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Identification of a fibrinolytic enzyme in Schistosoma mansoni eggs and modulated blood fibrinogen metabolism in S. mansoni-infected mice

Published online by Cambridge University Press:  10 March 2003

M. J. DOENHOFF
Affiliation:
School of Biological Sciences, University of Wales Bangor, Deiniol Road, Bangor, Gwynedd LL57 2UW, UK
R. G. STANLEY
Affiliation:
School of Biological Sciences, University of Wales Bangor, Deiniol Road, Bangor, Gwynedd LL57 2UW, UK
D. PRYCE
Affiliation:
School of Biological Sciences, University of Wales Bangor, Deiniol Road, Bangor, Gwynedd LL57 2UW, UK
R. C. H. CURTIS
Affiliation:
IACR, Rothamsted, Harpenden, Herts AL5 2JQ, UK
H. PARRY
Affiliation:
Ysbyty Gwynedd, Bangor, Gwynedd LL57 2PW, UK
K. GRIFFITHS
Affiliation:
Ysbyty Gwynedd, Bangor, Gwynedd LL57 2PW, UK
C. L. JACKSON
Affiliation:
Bristol Heart Institute, University of Bristol, Bristol BS2 8HW, UK

Abstract

Aqueous extracts of Schistosoma mansoni eggs have been shown to have fibrinolytic activity inhibitable by a serine protease inhibitor. Fibrinolytic activity was not present in extracts of either adult worms or cercariae. A 27 kDa enzyme that was proteolytically active on fibrinogen in zymography and that degraded fibrinogen in a pattern similar to that of plasmin, is presumed to be responsible for the schistosome egg fibrinolytic activity. Anti-human fibrinogen antisera were shown to have antibodies that cross-reacted with mouse fibrinogen in Western immunoblots. Electroblotted sera from S. mansoni-infected and control uninfected mice displayed different antigenic profiles when probed with the cross-reactive anti-human fibrinogen antibodies, suggesting an alteration in mouse host fibrinogen metabolism as a result of the parasitic infection. We discuss the possibility that modulation of fibrinogen metabolism is a factor in a recently discovered anti-atherogenic effect exerted by schistosomes.

Type
Research Article
Copyright
2003 Cambridge University Press

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