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The cysteine proteinases of Schistosoma mansoni cercariae

Published online by Cambridge University Press:  01 February 1997

J. P. DALTON ,
K. A. CLOUGH ,
M. K. JONES  and
P. J. BRINDLEY
J. P. DALTON
Affiliation:
Molecular Parasitology Unit, The Queensland Institute of Medical Research and The Australian Centre for International and Tropical Health and Nutrition, The Bancroft Centre, Post Office, Royal Brisbane Hospital, Q. 4029, Austra lia School of Biological Sciences, Dublin City University, Dublin 9, Republic of Ireland
K. A. CLOUGH
Affiliation:
Molecular Parasitology Unit, The Queensland Institute of Medical Research and The Australian Centre for International and Tropical Health and Nutrition, The Bancroft Centre, Post Office, Royal Brisbane Hospital, Q. 4029, Austra lia
M. K. JONES
Affiliation:
Centre for Microscopy and Microanalysis, University of Queensland, St Lucia, Q. 4072, Australia
P. J. BRINDLEY
Affiliation:
Molecular Parasitology Unit, The Queensland Institute of Medical Research and The Australian Centre for International and Tropical Health and Nutrition, The Bancroft Centre, Post Office, Royal Brisbane Hospital, Q. 4029, Austra lia
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Abstract

Based on substrate preferences, cercariae of Schistosoma mansoni were seen to express both cathepsin L and cathepsin B cysteine proteinases, although the former activity was many-fold greater. Two cathepsin L activities identified in cercarial extracts by zymography co-migrated with activities in extracts of 3 h and 24 h schisotosomula and in extracts of adult worms. Since these enzymes have been implicated in haemoglobin digestion by adult worms, they may perform a similar function in schistosomula. Immunolocalization using scanning electron micrographs showed that cathepsin L and cathepsin B proteinases were present in the cercarial post-acetabular glands. In addition, cercarial serine proteinase activities considered to facilitate skin penetration efficiently cleaved the substrates Z-Gly-Pro-Arg-NHMec and Z-Gly-Pro-Lys-NHMec. Cercariae release most of this serine proteinase activity when induced to secrete the contents of their acetabular glands. In contrast, newly transformed 3 h and 24 h schistosomula did not express this activity.

Keywords

schistosomecercariacysteine proteinaseserine proteinasecathepsin
Type
Research Article
Information
Parasitology , Volume 114 , Issue 2 , February 1997 , pp. 105 - 112
Copyright
© 1997 Cambridge University Press

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