Inhibition of enzyne activity of Riphicephalus (Boophilus) microplus triosephosphate isomerase and BME26 cell growth by monoclonal antibodies

• Autor(a) principal: Saramago, Luiz
• Data de Publicação: 2012
• Outros Autores: Franceschi, Mariana Ferreira da Silva, Logullo, Carlos, Masuda, Aoi, Vaz Junior, Itabajara da Silva, Farias, Sandra Estrazulas, Moraes, Jorge
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UFRGS
• Texto Completo: http://hdl.handle.net/10183/267613
• topic: Anticorpos monoclonais; Biotecnologia : Animal; Riphicephalus (Boophilus) microplus; Triosephosphate isomerase; Glycolytic pathway; Monoclonal antibody

In the present work, we produced two monoclonal antibodies (BrBm37 and BrBm38) and tested their action against the triosephosphate isomerase of Rhipicephalus (Boophilus) microplus (RmTIM). These antibodies recognize epitopes on both the native and recombinant forms of the protein. rRmTIM inhibition by BrBm37 was up to 85% whereas that of BrBrm38 was 98%, depending on the antibody-enzyme ratio. RmTIM activity was lower in ovarian, gut, and fat body tissue extracts treated with BrBm37 or BrBm38 mAbs. The proliferation of the embryonic tick cell line (BME26) was inhibited by BrBm37 and BrBm38 mAbs. In summary, the results reveal that it is possible to interfere with the RmTIM function using antibodies, even in intact cells.