Identification of cell membrane proteins linked to susceptibility to bovine viral diarrhoea virus infection.

Three monoclonal antibodies directed against cell surface molecules of bovine cells inhibited subsequent infections with bovine viral diarrhoea virus (BVDV). They specifically blocked the infectivity of three non-cytopathogenic and three cytopathogenic BVDV strains. These results showed that an important mechanism for virus uptake was inhibited. The ligand of the monoclonal antibody BVD/CA 17, which blocked infectivity most efficiently, was found on leukocytes from a wide range of domestic and wild even-toed ungulates using flow cytometric analysis. In contrast, the monoclonal antibodies BVD/CA 26 and BVD/CA 27 appeared to be specific for bovine cells. Immunoprecipitation of labelled bovine cell surface proteins showed that the three monoclonal antibodies bound to proteins with identical relative molecular masses (M(r)). Proteins of an apparent M(r) of 93 K and 60 K were precipitated from lysates of fetal bovine kidney cells irrespectively of the MAbs used.