Characterization of Ca2+-dependent neutral protease (calpain) from human blood flukes, Schistosoma mansoni

Afzal A. Siddiqui, You Zhou, Ron B. Podesta, Steve R. Karcz, Cristina E. Tognon, Gil H. Strejan, Gregory A. Dekaban, Michael W. Clarke

Research output: Contribution to journalArticlepeer-review

54 Scopus citations


Calcium-dependent, neutral cysteine-proteases (calpain) were purified from human blood flukes, Schistosoma mansoni. The electrophoretic mobilities, Western blot analyses and high specificity to peptide inhibitors confirmed the presence of both calpain I and II in the purified preparation. The schistosome calpains were localized in the surface syncytial epithelium and underlying musculature. Using peptide inhibitors, calpain was shown to function as a mediator of the surface membrane synthetic process. Since there was also no immunological cross-reactivity between vertebrate and schistosome calpains using antibodies affinity-purified from native and recombinant schistosome calpains, this protease may be usefully investigated as forming the basis of a molecular vaccine against schistosomiasis.

Original languageEnglish (US)
Pages (from-to)37-44
Number of pages8
JournalBBA - Molecular Basis of Disease
Issue number1
StatePublished - Mar 24 1993
Externally publishedYes


  • Binding protein, Ca-
  • Calpain
  • Membrane turnover
  • Schistosome
  • Syncytical epithelium

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology


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