Cloning and characterization of thioredoxin peroxidases from Trichinella spiralis

•Thioredoxin peroxidases (TPXs) are developed to protect helminths against oxidative stress.•The ORFs of TsTPX1, TsTPX2 and TsTPX3 were cloned from T. spiralis muscle larvae (ML) with the lengths of 747bp, 588bp and 594bp, respectively.•TsTPX genes could express in all the three developmental stages of T. spiralis.•rTsTPX1 could be recognized by T. spiralis infected swine sera and distinguish from the T. spiralis negative sera.•rTsTPX proteins could deoxidate H2O2 in the present of DTT. The intracellular parasitic nematode, Trichinella spiralis, can initiate a high level of oxidative stress, especially during rapid growth and generative propagation phases. Thioredoxin peroxidases (TPXs) protect helminths against oxidative stress, but none has been identified in T. spiralis. Here, 3 members of the TPX family were cloned from T. spiralis muscle larvae (ML). The lengths of TsTPX ORFs were 747bp, 588bp and 594bp, respectively, and the deduced proteins predicted to contain AhpC-TSA and 1-cys Prx_C domains. Interestingly, qRT-PCR data showed that TsTPX genes were expressed in all three developmental stages of T. spiralis. The TsTPX2 and TsTPX3 genes were up-regulated in day 3 adults (Ad3) compared with newborn larvae (NBL) and ML (P