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Thirteen monoclonal antibodies were prepared against five isolates of bovine viral diarrhea virus (BVDV). All of the antibodies reacted with viral protein gp53. In the absence of serum complement, each antibody neutralized infectivity of BVDV. The monoclonal antibodies were used in a competitive binding assay (CBA) to determine the topographic relationship of neutralizing epitopes on gpS3. Two distinct antigenic domains on the gp53 of cytopathic and noncytopathic isolates of BVDV were identified. The majority of monoclonal antibodies recognized overlapping epitopes in a single domain. A possible second domain was identified by the binding of one monoclonal antibody. A dot-immunoblot assay using denatured viral protein was performed. The results indicated that the neutralizing epitopes on gp 53 were conformationally-dependent. Endoglycosidase treatment of viral glycoproteins significantly reduced or prevented the binding of all thirteen monoclonal antibodies.

Extraction and epitopic analysis of the 53 kd envelope glycoprotein of bovine viral diarrhea virus