Abstract
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 language | English (US) |
---|---|
Pages (from-to) | 37-44 |
Number of pages | 8 |
Journal | BBA - Molecular Basis of Disease |
Volume | 1181 |
Issue number | 1 |
DOIs | |
State | Published - Mar 24 1993 |
Externally published | Yes |
Keywords
- Binding protein, Ca-
- Calpain
- Membrane turnover
- Schistosome
- Syncytical epithelium
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology