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.
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3497315 | PMC |
http://dx.doi.org/10.3390/ijms131013118 | DOI Listing |
Int J Mol Sci
October 2012
Laboratory of Biochemistry Hatisaburo Masuda, Institute of Medical Biochemistry, Federal University of Rio de Janeiro, NUPEM - UFRJ/Macaé, Av. São José do Barreto 764, São José do Barreto, Macaé, RJ, CEP 27971-550, Brazil.
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