Title: Isolation of native, biochemically purified triosephosphate isomerase from a Chinese strain of Schistosoma japonicum and its protective efficacy in mice
Abstract: The glycolytic enzyme triosephosphate isomerase (TPI) was isolated biochemically from homogenates of a Chinese strain of Schistosoma japonicum (Sjc). Purified SjcTPI migrated on SDS polyacrylamide gels with an apparent molecular size of 28 kDa and had an enzyme activity of 177 IU/mg protein. Immunization of mice with the purified, native SjcTPI resulted in a modest reduction in adult worm burdens relative to adjuvant control mice after the cercarial challenge. No significant reduction in worm burden was noted compared with a soluble extract of adult worm antigen (SWAP). However, mice immunized with SjcTPI exhibited a marked and significant reduction in the number of eggs deposited in the liver relative to both SWAP immunized mice (47–64% reduction) and adjuvant control mice (58–60% reduction). The SjcTPI offers promise as a potential schistosomiasis japonica vaccine antigen, possibly as a `cocktail' with other Sjc recombinant antigens under investigation.
Publication Year: 1998
Publication Date: 1998-09-01
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 8
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