Monoclonal antibodies against structural proteins of bovine viral diarrhea virus |
Chang-hee Kweon1, Yuan Chun Zee2, Hee-jong Woo3 |
1Veterinary Research Institute 2Department of Veterinary Microbiology and immunology Univeristy of California Davis 3Laboratory of Cancer Biology, Harvard Medical School |
소 설사병 바이러스 구조단백에 대한 단크론항체 성상에 대한 연구 |
권창희1, 2, 우희종3 |
1가축위생연구소 2미국 캘리포니아 수의과 대학 3미국 하버드 의과대학 |
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Abstract |
Monoclonal antibodies against structural proteins of bovine viral diarrhea virus(BVDV) were derived by classical hybridoma techniques. These antibodies were characterized by serum neutralization, immunoblotting and immunoprecipitation. The neutralizing monoclonal antibody reacted with the 56kd to 54kd(M.W.) viral protein in western blotting and immunoprecipitation analysis. Although there was no neutralizing activity, another monoclanal antibody reacted with the 45kd protein by immunoprecipitation and with both the 45kd and 36kd proteins in immunoblotting analysis. respectively. Densitometer scanning of purified BVDV and the immunopreipitation of whole virus particles with neutralizing monoclonal antibody revealed the presence of more than twelve viral polypeptides. Although no possible precursor form of protein was identified with the neutralizing monoclonal antibody. the presence of intact virion was detected in the infected cell supernatant immediatelty after pulse labeling, indicating rapid translational processing as well as packaging of the virus. The partial peptide mapping of 45kd and 36kd proteins with Staphylococcus aureus V 8 protease showed that these two proteins are related. |
Key Words:
Monoclonal antibodies, bovine viral diarrhea virus, neutralizing epitope, structural proteins, pulse labeling, partial peptide mapping |
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