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1 Unité de Pathogénie Microbienne Moléculaire, INSERM U389, Institut Pasteur, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France
2 Unité de Pharmacologie Cellulaire, Institut Pasteur, 25 rue du Docteur Roux, 75724 Paris Cedex 15, France
3 Centro CNR Biomembrane and Dipartimento di Scienze Biomediche, Universita di Padova, Via Trieste 75, 35121 Padova, Italy
Author for correspondence: Claude Parsot. Tel: + 33 1 45 68 83 00. Fax: + 33 1 45 68 89 53.
ABSTRACT
Shigellosis is characterized by a strong inflammatory response which is induced by bacteria invading the colonic mucosa. Characterization of a sepA mutant indicated that SepA, the major protein secreted by Shigella flexneri growing in laboratory media, might be involved in invasion and destruction of the host intestinal epithelium. The sequence of the first 500 residues of mature SepA (110 kDa) is homologous to that of the N-terminal region of lgA1 proteases. To investigate the potential proteolytic activity of SepA, the activity of the purified protein on a wide range of synthetic peptides was tested. SepA hydrolysed several of these substrates and the activity was inhibited by PMSF. Several peptides which were hydrolysed by SepA have been described as specific substrates for cathepsin G, a serine protease produced by polymorphonuclear leukocytes that was proposed to play a role in inflammation. However, unlike cathepsin G, SepA degraded neither fibronectin nor angiotensin I and had no effect on aggregation of human platelets. In addition, analysis of SepA hydrolysis by proteinase K suggested that the protein is composed of two domains of about 450 residues separated by a hinge region of 100 residues. The 47 kDa N-terminal domain was stable and endowed with proteolytic activity.
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