Cloning And Identification Of Two Kinds Of Thioredoxin In Babesia Microti

Babesia microti,an intracell?lar parasite, a kind of apicomplexan protozoa, is lack of catalase and glutathione peroxidase andresiststo the ROS and the RNS in the host depending on the thioredoxin system.The function of the Trxs of Babeisia is still unknown up to date. In this paper, two kinds of Trxs, named BmTrx5 and BmTrx6 were isolated from the transcriptome of B. microti.BmTrx5, with a f?ll length of 770 bp and conposed of 201 amino acid, has no signal peptide but contains a Trx domain. BmTrx6, with a f?ll length of 660 bp and conposed of 142 amino acid, has no signal peptide but contains a Trx-like and a DIMI domain.The native proteins of BmTrx5 and BmTrx6 were detected in the parasites by western blotting and IFAT. Through the ins?lin reduction to assay Trx5 and Trx6 activity and its principle: TRX in the role of TrxR, NADPH can change from oxidized to prototype and reduction type thioredoxin(TRX-(SH) 2) thiol, ins?lin action and variable is oxidized and oxidized thioredoxin(TRX- S2) containing dis?lfide bonds and become a prototype in the role of TrxR, NADPH, the process requires NADPH cons?Mption, making it into NADPH to NADP + and reduced TRX to and ins?lin action and repeat the process. With the depletion of NADPH, the absorption value of the reaction system at 340nm(O Dzhi) will be reduced.The recombinant proteins of both genes demonstrated the reductive activities. This study provides the important information for the development of anti-parasite drugs and vaccines.