Characterization of the molecular interaction between Yersinia outer protein p (YopP) and the endogenous lectin Galectin-1.

DAVICINO RC; GOMEZ-BARROSO A; SCHULE KEVIN; ELIÇABE RJ; RABINOVICH G; DI GENARO MS

Buenos Aires

Congreso; la LXIII Reunión Anual de SAI en el marco del Primer Congreso Internacional conjunto (I Meeting LASID-SAI-FAIC) junto a LASID (IV Meeting LASID) y FAIC(FAIC-II); 2015

Sociedad Argentina de Inmunología (SAI)

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 b-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 dYopP 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 dYopP as well as in WT macrophages infected with dYopP (p