Abstract
A Schistosoma mansoni cercarial cDNA expression library, constructed in λgt11, was screened using the IgG fraction of sera taken from rabbits vaccinated with irradiated cercariae. A positive cDNA clone (1,431 base pairs) was selected and characterized. The amino acid sequence predicted from the cDNA sequence identified a polypeptide of 363 amino acids that showed significant homology to different family members of the enzyme fructose-1,6- bisphosphate aldolase (EC 1.4.2.13). The identity was 66% and 65% with human C and A isoenzymes, respectively. Active sites and substrate-binding determinant analysis suggest that the isolated enzyme in terms of function resembles type A aldolase. The recombinant protein expressed in the vector pGEX-2T was found to be active enzymatically. Antibodies raised against the purified recombinant protein recognized a 40-kDa band in extracts from cercariae, schistosomula (5 and 25 days), adult worms, and eggs. Using immunocytochemistry, aldolase localized to the tegumental region of the adult worms.
Original language | English (US) |
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Pages (from-to) | 954-960 |
Number of pages | 7 |
Journal | Journal of Parasitology |
Volume | 84 |
Issue number | 5 |
DOIs | |
State | Published - Oct 1998 |
ASJC Scopus subject areas
- Parasitology
- Ecology, Evolution, Behavior and Systematics