Characterization of the thioredoxin peroxidase from Cryptosporidium parvum |
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| Authors: | Joung Migyo Yoon Sejoung Choi Kyungmi Kim Joung-Yeon Park Woo-Yoon Yu Jae-Ran |
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| Institution: | aDepartment of Environmental and Tropical Medicine, Konkuk University, School of Medicine, Seoul 143-701, Republic of Korea;bDepartment of Malaria and Parasitic Diseases, Korea National Institute of Health, Korean Center for Disease Control and Prevention, Osong 363-951, Republic of Korea;cDepartment of Radiation Oncology, College of Medicine, Chungbuk National University, Cheongju 361-763, Republic of Korea |
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| Abstract: | 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. |
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| Keywords: | Cryptosporidium parvum Thioredoxin peroxidase |
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