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Cloning and characterization of a 2-Cys peroxiredoxin from Babesia gibsoni.


ABSTRACT: 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.

SUBMITTER: Masatani T 

PROVIDER: S-EPMC3979947 | biostudies-literature | 2014 Jan

REPOSITORIES: biostudies-literature

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Cloning and characterization of a 2-Cys peroxiredoxin from Babesia gibsoni.

Masatani Tatsunori T   Asada Masahito M   Ichikawa-Seki Madoka M   Usui Miho M   Terkawi Mohamad A MA   Hayashi Kei K   Kawazu Shin-Ichiro S   Xuan Xuenan X  

The Journal of veterinary medical science 20130911 1


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 protei  ...[more]

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