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Identification of a developmentally regulated Schistosoma mansoni serine protease homologous to mouse plasma kallikrein and human factor I

Published online by Cambridge University Press:  01 April 1999

C. COCUDE
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, INSERM U167, Institut Pasteur, 1 rue du Professeur Calmette, BP 245, 59019 Lille, France
C. PIERROT
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, INSERM U167, Institut Pasteur, 1 rue du Professeur Calmette, BP 245, 59019 Lille, France
C. CÊTRE
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, INSERM U167, Institut Pasteur, 1 rue du Professeur Calmette, BP 245, 59019 Lille, France
J. FONTAINE
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, INSERM U167, Institut Pasteur, 1 rue du Professeur Calmette, BP 245, 59019 Lille, France
C. GODIN
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, INSERM U167, Institut Pasteur, 1 rue du Professeur Calmette, BP 245, 59019 Lille, France
A. CAPRON
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, INSERM U167, Institut Pasteur, 1 rue du Professeur Calmette, BP 245, 59019 Lille, France
J. KHALIFE
Affiliation:
Centre d'Immunologie et de Biologie Parasitaire, INSERM U167, Institut Pasteur, 1 rue du Professeur Calmette, BP 245, 59019 Lille, France

Abstract

The isolation of 2 genomic clones has allowed us to further characterize a Schistosoma mansoni serine protease designated SmSP1. The deduced amino acid sequence (248aa) considered as a ‘light chain’ encoding the active site, presents significant homologies with mouse plasma kallikrein and human factor I light chain. The secondary structure of SmSP1 ‘light chain’ is correctly predicted and may be sufficient by itself to constitute an active enzyme. The biological function of SmSP1 is unknown, however, the homology with 2 serine proteases suggests that SmSP1 may play a role in the evasion of the host immune response. This is supported by the presence of the native protein corresponding to SmSP1 particularly in schistosomula released products (SRP) and in male dorsal spines. The expression of this enzyme is differentially regulated throughout the parasite life-cycle. However, infected animals with S. mansoni did not produce specific antibodies to recombinant SmSP1. The lack of such response could be advantageous to the parasite by protecting itself from host effector mechanisms.

Type
Research Article
Copyright
© 1999 Cambridge University Press

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