Identification of a fibrinolytic enzyme in Schistosoma mansoni eggs and modulated blood fibrinogen metabolism in S. mansoni-infected mice.
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.
Doenhoff
M J
MJ
School of Biological Sciences, University of Wales Bangor, Deiniol Road, Bangor, Gwynedd LL57 2UW, UK. m.doenhoff@bangor.ac.uk
Stanley
R G
RG
Pryce
D
D
Curtis
R C H
RC
Parry
H
H
Griffiths
K
K
Jackson
C L
CL
D000818:Animals; D005340:Fibrinogen / Q000378:metabolism*; D005342:Fibrinolysis; D051379:Mice; D010063:Ovum / Q000201:enzymology*; D012376:Rodent Diseases / Q000378:metabolism* / Q000469:parasitology*; D012550:Schistosoma mansoni / Q000201:enzymology*; D012555:Schistosomiasis mansoni / Q000503:physiopathology
D005340:Fibrinogen