CHARACTERIZATION OF STRUCTURAL AND NONSTRUCTURAL PROTEINS OF HOG-CHOLERA VIRUS BY MEANS OF MONOCLONAL-ANTIBODIES

A panel of 15 monoclonal antibodies, produced against the hog cholera virus, were characterized by radioimmunoprecipitation assays. Using th is panel, we were able to identify 4 sets of monoclonal antibodies pre cipitating each a different viral protein with relative molecular weig ht of 40, 46, 120 kDa, respectively, and a protein complex containing 15, 16, 27, and 55 kDa polypeptides which were further characterized. One monoclonal antibody recognized an antigenic determinant at the C-t erminal cleavage product of the non-structural p 125 of BVDV. The 40 k Da protein was precipitated from the pelleted virions, indicating its structural importance. On the contrary the 46 kDa protein could only b e precipitated from the cell lysate and not from the pelleted virions. The glycosylated 15/16 kDa-55 kDa proteins form a disulfide linked he terodimer on the virus particle with a relative molecular weight of 65 kDa.