In vitro effect of temperature on the conformational structure and collagen binding of SdrF, a Staphylococcus epidermidis adhesin

Massimiliano Papi, Marco De Spirito, Alessandro Maiorana, Antonella Di Poto, Sheetal Trivedi, Paola Gavazzo, Massimo Vassalli, Franklin D. Lowy, Lucio Montanaro, Marcello Imbriani, Carla Renata Arciola, Livia Visai

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2 Citazioni (Scopus)

Abstract

Staphylococcus epidermidis is the leading etiologic agent of device-related infections. S. epidermidis is able to bind, by means of the adhesins of its cell wall, the host matrix proteins filming the artificial surfaces. Thence, bacteria cling to biomaterials and infection develops. The effect of temperature on integrity, structure, and biological activity of the collagen-binding adhesin (SdrF) of S. epidermidis has been here investigated. By cloning in E. coli XL1-Blue, a recombinant of the SdrF binding domain B (rSdrFB), carrying an Nterminal polyhistidine, was obtained. Purification was by HiTrapTM Chelating HP columns. Assessment of purity, molecular weight, and integrity was by SDS-PAGE. The rSdrFBcollagen binding was investigated by ELISA. A full threedimensional reconstruction of rSdrFB was achieved by small-angle X-ray scattering (SAXS). At 25 °C, rSdrFB bound to type I collagen in a dose-dependent, saturable manner, with a Kd of 2.48×10−7 M. When temperature increased from 25 to 37 °C, a strong conformational change occurred, together with the abolition of the rSdrFB-collagen binding. The rSdrFB integrity was not affected by temperature variation. SdrFB-collagen binding is switched on/off depending on the temperature. Implications with the infection pathogenesis are enlightened.
Lingua originaleEnglish
pagine (da-a)N/A-N/A
Numero di pagine11
RivistaApplied Microbiology and Biotechnology
DOI
Stato di pubblicazionePubblicato - 2015

Keywords

  • SdrF adhesin
  • Staphylococcus epidermidis

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