Characterization of the cathepsin-like cysteine proteinases of Schistosoma mansoni

Dalton, John P., Clough, Karen A., Jones, Malcolm K. and Brindley, Paul J. (1996) Characterization of the cathepsin-like cysteine proteinases of Schistosoma mansoni. Infection and Immunity, 64 4: 1328-1334.

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Author Dalton, John P.
Clough, Karen A.
Jones, Malcolm K.
Brindley, Paul J.
Title Characterization of the cathepsin-like cysteine proteinases of Schistosoma mansoni
Journal name Infection and Immunity
ISSN 1098-5522
Publication date 1996-04
Sub-type Article (original research)
Open Access Status File (Publisher version)
Volume 64
Issue 4
Start page 1328
End page 1334
Total pages 7
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Language eng
Abstract Adult Schistosoma mansoni parasites synthesize and secrete both cathepsin L and cathepsin B cysteine proteinases. These cysteine proteinase activities, believed to be involved in hemoglobin digestion by adult schistosomes, were characterized by using specific fluorogenic peptide substrates and zymography. Both cathepsin L- and B-like activities with pH optima of 5.2 and 6.2, respectively, predominated in soluble extracts of worms, and both these activities were secreted by adult worms into the culture medium. The specific activity of cathepsin L was about double that of cathepsin B when each was assayed at its pH optimum, and moreover, the specific activities of cathepsins L and B in extracts of female schistosomes were 50 to 100% higher than in extracts of male schistosomes. Analysis of the primary structure of two cloned S. mansoni cathepsins L, here termed cathepsin L1 and cathepsin L2, revealed that they are only 44% similar and that cathepsin L2 showed more identity (52%) with human cathepsin L than with schistosome cathepsin L1. Moreover, differences in their active site, propeptide region, and potential for glycosylation suggest separate functions for schistosome cathepsin L1 and cathepsin L2.
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Document type: Journal Article
Sub-type: Article (original research)
Collection: Centre for Microscopy and Microanalysis Publications
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Citation counts: TR Web of Science Citation Count  Cited 58 times in Thomson Reuters Web of Science Article | Citations
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