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Published on: February 14, 2011
Monoclonal antibodies to the recombinant protein TmpA of the Treponema pallidum
Adys I Brito Moreno1, Carmen Acosta Bas, Maya Rodríguez
1Laboratorio de Anticuerpos Monoclonales, Centro de Inmunoensayo, Calle 134 y ave. 25, Apartado 6653, Cubanacán, Playa, Havana City, Cuba.
Spleen cells from BALB/c mice immunized with recombinant TmpA were fused with mouse myeloma cells (P3/X63-Ag8), and five hybridomas secreting monoclonal antibodies were obtained. These hybridomas specifically recognize TmpA and do not cross-react with other molecules such as recombinant HBsAg of HBV and synthetic HCV core peptides. The monoclonal antibodies were IgG1 subclass and ascitic fluid from these hybridomas was purified by affinity chromatography on Protein A-Sepharose CL-4B column to isolate the IgG1 active fraction. The affinity constant of these monoclonal antibodies ranged from 6.4 x 10(8) and 1.73 x 10(10) M(-1).
Spleen cells from BALB/c mice immunized with recombinant TmpA were fused with mouse myeloma cells (P3/X63-Ag8), and five hybridomas secreting monoclonal antibodies were obtained. These hybridomas specifically recognize TmpA and do not cross-react with other molecules such as recombinant HBsAg of HBV and synthetic HCV core peptides. The monoclonal antibodies were IgG1 subclass and ascitic fluid from these hybridomas was purified by affinity chromatography on Protein A-Sepharose CL-4B column to isolate the IgG1 active fraction. The affinity constant of these monoclonal antibodies ranged from 6.4 x 10(8) and 1.73 x 10(10) M(-1).
