Inhibition of Enzyme Activity of Rhipicephalus (Boophilus) microplus Triosephosphate Isomerase and BME26 Cell Growth by Monoclonal Antibodies

• Main Authors: Jorge Moraes, Sandra Estrazulas Farias, Itabajara da Silva Vaz, Aoi Masuda, Mariana Franceschi, Carlos Logullo, Luiz Saramago
• Format: Article
• Language: English
• Published: MDPI AG 2012-10-01
• Series: International Journal of Molecular Sciences
• Subjects: Rhipicephalus (Boophilus) microplus; triosephosphate isomerase; glycolytic pathway; monoclonal antibody
• Online Access: http://www.mdpi.com/1422-0067/13/10/13118

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.