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Int. J. Mol. Sci. 2012, 13(10), 13118-13133; doi:10.3390/ijms131013118
Article

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

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Received: 5 July 2012 / Revised: 1 October 2012 / Accepted: 6 October 2012 / Published: 12 October 2012
(This article belongs to the Special Issue Advances in Molecular Immunology)
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Abstract

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.
Keywords: Rhipicephalus (Boophilus) microplus; triosephosphate isomerase; glycolytic pathway; monoclonal antibody Rhipicephalus (Boophilus) microplus; triosephosphate isomerase; glycolytic pathway; monoclonal antibody
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Saramago, L.; Franceschi, M.; Logullo, C.; Masuda, A.; Vaz, I.S., Jr.; Farias, S.E.; Moraes, J. Inhibition of Enzyme Activity of Rhipicephalus (Boophilus) microplus Triosephosphate Isomerase and BME26 Cell Growth by Monoclonal Antibodies. Int. J. Mol. Sci. 2012, 13, 13118-13133.

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