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Flavoridin inhibits Yersinia enterocolitica uptake into fibronectin-adherent HeLa cells
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Flavoridin inhibits Yersinia enterocolitica uptake into fibronectin-adherent HeLa cells
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Journal Article
Flavoridin inhibits Yersinia enterocolitica uptake into fibronectin-adherent HeLa cells
2005
Overview
In this study, three structurally distinct disintegrins (flavoridin, echistatin, kistrin) were used as molecular probes to further characterize the molecular mechanisms underlying
Yersinia enterocolitica infection of host cells. The activity of the three disintegrins on
Y. enterocolitica uptake into fibronectin-adherent HeLa cells was evaluated at disintegrin doses which were non-cytotoxic and unable to induce cell detachment. Flavoridin resulted to be the most effective in inhibiting bacterial entry into host cells; echistatin was almost 50% less effective than flavoridin, whereas kistrin was definitely inactive. Our results suggest that α
5β
1 integrin receptor, which binds flavoridin with higher affinity than the other two disintegrins, plays a major role in
Y. enterocolitica uptake into HeLa cells. Furthermore, flavoridin binding to this integrin prevented the disruption of the functional complex FAK–Cas, which occurs in the
Y. enterocolitica uptake process.
Publisher
Elsevier B.V,Blackwell Publishing Ltd,Blackwell,Oxford University Press
Subject
Bacterial Adhesion - drug effects
/ Biological and medical sciences
/ Cas
/ Cell membranes. Ionic channels. Membrane pores
/ Cell structures and functions
/ Crotalid Venoms - pharmacology
/ FAK
/ Focal Adhesion Kinase 1 - chemistry
/ Focal Adhesion Kinase 1 - metabolism
/ Fundamental and applied biological sciences. Psychology
/ Humans
/ Integrin alpha5beta1 - chemistry
/ Integrin alpha5beta1 - metabolism
/ Molecular and cellular biology
/ Paxillin
/ Uptake
