Cloning and Characterization of a 2-Cys Peroxiredoxin from Babesia gibsoni

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) ind...

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Detalles Bibliográficos
Autores principales: MASATANI, Tatsunori, ASADA, Masahito, ICHIKAWA-SEKI, Madoka, USUI, Miho, TERKAWI, Mohamad A., HAYASHI, Kei, KAWAZU, Shin-ichiro, XUAN, Xuenan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Japanese Society of Veterinary Science 2013
Materias:
Parasitology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3979947/
https://www.ncbi.nlm.nih.gov/pubmed/24025459
http://dx.doi.org/10.1292/jvms.13-0274
Descripción
Sumario: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.

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