2-Cys peroxiredoxins from Schistosoma japonicum: the expression profile and localization in the life cycle.

Peroxiredoxin (Prx) is known to be an antioxidant protein that protects the organisms against various oxidative stresses and functions as a signal transductor. Here, we determined the full-length cDNA sequences of three types of Prx from an Asian blood fluke, Schistosoma japonicum: Prx-1, Prx-2 and Prx-3. According to the deduced amino acid sequences, only Prx-3 had a mitochondria-targeting sequence. Using RT-PCR, it was shown that these Prx genes were constitutively expressed in the eggs, cercariae and adult worms of the schistosome. Western blot analysis using antisera specific for each Prx revealed that all the three Prx proteins existed in these developmental stages. By immunolocalization analysis, Prx-1 existed on the surface of a miracidium and in the space between a miracidium and an eggshell. Furthermore, Prx-1 was deposited in the host tissues around the eggs. In adult worms, Prx-1 was not only expressed in the tegument, but also contained in their excretory/secretory products. The surface of the 7 day-schistosomula was stained with anti-Prx-1 antiserum. On the other hand, Prx-2 only existed inside the miracidia in eggs. In addition, Prx-2 was mainly detected in the sub-tegumental tissues, parenchyma, vitelline gland and gut epithelium of the adult worms, but was not detected in the tegument of adults and schistosomula. Taken together with previous reports by other investigators, these data suggest that Prx-1 acts to protect the parasite against the ROS produced by host immune cells, and that Prx-2 plays important roles in intracellular redox signaling and/or in the reduction of ROS generated through the hemoglobinolytic process in the digestive tract.