Adherence to host extracellular matrix and serum components by Enterococcus faecium isolates of diverse origin.
FEMS Microbiology Letters
Enterococcus faecium has emerged as an important cause of nosocomial infections over the last two decades. We recently demonstrated collagen type I (CI) as a common adherence target for some E. faecium isolates and a significant correlation was found to exist between acm-mediated CI adherence and clinical origin. Here, we evaluated 60 diverse E. faecium isolates for their adherence to up to 15 immobilized host extracellular matrix and serum components. Adherence phenotypes were most commonly observed to fibronectin (Fn) (20% of the 60 isolates), fibrinogen (17%) and laminin (Ln) (13%), while only one or two of the isolates adhered to collagen type V (CV), transferrin or lactoferrin and none to the other host components tested. Adherence to Fn and Ln was almost exclusively restricted to clinical isolates, especially the endocarditis-enriched nosocomial genogroup clonal complex 17 (CC17). Thus, the ability to adhere to Fn and Ln, in addition to CI, may have contributed to the emergence and adaptation of E. faecium, in particular CC17, as a nosocomial pathogen.
Animals, Bacterial Adhesion, Blood Proteins, Collagen Type I, Collagen Type V, Cross Infection, Enterococcus faecium, Extracellular Matrix Proteins, Fibrinogen, Fibronectins, Gram-Positive Bacterial Infections, Host-Pathogen Interactions, Humans, Lactoferrin, Laminin, Transferrin