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The schistosoma japonicum causes the schistosomiasis disease that severely threatens animals life and hampers the economic and social development.Developing a vaccine for domestic animals remains a research priority to the control of schistosomiasis.The soluble immature egg antigen (SIEA) 26-28 kDa had been proven to be a very important and potent vaccine candidate.The SIEA 26-28 kDa component was isolated and purified by SDS-PAGE and RP-HPLC.The SIEA was separated by 2-DE which revealed about 114 spots in the proteome of Schistosoma japonicumand the 23th spot is the dominant component of SIEA 26-28 kDa proteins.The tryptic peptide products spot 23 from the 2-DE gels analyzed by MALDI-TOF.Mascot search result shows that the SIEA 26-28 kDa 2-DE protein spot 23 matches thioredoxin peroxidase-3,with score value as high as 131.Eleven peptides were matched with thioredoxin peroxidase-3 protein in the protein database SWISS-PROT.To find more members of the thioredoxin peroxidase (TPx)family of SIEA protein,we analyze 54 spots peptide masses ranged between 20 and 31 kDa from 2-DE gel by MALDI-TOF-MS.Using LC-MS/MS,it was shown that three Significant homologous proteins were identified whose two peptide sequences match with Schistosoma mansoni of thioredoxin peroxidase.These tell us that SIEA contains other members of thethioredoxin peroxidase family.We successfully identified thioredoxin peroxidase (TPx) of SIEA 26-28 kDa protein which might be involved in a critical component in the parasite s defense against injury caused by oxygen radicals.Based on these findings,novel anti-parasite drugs and vaccines against the parasite will be developed.