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

International Journal of Molecular Sciences

Luiz Saramago³  Mariana Franceschi²  Carlos Logullo¹  Aoi Masuda²  Itabajara da Silva Vaz²  Sandra Estrazulas Farias² 

[1] 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; E-Mail:;Center of Biotechnology, Federal University of Rio Grande do Sul, Avenida Bento Gonçalves, 9500, Prédio 43421, Porto Alegre, RS, CEP 91501-970, Brazil; E-Mails:;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; E-Mail:

关键词: Rhipicephalus (Boophilus) microplus;    triosephosphate isomerase;    glycolytic pathway;    monoclonal antibody;   

DOI  :  10.3390/ijms131013118

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2012 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.