Characterization of a novel otubain-like cysteine protease of Cryptosporidium parvum |
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| Institution: | 1. Department of Parasitology and Tropical Medicine, Gyeongsang National University School of Medicine, Jinju 660-751, Republic of Korea;2. Institute of Health Sciences, Gyeongsang National University School of Medicine, Jinju 660-751, Republic of Korea;3. Department of Biochemistry, Gyeongsang National University School of Medicine, Jinju 660-751, Republic of Korea;4. Department of Parasitology and Tropical Medicine, Kyungpook National University School of Medicine, Daegu 700-422, Republic of Korea;1. Laboratory of Parasitology, Joint Faculty of Veterinary Medicine, Kagoshima University, Kagoshima 890-0065, Japan;2. Laboratory of Emerging Infectious Diseases, Joint Faculty of Veterinary Medicine, Kagoshima University, Kagoshima 890-0065, Japan;3. Bacterial and Parasitic Disease Research Division, National Institute of Animal Health, National Agriculture and Food Research Organization, 3-1-5 Kannondai, Tsukuba, Ibaraki 305-0856, Japan;4. Kawasaki, Kanagawa 215-0017, Japan;1. Laboratory of Parasitology, Department of Disease Control, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo 060-0818, Japan;2. Department of Pharmacology and Parasitology, University of Veterinary Science, Nay Pyi Taw 05282, Myanmar;3. Livestock Breeding and Veterinary Department (Head Quarter), Nay Pyi Taw, Myanmar;1. Department of Zoology, Panjab University, Chandigarh-160014, India;2. Department of Parasitology, Postgraduate Institute of Medical Education & Research, Chandigarh, India;1. Department of Infectious Diseases, Hokkaido Institute of Public Health, North 19, West 12, Kitaku, Sapporo 060-0819, Hokkaido, Japan;2. Sapporo Maruyama Zoo, Miyagaoka 3-1, Chuoku, Sapporo 064-0959, Hokkaido, Japan;3. Hamamatsu Zoological Gardens, Kanzanjicho 199, Nishiku, Hamamatsu 431-1209, Shizuoka, Japan;4. Laboratory of Veterinary Internal Medicine, Department of Veterinary Clinical Sciences, Graduate School of Veterinary Medicine, Hokkaido University, North 18, West 9, Kitaku, Sapporo 060-0818, Hokkaido, Japan |
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| Abstract: | Otubains are a recently discovered family of cysteine proteases that participate in the ubiquitin pathway. Here, we partially characterized the biochemical properties of a cysteine protease of Cryptosporidium parvum, which is closely related to otubains. The gene encoding otubain-like cysteine protease of C. parvum (CpOTU) contained the aspartate, cysteine and histidine residues that form the catalytic triad of otubains. The modified ubiquitin-associated domain and LxxL motif were identified in CpOTU. The recombinant CpOTU showed the isopeptidase activity at neutral pH values and its activity was effectively inhibited by ubiquitin aldehyde, N-ethylmaleimide and iodoacetic acid. Interestingly, CpOTU had an unusual C-terminal extension of 217 amino acids compared to mammalian otubains, and the C-terminal extension is essential for the activity of the enzyme. Expression of CpOTU peaked in the oocyst stage of the parasite, which suggested its potential physiological role for the oocyst stage. |
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