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PubMed2004

The protective immunity of a DNA vaccine encoding Schistosoma japonicum Chinese strain triose-phosphate isomerase in infected BALB/C mice.

The development of a DNA vaccine for schistosomiasis japonica and testing the protective efficacy after challenge in BALB/c mice were performed. Thirty-nine female BALB/c mice were divided into three groups. Each mouse of the control group was injected intramuscularly with 100 microg of pcDNA3.1 DNA. In the TPI group, each mouse was injected with 100 microg of pcDNA3.1-SjCTPI DNA. The TPI+IL-12 group was injected with 100 microg of pcDNA3.1-SjCTPI DNA and 100 microg of the mixture of pcDNA3.1-P35 and pcDNA3.1-P40 DNA. Each mouse was immunized three times at two-week intervals and challenged with 45 cercariae of Schistosoma japonicum Chinese strain four weeks post-immunization. Then the mice were sacrificed and perfused at 45 days after challenge; the recovered worms and hepatic eggs were counted. Cytotoxic T lymphocyte (CTL) activity mediated by SjCTPI was detected with the 51Cr release assay. ELISA was performed for the detection of anti-rTPI antibodies. Anti-rTPI antibody detection with ELISA after immunization showed ten serum samples from the control group were negative, five of ten serum samples from the TPI group were weakly positive, six of ten from the TPI+IL-12 group were also weakly positive. The CTL activity of the control group was 9.1%, while CTL activities of the TPI group and the TPI+IL-12 group were 27.6% and 54.4%, respectively. The worm and egg reduction rates of TPI group and the TPI+IL-12 group were 30.2%, 52.9%, 32.7%, and 47.0%, respectively in comparison with the control group. This study further proved the possibility of the SjCTPI DNA vaccine as a potential DNA vaccine for schistosomiasis.

Animals↗
PubMed1992

A protective monoclonal antibody specifically recognizes and alters the catalytic activity of schistosome triose-phosphate isomerase.

mAb M.1 was previously shown to recognize a 28-kDa Ag in all stages of the human helminth parasite, Schistosoma mansoni, and to bind to the surface membranes of newly transformed schistosomula in a transient manner. Here we demonstrate that M.1 passively transfers partial resistance (41-49%) to cercarial challenge in naive mice. Thus, the 28-kDa Ag recognized by M.1 is a putative vaccine candidate. After immunoaffinity purification, tryptic digests of the 28-kDa Ag were prepared and individual peptides were sequenced. Amino terminus sequences of tryptic peptides of the 28-kDa Ag had high (79-87%) sequence homology with the mammalian glycolytic/gluconeogenic enzyme triosephosphate isomerase (TPI). Purified, native 28-kDa Ag from adult parasites was shown to function enzymatically in an analogous manner to yeast and mammalian TPI in the reverse reaction. Addition of M.1 antibody to the enzyme reaction altered the catalytic activity of schistosome TPI. To determine the immunologic cross-reactivity of this vaccine candidate with mammalian TPI, Western blot analysis was performed and demonstrated that M.1 was immunologically specific for the schistosome enzyme.

Amino Acid Sequence↗