Bonds between fibronectin and fibronectin-binding proteins on Staphylococcus aureus and Lactococcus lactis.

Détails

Ressource 1Télécharger: BIB_7B4C52AFB29D.P001.pdf (1934.93 [Ko])
Etat: Serval
Version: de l'auteur
ID Serval
serval:BIB_7B4C52AFB29D
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Bonds between fibronectin and fibronectin-binding proteins on Staphylococcus aureus and Lactococcus lactis.
Périodique
Langmuir
Auteur(s)
Buck A.W., Fowler V.G., Yongsunthon R., Liu J., DiBartola A.C., Que Y.A., Moreillon P., Lower S.K.
ISSN
1520-5827 (Electronic)
ISSN-L
0743-7463
Statut éditorial
Publié
Date de publication
2010
Volume
26
Numéro
13
Pages
10764-10770
Langue
anglais
Résumé
Bacterial cell-wall-associated fibronectin binding proteins A and B (FnBPA and FnBPB) form bonds with host fibronectin. This binding reaction is often the initial step in prosthetic device infections. Atomic force microscopy was used to evaluate binding interactions between a fibronectin-coated probe and laboratory-derived Staphylococcus aureus that are (i) defective in both FnBPA and FnBPB (fnbA fnbB double mutant, DU5883), (ii) capable of expressing only FnBPA (fnbA fnbB double mutant complemented with pFNBA4), or (iii) capable of expressing only FnBPB (fnbA fnbB double mutant complemented with pFNBB4). These experiments were repeated using Lactococcus lactis constructs expressing fnbA and fnbB genes from S. aureus. A distinct force signature was observed for those bacteria that expressed FnBPA or FnBPB. Analysis of this force signature with the biomechanical wormlike chain model suggests that parallel bonds form between fibronectin and FnBPs on a bacterium. The strength and covalence of bonds were evaluated via nonlinear regression of force profiles. Binding events were more frequent (p < 0.01) for S. aureus expressing FnBPA or FnBPB than for the S. aureus double mutant. The binding force, frequency, and profile were similar between the FnBPA and FnBPB expressing strains of S. aureus. The absence of both FnBPs from the surface of S. aureus removed its ability to form a detectable bond with fibronectin. By contrast, ectopic expression of FnBPA or FnBPB on the surface of L. lactis conferred fibronectin binding characteristics similar to those of S. aureus. These measurements demonstrate that fibronectin-binding adhesins FnBPA and FnBPB are necessary and sufficient for the binding of S. aureus to prosthetic devices that are coated with host fibronectin.
Mots-clé
Bacterial Proteins/chemistry, Bacterial Proteins/metabolism, Biofilms/growth & development, Carrier Proteins/chemistry, Carrier Proteins/metabolism, Fibronectins/chemistry, Fibronectins/metabolism, Lactococcus lactis/growth & development, Lactococcus lactis/metabolism, Staphylococcus aureus/growth & development, Staphylococcus aureus/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
11/01/2011 15:42
Dernière modification de la notice
08/05/2019 20:49
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