吉氏巴贝斯虫2-半胱氨酸过氧化物酶的克隆与鉴定
Cloning and characterization of a 2-Cys peroxiredoxin from Babesia gibsoni.
作者信息
Masatani Tatsunori, Asada Masahito, Ichikawa-Seki Madoka, Usui Miho, Terkawi Mohamad A, Hayashi Kei, Kawazu Shin-Ichiro, Xuan Xuenan
机构信息
National Research Center for Protozoan Diseases, Obihiro University of Agriculture and Veterinary Medicine, Inada-cho, Obihiro, Hokkaido 080-8555, Japan.
出版信息
J Vet Med Sci. 2014 Jan;76(1):139-43. doi: 10.1292/jvms.13-0274. Epub 2013 Sep 11.
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.
过氧化物还原酶（Prxs）是一类抗氧化酶。在此，我们从犬巴贝斯虫吉氏巴贝斯虫中克隆了一种双半胱氨酸Prx，即BgTPx-1。BgTPx-1与牛巴贝斯虫的双半胱氨酸Prx在氨基酸水平上的序列同一性为81%。使用重组BgTPx-1（rBgTPx-1）进行的酶活性测定表明BgTPx-1具有抗氧化活性。用rBgTPx-1免疫的小鼠产生的抗血清与寄生虫裂解物发生反应，并检测到一种单体大小为22 kDa的蛋白质以及一种44 kDa的蛋白质，后者可能是还原效率低下的二聚体。BgTPx-1在吉氏巴贝斯虫裂殖子的细胞质中表达。这些结果表明BgTPx-1可能在控制吉氏巴贝斯虫细胞质中的氧化还原平衡方面发挥作用。
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