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Characterization of epitopes on a 32 kDa merozoite surface protein of Theileria sergenti
W Z Zhuang1, S Kubota, C Sugimoto
1Department of Epizootiology, Faculty of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Epitopes on a 32 kDa protein, which is an immunodominant major surface protein of Theileria sergenti, recognized by anti-merozoite monoclonal antibodies were characterized. The results of a competitive binding assay between monoclonal antibodies indicated that there were at least three epitopes in this protein. The presence of repeated epitopes was suggested by using two-site enzyme-linked immunosorbent assay. The protein was partitioned into the detergent phase of Triton X-114 extracts, indicating that the 32 kDa protein is an integral membrane protein. Periodate treatment of 32 kDa protein implies that one epitope of the epitopes recognized by monoclonal antibody has a carbohydrate moiety.
Epitopes on a 32 kDa protein, which is an immunodominant major surface protein of Theileria sergenti, recognized by anti-merozoite monoclonal antibodies were characterized. The results of a competitive binding assay between monoclonal antibodies indicated that there were at least three epitopes in this protein. The presence of repeated epitopes was suggested by using two-site enzyme-linked immunosorbent assay. The protein was partitioned into the detergent phase of Triton X-114 extracts, indicating that the 32 kDa protein is an integral membrane protein. Periodate treatment of 32 kDa protein implies that one epitope of the epitopes recognized by monoclonal antibody has a carbohydrate moiety.