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Background  Human babesiosis is an infectious disease that is epidemic in various regions all over the world. The predominant causative pathogen of this disease is the intra-erythrocytic parasite  Babesia microti . The thioredoxin system is one of the major weapons that is used in the resistance to the reactive oxygen species (ROS) and reactive nitrogen species (RNS) produced by host immune system. In other intra-erythrocytic apicomplexans like the malaria parasite  Plasmodium falciparum , anti-oxidative proteins are promising targets for the development of anti-parasitic drugs. However, to date, the sequences and biological properties of thioredoxins and thioredoxin-like molecules of  B. microti  remain unknown. Understanding the molecular characterization and function of  B. microti  thioredoxins may help to develop anti- Babesia  drugs and controlling babesiosis.    Methods  The full-length  B. microti thioredoxin 2  ( BmTrx2 ) gene was obtained using a rapid amplification of cDNA ends (RACE) method, and the deduced BmTrx2 amino acid sequence was analyzed using regular bioinformatics tools. Recombinant BmTrx2 protein was expressed in vitro and purified using His-tag protein affinity chromatography resins. Reverse transcription PCR, quantitative real-time PCR and Western blot were employed to detect the expression and native proteins of BmTrx2. Indirect immunofluorescence assay was used to localize BmTrx2 in  B. microti . Bovine insulin reduction assays were used to determine the enzyme activity of the purified recombinant BmTrx2 protein.    Results  The full-length  BmTrx2  was 564 bp with a 408 bp open reading frame encoding a protein of 135 amino acids. The predicted molecular weight of the protein was 15.5 kDa. A conserved thioredoxin-like family domain was found in  BmTrx2 . The expression of  BmTrx2  was upregulated on both the third and eighth day post-infection in mice, whereas expression was downregulated during the beginning and later stages. The results of Western blot analysis showed the native BmTrx2 in parasite lysates could be detected by mouse anti-BmTrx2 serum and that the recombinant BmTrx2 protein could be recognized by serum of  B. microti -infected mice. Immunofluorescence microscopy showed that BmTrx2 localized in the cell cytoplasm of  B. microti  merozoites in  B. microti- infected red blood cells. The results of bovine insulin reduction assay indicated the purified recombinant BmTrx2 protein possesses antioxidant enzyme activity. Dihydroartemisinin and quinine, known anti-malaria drugs, and clindamycin, a known anti-babesiosis drug, induced significantly higher upregulation of  BmTrx2  mRNA.    Conclusions  Our results indicate that  BmTrx2  is a functional enzyme with antioxidant activity and may be involved in the response of  B. microti  to anti-parasite drugs.    Electronic supplementary material  The online version of this article (10.1186/s13071-018-2619-9) contains supplementary material, which is available to authorized users.

Molecular characterization of Babesia microti thioredoxin (BmTrx2) and its expression patterns induced by antiprotozoal drugs