Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis.

Détails

Ressource 1Télécharger: BIB_AC3F5C623CF4.P001.pdf (1416.56 [Ko])
Etat: Public
Version: de l'auteur⸱e
ID Serval
serval:BIB_AC3F5C623CF4
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Fibrinogen and fibronectin binding cooperate for valve infection and invasion in Staphylococcus aureus experimental endocarditis.
Périodique
Journal of Experimental Medicine
Auteur⸱e⸱s
Que Y.A., Haefliger J.A., Piroth L., François P., Widmer E., Entenza J.M., Sinha B., Herrmann M., Francioli P., Vaudaux P., Moreillon P.
ISSN
0022-1007
Statut éditorial
Publié
Date de publication
2005
Peer-reviewed
Oui
Volume
201
Numéro
10
Pages
1627-1635
Langue
anglais
Notes
Publication types: Journal Article
Résumé
The expression of Staphylococcus aureus adhesins in Lactococcus lactis identified clumping factor A (ClfA) and fibronectin-binding protein A (FnBPA) as critical for valve colonization in rats with experimental endocarditis. This study further analyzed their role in disease evolution. Infected animals were followed for 3 d. ClfA-positive lactococci successfully colonized damaged valves, but were spontaneously eradicated over 48 h. In contrast, FnBPA-positive lactococci progressively increased bacterial titers in vegetations and spleens. At imaging, ClfA-positive lactococci were restricted to the vegetations, whereas FnBPA-positive lactococci also invaded the adjacent endothelium. This reflected the capacity of FnBPA to trigger cell internalization in vitro. Because FnBPA carries both fibrinogen- and fibronectin-binding domains, we tested the role of these functionalities by deleting the fibrinogen-binding domain of FnBPA and supplementing it with the fibrinogen-binding domain of ClfA in cis or in trans. Deletion of the fibrinogen-binding domain of FnBPA did not alter fibronectin binding and cell internalization in vitro. However, it totally abrogated valve infectivity in vivo. This ability was restored in cis by inserting the fibrinogen-binding domain of ClfA into truncated FnBPA, and in trans by coexpressing full-length ClfA and truncated FnBPA on two separate plasmids. Thus, fibrinogen and fibronectin binding could cooperate for S. aureus valve colonization and endothelial invasion in vivo.
Mots-clé
Adhesins, Bacterial, Animals, Bacterial Adhesion, Coagulase, Endocarditis, Bacterial, Endothelium, Vascular, Female, Fibrinogen, Fibronectins, Heart Valves, Lactococcus lactis, Protein Binding, Protein Structure, Tertiary, Rats, Rats, Wistar, Sequence Deletion, Spleen, Staphylococcal Infections, Staphylococcus aureus
Pubmed
Web of science
Open Access
Oui
Création de la notice
07/04/2008 8:46
Dernière modification de la notice
20/08/2019 16:16
Données d'usage