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

JOFRÉ B.; DI GENARO MS.; SCHÜLE KEVIN; RABINOVICH G

Mendoza

Congreso; XXXIV REUNIÓN CIENTIFICA ANUAL DE LA SOCIEDAD DE BIOLOGÍA DE CUYO; 2016

Yersinia enterocolitica (Ye) is a Gram-negative enteropathogenic bacterium. Ye injects the effector proteins called Yersinia outer proteins (Yops) into the cytosol of host cells. YopP induces apoptosis. Galectin-1 (Gal-1) is a ?proto-type? β-galactoside-binding lectin widely distributed in host tissues. We previously demonstrated that the Ye-induced apoptosis of macrophages depends on both 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 ΔyopP cultures. Binding of Gal-1 to YopP was evaluated by Western blot (WB) and ELISA using rhGal-1, and anti-Gal-1 or anti-YopP antibodies. Clustal Modeller 9v12v and 3Drefine were used for YopP modeling; and YopP-Gal-1 interaction was assayed using the server Dock / Pierr. Moreover, Yops were incubated with rhGal-1, and the stability of YopP was studied by WB at different times. The Gal-1 binding was observed to a band of Yops of Ye WT, whereas non binding was detected with Yops of Ye ΔyopP. 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 and this interaction has a protective role against rapid YopP auto-degradation.