ULTRA-PATHOLOGICAL STUDY ON THE SYNCYTIUM OF SCHISTOSOMA MANSONI EXPOSED TO CYCLOSPORIN A IN VITRO / 中国寄生虫学与寄生虫病杂志

Objective] To study the ultra pathological changes of syncytium of Schistosoma mansoni after cyclosporin A (CsA) treatment. [Methods] MF1 mice were infected with Schistosoma mansoni cercariae. Six weeks later, the adult worms were recovered by portal vein perfusion. After the worms were exposed to CsA of 20 ?g/ml for 24 h, the drug induced damage of the worm surface was observed by SEM and TEM. [Results] Incubation of male and female schistosomes with 20 ?g/ml of CsA for 24 h resulted in disruption of the tegument and rupture of the spines. Progressive surface damage and swelling and vacuolization of the tegument led to eventual disruption of the syncytium. [Conclusion]The antischistosomal action of CsA is direct, the syncytium is the main site for CsA attack.

Epidemiological Investigation on the Intermediate Hosts of Paragonimus in Ninghai County of Zhejiang Province / 中国寄生虫学与寄生虫病杂志

Freshwater crabs and snails were collected from Ninghai County in Zhejiang Province, and examined respectively for Paragonimus metacercariae and cercariae. Among 97 freshwater crabs found, the prevalence was 11.3% (11/97) with a mean intensity of 1 metacercariae per crab. It was 10.2% (5/49) and 20.2% (4/20) in the groups weighted 5-15 g and 15-25 g respectively, with an average intensity of 1, and no metacercariae were found in weight group of 25-35 g. Two positive crabs were found from 20 crabs with a low weight (

Fusion Expression and Antigenicity Analysis of MiracidialAntigen from Eggs of Schistosoma japonicum / 中国寄生虫学与寄生虫病杂志

Objectives To express the miracidial antigen from eggs of Schistosoma japonicum (Chinese mainland strain) (SjMP10), and investigate the role of the miracidial antigen during the hepatic granuloma formation of schistosomiasis. Methods A pair of specific primers was designed and synthesized according to the nucleotide sequence of the open reading frame of the miracidial antigen gene. The open reading frame of the miracidial antigen gene was amplified, digested by restrictive enzyme(BamHI, SalI), and cloned directly into the expression plasmid pGEX-4T-3 to construct the recombinant plasmid. The recombinant plasmids were transformed into E. coli BL21(DE3), and induced by IPTG to express the fusion protein of GST-SjMP10. The expressed fusion protein was purified by electric elution method, and its antigenicity was examined by Western blotting and lymphocyte proliferation test. Results The gene of miracidial antigen was cloned into the expression plasmid pGEX-4T-3. After induced by IPTG, the recombinant expressed a fusion protein of GST-SjMP10, with a molecular weight of 39 000 approximately. The purified fusion protein showed proper antigenicity that could be recognized by the sera of rabbits heavily infected by Schistosoma japonicum and could stimulate the proliferation of splenic lymphocytes of infected BALB/c mice. Conclusion The miracidial antigen from eggs of Schistosoma japonicum was expressed successfully.

Expression and Characterization of 21.7 kDa Membrane Protein of Schistosoma japonicum / 中国寄生虫学与寄生虫病杂志

Objective To express, purify and characterize the 21.7 kDa membrane protein of Chinese strain S. japonicum (SjC21.7). Methods The gene of SjC21.7 was subcloned into the expression vector pGEX 4T 3 to form recombinant plasmid. The recombinant plasmids were transformed into E. coli BL21 and the GST SjC21.7 fusion protein was expressed by IPTG induction. The recombinant SjC21.7 molecule was prepared by affinity chromatography and digested by thrombin. The Kunming strain mice were immunized with the recombinant SjC21.7 molecule to produce anti SjC21.7 antibody. The purified SjC21.7 was recognized by the immunized mouse serum and the sera of rabbits infected by S. japonicum . Results The SjC21.7 gene was subcloned into expression vector pGEX 4T 3, then transformed into E.coli BL21 to express the GST SjC21.7 fusion protein. The recombinant SjC21.7 molecule obtained from the fusion protein could stimulate the mice to produce a high titer of specific antibody and could be recognized by sera of both the immunized and infected rabbits. The sera of immunized mice could also recognize the 21.7 kDa protein molecule of the adult worm antigen (AWA). Conclusion The recombinant and purified SjC21.7 was prepared and showed similar immunological characteristics to the natural SjC21.7 molecule, providing a basis for further investigation of the immunological protection of the recombinant SjC21.7.