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 alpha(5)beta(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.

Flavoridin inhibits Yersinia enterocolitica uptake into fibronectin-adherent HeLa cells / A., Scibelli; Matteoli, G.; Roperto, Sante; Alimenti, E.; Dipineto, Ludovico; Pavone, LUIGI MICHELE; DELLA MORTE, Rossella; Menna, LUCIA FRANCESCA; Fioretti, Alessandro; Staiano, Norma. - In: FEMS MICROBIOLOGY LETTERS. - ISSN 0378-1097. - STAMPA. - 247:1(2005), pp. 51-57. [10.1016/j.femsle.2005.04.024]

Flavoridin inhibits Yersinia enterocolitica uptake into fibronectin-adherent HeLa cells

ROPERTO, SANTE;DIPINETO, LUDOVICO;PAVONE, LUIGI MICHELE;DELLA MORTE, ROSSELLA;MENNA, LUCIA FRANCESCA;FIORETTI, ALESSANDRO;STAIANO, NORMA
2005

Abstract

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 alpha(5)beta(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.
2005
Flavoridin inhibits Yersinia enterocolitica uptake into fibronectin-adherent HeLa cells / A., Scibelli; Matteoli, G.; Roperto, Sante; Alimenti, E.; Dipineto, Ludovico; Pavone, LUIGI MICHELE; DELLA MORTE, Rossella; Menna, LUCIA FRANCESCA; Fioretti, Alessandro; Staiano, Norma. - In: FEMS MICROBIOLOGY LETTERS. - ISSN 0378-1097. - STAMPA. - 247:1(2005), pp. 51-57. [10.1016/j.femsle.2005.04.024]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/201684
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