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Asparaginyl endopeptidase activity in adult Schistosoma mansoni

Published online by Cambridge University Press:  06 April 2009

J. P. Dalton ,
L. Hola-Jamriska  and
P. J. Brindley
J. P. Dalton
Affiliation:
Molecular Parasitology Unit, Queensland Institute of Medical Research, The Bancroft Centre, Post Office, Royal Brisbane Hospital, Queensland 4029, Australia School of Biological Sciences, Dublin City University, Dublin 9, Republic of, Ireland
L. Hola-Jamriska
Affiliation:
Molecular Parasitology Unit, Queensland Institute of Medical Research, The Bancroft Centre, Post Office, Royal Brisbane Hospital, Queensland 4029, Australia
P. J. Brindley
Affiliation:
Molecular Parasitology Unit, Queensland Institute of Medical Research, The Bancroft Centre, Post Office, Royal Brisbane Hospital, Queensland 4029, Australia
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Summary

Sequence comparisons have recently shown that the Schistosoma mansoni protein Sm32 is similar to asparaginyl endo-proteinases, a novel family of cysteine proteinases, of which the legumains rom legumes are the best characterized. By synthesizing and employing fluorogenic peptide substrates for the specific detection of asparaginyl endopeptidases, we have identified this type of activity in extracts of adult S. mansoni. The S. mansoni activity is similar to that of the legumains in its substrate specificity and sensitivity to thiol inhibitors, but differs in its pH and temperature optima for activity. In contrast, unlike the legumains, the schistosome asparaginyl endopeptidase activity is not activated by the reducing agent dithiothreitol. As suggested for legumains, Sm32 may function in the post-translational modification processes that regulate the activity of other molecules.

Keywords

Schistosoma mansoniproteaseasparaginylendopeptidase
Type
Research Article
Information
Parasitology , Volume 111 , Issue 5 , December 1995 , pp. 575 - 580
Copyright
Copyright © Cambridge University Press 1995

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