addition, these techniques demonstrated differential reactivities of the monoclonal antibodies with GVP 11 and GVP 16. The monoclonal antibodies were used to analyze the biological roles of these three sets of glycoproteins. Monoclonal antibodies directed against GVP 3/GVP 9 did not neutralize viral infectivity, but most of them mediated complement-dependent lysis of the infected cell. Individual monoclonal antibodies directed against GVP 6/GVP 11/GVP 16 could neutralize virus as well as participate in complement-mediated lysis. The only available monoclone against GVP 7 did not show any biological activity in the above two assays. Thus, GVP 6/GVP 11/GVP 16 may contain the attachment site of the virion.