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Five murine monoclonal antibodies (MAbs) against the NADL strain of bovine viral diarrhea (BVD) virus were developed, identified, and characterized. Four of the MAbs were directed against a 53-kilodalton (kDa) viral protein, and one was specific to a 47-kDa polypeptide. Competitive radioimmunoassay showed that two MAbs were specific to related epitopes of the 53-kDa protein, and the other three MAbs were each specific to a different epitope. The MAbs were used to study heterogeneity among BVD virus strains. Various degrees of reactivity of cytopathic and noncytopathic virus isolates were detected by virus neutralization and immunofluorescence assays. The virus isolates were divided into six groups based on the neutralization test. The results indicated that the 53-kDa glycoprotein of BVD virus is the major protein involved in virus neutralization and that only a few epitopes of the protein contribute to the neutralization. None of the MAbs neutralized all the BVD virus isolates tested in this study, suggesting antigenic variations among BVD virus isolates.

Antigenic variations in bovine viral diarrhea viruses detected by monoclonal antibodies