Characterization of Ca(2+)-dependent neutral protease (calpain) from human blood flukes, Schistosoma mansoni.
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.
Siddiqui
A A
AA
Department of Zoology, University of Western Ontario, London, Canada.
Zhou
Y
Y
Podesta
R B
RB
Karcz
S R
SR
Tognon
C E
CE
Strejan
G H
GH
Dekaban
G A
GA
Clarke
M W
MW
D000818:Animals; D015153:Blotting, Western; D002154:Calpain / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D002462:Cell Membrane / Q000378:metabolism; D002794:Choline / Q000378:metabolism; D006224:Cricetinae; D003429:Cross Reactions; D010450:Endopeptidases / Q000378:metabolism; D007700:Kinetics; D008647:Mesocricetus; D008715:Methionine / Q000378:metabolism; D008855:Microscopy, Electron, Scanning; D012550:Schistosoma mansoni / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure
D008715:Methionine; D010450:Endopeptidases; D002154:Calpain; D002794:Choline