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Cloning and Characterization of a 2-Cys Peroxiredoxin from Babesia gibsoni OAK
MASATANI, Tatsunori; ASADA, Masahito; ICHIKAWA-SEKI, Madoka; USUI, Miho; TERKAWI, Mohamad A.; HAYASHI, Kei; KAWAZU, Shin-ichiro; XUAN, Xuenan; 河津, 信一郎; 玄, 学南.
Peroxiredoxins (Prxs) are a family of antioxidant enzymes. Here, we cloned a 2-Cys Prx, BgTPx-1, from the canine Babesia parasite B. gibsoni. Sequence identity between BgTPx-1 and 2-Cys Prx of B. bovis was 81% at the amino acid level. Enzyme activity assay by using recombinant BgTPx-1 (rBgTPx-1) indicated that BgTPx-1 has antioxidant activity. Antiserum from a mouse immunized with rBgTPx-1 reacted with parasite lysates and detect a protein with a monomeric size of 22 kDa and also a 44 kDa protein, which might be an inefficiently reduced dimer. BgTPx-1 was expressed in the cytoplasm of B. gibsoni merozoites. These results suggest that the BgTPx-1 may play a role to control redox balance in the cytoplasm of B. gibsoni.
Palavras-chave: Antioxidant activity; Babesia gibsoni; Canine; Peroxiredoxin.
Ano: 2014 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/3925
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