Cloning and characterization of Schistosoma mansoni fructose-1,6- bisphosphate aldolase isoenzyme

E. El-Dabaa, H. Mei, A. El-Sayed, A. M. Karim, H. M. Eldesoky, F. A. Fahim, P. T. LoVerde, M. A. Saber

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20 Scopus citations

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 languageEnglish (US)
Pages (from-to)954-960
Number of pages7
JournalJournal of Parasitology
Volume84
Issue number5
DOIs
StatePublished - Oct 1998

ASJC Scopus subject areas

  • Parasitology
  • Ecology, Evolution, Behavior and Systematics

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