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

2 Center of Biotechnology, Federal University of Rio Grande do Sul, Avenida Bento Gonçalves, 9500, Prédio 43421, Porto Alegre, RS, CEP 91501-970, Brazil 3 Laboratory of Chemistry and Function of Proteins and Peptides, Animal Experimentation Unit, CBB–UENF, Avenida Alberto Lamego, 2000, Horto, Campos dos Goytacazes, RJ, CEP 28015-620, Brazil 4 Department of Molecular Biology and Biotechnology, Federal University of Rio Grande do Sul, Porto Alegre, RS, CEP 91501-970, Brazil 5 Faculty of Veterinary Sciences, Federal University of Rio Grande do Sul, Porto Alegre, RS, CEP 91501-970, Brazil 6 Department of Physiology, Federal University of Rio Grande do Sul, Porto Alegre, RS, CEP 91501-970, Brazil
* Author to whom correspondence should be addressed.
Received: 5 July 2012; in revised form: 1 October 2012 / Accepted: 6 October 2012 / Published: 12 October 2012
(This article belongs to the Special Issue Advances in Molecular Immunology)
PDF Full-text Download PDF Full-Text [357 KB, uploaded 12 October 2012 10:46 CEST]
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

Article Statistics

Load and display the download statistics.

Citations to this Article

Cite This Article

MDPI and ACS Style

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.

AMA Style

Saramago L, Franceschi M, Logullo C, Masuda A, Vaz IS, Jr, Farias SE, Moraes J. Inhibition of Enzyme Activity of Rhipicephalus (Boophilus) microplus Triosephosphate Isomerase and BME26 Cell Growth by Monoclonal Antibodies. International Journal of Molecular Sciences. 2012; 13(10):13118-13133.

Chicago/Turabian Style

Saramago, Luiz; Franceschi, Mariana; Logullo, Carlos; Masuda, Aoi; Vaz, Itabajara S., Jr.; Farias, Sandra E.; Moraes, Jorge. 2012. "Inhibition of Enzyme Activity of Rhipicephalus (Boophilus) microplus Triosephosphate Isomerase and BME26 Cell Growth by Monoclonal Antibodies." Int. J. Mol. Sci. 13, no. 10: 13118-13133.

Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert