Characterization of the molecular interaction between Yersinia outer protein P (YopP) and the endogenous lectin galectin-1

ROBERTO CARLOS DAVICINO; ARTURO GOMEZ-BARROSO; KEVIN, SCHULE; RICARDO JAVIER ELIÇABE; GABRIEL ADRIÁN RABINOVICH; MARÍA SILVIA DI GENARO

Buenos Aires

Congreso; IV LASID Meeting LXIII Argentinean Immunology Society Meeting II French-Argentinean Immunology Meeting; 2015

Abstract: Background. Yersinia enterocolitica (Ye) is a Gram-negative enteropathogenic bacteria. Ye inject effector Yersinia outer proteins (Yops) inside target cells. Galectin-1 (Gal-1) is a ?proto-type? β-galactoside-binding lectin widely distributed in host tissues. Here we aimed to demonstrate that Yops are glycosylated and may interact physically with Gal-1. Methods. Ye or YopP were cultured, Yops secretion was induced and glycans were obtained. Lgals1-/- and C57BL/6 (WT) mice were used. Peritoneal macrophages were obtained and infected. Apoptosis was evaluated by flow cytometry. Potential glycosylation sites were explored using the GlycoPP program. Determination of Yops glycosylation was performed. Binding of Gal-1 and YopP was evaluated by WB and ELISA using rhGal-1 and anti-Gal-1 antibodies. Clustal, Modeller 9v12v and 3Drefine was used for modeling Yersinia outer protein P (YopP) interactions. Statistical significance was determined by ANOVA and Student t test. Results. We found increased viability of Lgals1 -/- macrophages infected with Ye or YopP as well as in WT macrophages infected with YopP (p