Yersinia outer protein p (YopP) interacts with the endogenous lectin galectin-1

JOFRE B; DAVICINO R; GOMEZ-BARROSO A; SCHULE KEVIN; ELICABE RJ; RABINOVICH GA; , DI GENARO MS

Mendoza

Congreso; XXIV Reunión Anual de la Sociedad de Biología de Cuyo (SOBIO); 2016

Yersinia enterocolitica (Ye) is a Gram-negative enteropathogenic bacterium. Ye injects the effector proteins called Yersinia outerproteins (Yops) into the cytosol of host cells. YopP induces apoptosis. Galectin-1 (Gal-1) is a ?proto-type? â-galactoside-bindinglectin widely distributed in host tissues. We previously demonstrated that the Ye-induced apoptosis of macrophages depends onboth YopP and Gal-1. The aim was to demonstrate that Gal-1 binds to YopP, and that this interaction prevents YopP degradation.Secretion of Yops was induced in Ye wild-type (WT) or Ye yopP cultures. Binding of Gal-1 to YopP was evaluated byWestern blot (WB) and ELISA using rhGal-1, and anti-Gal-1 or anti-YopP antibodies. Clustal Modeller 9v12v and 3Drefinewere used for YopP modeling; and YopP-Gal-1 interaction was assayed using the server Dock / Pierr. Moreover, Yops wereincubated with rhGal-1, and the stability of YopP was studied by WB at different times. The Gal-1 binding was observed to aband of Yops of Ye WT, whereas non binding was detected with Yops of Ye yopP. Glycosylation sites were found in YopP.The YopP band was conserved in samples pre-incubated with rhGal-1. We conclude that Gal-1 binds specifically to YopP andthis interaction has a protective role against rapid YopP auto-degradation.