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Lp95, a novel leptospiral protein that binds extracellular matrix components and activates e-selectin on endothelial cells.

Atzingen, Marina V; Gómez, Ricardo M; Schattner, Mirta; Pretre, Gabriela; Gonçales, Amane P; de Morais, Zenaide M; Vasconcellos, Silvio A; Nascimento, Ana L T O.
J Infect ; 59(4): 264-76, 2009 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-19665803

OBJECTIVES:

The study of a predicted outer membrane leptospiral protein encoded by the gene LIC12690 in mediating the adhesion process.

METHODS:

The gene was cloned and expressed in Escherichia coli BL21 (SI) strain by using the expression vector pAE. The recombinant protein tagged with N-terminal hexahistidine was purified by metal-charged chromatography and used to assess its ability to activate human umbilical vein endothelial cells (HUVECs).

RESULTS:

The recombinant leptospiral protein of 95kDa, named Lp95, activated E-selectin in a dose-dependent fashion but not the intercellular adhesion molecule 1 (ICAM-1). In addition, we show that pathogenic and non-pathogenic Leptospira are both capable to stimulate endothelium E-selectin and ICAM-1, but the pathogenic L. interrogans serovar Copenhageni strain promotes a statistically significant higher activation than the non-pathogenic L. biflexa serovar Patoc (P<0.01). The Lp95 was identified in vivo in the renal tubules of animal during experimental infection with L. interrogans. The whole Lp95 as well as its fragments, the C-terminal containing the domain of unknown function (DUF), the N-terminal and the central overlap regions bind laminin and fibronectin ECM molecules, being the binding stronger with the DUF containing fragment.

CONCLUSION:

This is the first leptospiral protein capable to mediate the adhesion to ECM components and the activation of HUVECS, thus suggesting its participation in the pathogenesis of Leptospira.