Characterization of the thioredoxin peroxidase from Cryptosporidium parvum

[Display omitted] ► Recombinant thioredoxin peroxidase of Cryptosporidium parvum (CpTPx) was expressed. ► CpTPx is a two-cysteine peroxiredoxin containing cysteines at positions 49 and 170. ► CpTPx exhibited substantial thiol-dependent peroxidase activity. ► CpTPx protected plasmid DNA from damage by metal-catalyzed oxidation in vitro. ► CpTPx was expressed mainly in the cytoplasm of C. parvum. Cryptosporidium parvum can survive exposure to harsh environmental conditions, various disinfectants, and high doses of γ-radiation. Recently, it was found that the expression of thioredoxin peroxidase (CpTPx) in C. parvum increased after a high dose of γ-irradiation to the parasite. CpTPx is a two-cysteine peroxiredoxin that contains cysteines at positions 49 and 170. Recombinant CpTPx fused to an N-terminal hexahistidine sequence, (His)6-CpTPx, exhibited substantial thiol-dependent peroxidase activity that protected plasmid DNA from damage by metal-catalyzed oxidation in vitro. (His)6-CpTPx was used to screen sera from C. parvum-infected mice and humans for antibodies against CpTPx. In Western blots, 10% of the mouse sera and 20% of the human sera reacted with (His)6-CpTPx, suggesting that after infection by C. parvum CpTPx can induce a host-immune reaction but is not a major antigen. Immunolocalization studies revealed that CpTPx is expressed mainly in the cytoplasm of C. parvum at various developmental stages.