The present study was intend to clone and express the
cDNA encoding
Cyclophilin B (CyPB) of Schistosoma japonicum, its preliminary
biological function and further immunoprotective effect against schistosome
infection in mice. RT-PCR technique was applied to amplify a full-length
cDNA encoding
protein Cyclophilin B (Sj CyPB) from schistosomula
cDNA. The expression profiles of Sj CyPB were determined by Real-time PCR using the template cDNAs isolated from 7, 13, 18, 23, 32 and 42 days parasites. The
cDNA containing the Open Reading Frame of CyPB was then subcloned into a pGEX-6P-1 vector and transformed into competent Escherichia coli BL21 for expressing. The
recombinant protein was renaturated, purified and its antigenicity were detected by Western blotting, and the immunoprotective effect induced by recombinant Sj CyPB was evaluated in Balb/C mice. The
cDNA containing the ORF of Sj CyPB was cloned with the length of 672 base pairs, encoding 223
amino acids. Real-time PCR analysis revealed that the gene had the highest expression in 18-day schistosomula, suggesting that Sj CyPB was schistosomula differentially expressed gene. The
recombinant protein showed a good antigenicity detected by Western blotting. Animal experiment indicated that the vaccination of recombinant
CyPB protein in mice led to 31.5% worm and 41.01% liver egg burden reduction, respectively, compared with those of the control. A full-length
cDNA differentially expressed in schistosomula was obtained. The recombinant Sj
CyPB protein could induce partial protection against schistosome
infection.