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

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.

journal_name

Parasitology

journal_title

Parasitology

authors

Cocude C,Pierrot C,Cêtre C,Fontaine J,Godin C,Capron A,Khalife J

doi

10.1017/s0031182098003874

subject

Has Abstract

pub_date

1999-04-01 00:00:00

pages

389-96

eissn

0031-1820

issn

1469-8161

journal_volume

118 ( Pt 4)

pub_type

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