P-Sulfonato-calix[n]arenes inhibit staphylococcal bicomponent leukotoxins by supramolecular interactions. - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Biochemical Journal Année : 2013

P-Sulfonato-calix[n]arenes inhibit staphylococcal bicomponent leukotoxins by supramolecular interactions.

Gabriella Viero
  • Fonction : Auteur
Christoph Bachmeyer
  • Fonction : Auteur
Valeria Antonini
  • Fonction : Auteur
Ines Mancini
  • Fonction : Auteur
Gregor Anderluh
  • Fonction : Auteur
  • PersonId : 955057
Mauro Dalla Serra
  • Fonction : Auteur
Cristina Potrich
  • Fonction : Auteur

Résumé

PVL (Panton-Valentine leukocidin) and other Staphylococcus aureus β-stranded pore-forming toxins are important virulence factors involved in various pathologies that are often necrotizing. The present study characterized leukotoxin inhibition by selected SCns (p-sulfonato-calix[n]arenes): SC4, SC6 and SC8. These chemicals have no toxic effects on human erythrocytes or neutrophils, and some are able to inhibit both the activity of and the cell lysis by leukotoxins in a dose-dependent manner. Depending on the type of leukotoxins and SCns, flow cytometry revealed IC50 values of 6-22 μM for Ca2+ activation and of 2-50 μM for cell lysis. SCns were observed to affect membrane binding of class S proteins responsible for cell specificity. Electrospray MS and surface plasmon resonance established supramolecular interactions (1:1 stoichiometry) between SCns and class S proteins in solution, but not class F proteins. The membrane-binding affinity of S proteins was Kd=0.07-6.2 nM. The binding ability was completely abolished by SCns at different concentrations according to the number of benzenes (30-300 μM; SC8

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Dates et versions

hal-01272751 , version 1 (11-02-2016)

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Citer

Gabriella Viero, Christoph Bachmeyer, Valeria Antonini, Ines Mancini, Sarah Cianferani-Sanglier, et al.. P-Sulfonato-calix[n]arenes inhibit staphylococcal bicomponent leukotoxins by supramolecular interactions.. Biochemical Journal, 2013, 450 (3), pp.559-71. ⟨10.1042/BJ20121628⟩. ⟨hal-01272751⟩
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