Lp95: a novel leptospiral protein that binds extracellular matrix components and promotes up-regulation of E-selectin on human umbilical vein endothelial cells

ATZINGEN MV; GÓMEZ RM; SCHATTNER M; PRETRE G; GONÇALES AP; DE MORAIS ZM; VASCONCELLOS SA; NASCIMENTO ALTO

THE JOURNAL OF INFECTION.

Año: 2009

0163-4453

We report the study of a predicted outer membrane leptospiral protein encoded by the gene LIC12690 in mediating the adhesion process. This protein has a Domain of Unknown Function 1554 (DUF) also present the family of proteins carrying the Len motif. 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). The recombinant leptospiral protein of 95 kDa, 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