Carla Renata Arciola, Yasser Bustanji, Matteo Conti,
Davide Campoccia, Lucilla Baldassarri, Bruno Samorì, Lucio
Staphylococcus-Fibronectin binding and its inhibition by
Biomaterials. 2003, 24, 3013.
Staphylococcus epidermidis is able to
adhere onto biomaterials and to cause implant infections.
Recently, host matrix proteins, which in vivo cover the
implants, have been indicated as substrates for adhesion by
specific bacterial adhesins. Here, the binding of S. epidermidis
to fibronectin, a main protein of the extracellular matrix, and
the effect of heparin on this interaction were studied by
dynamic force spectroscopy (DFS). Novelties are that S.
epidermidis strains analysed by DFS were clinical isolates from
prosthesis-associated infections, genotyped and phenotyped for
their adhesion properties to fibronectin and examined as living
cells. Thus, fibronectin-binding staphylococci adhered to the
fibronectin-coated substratum and formed a continuous layer
assuring their contact with the fibronectin-coated cantilever
tip during the approach-retraction cycles of the DFS
measurements. Results show that only a single molecular binding
site of fibronectin is involved in the interaction with S.
epidermidis, that it takes place at the domain near the
C-terminus and that it is specifically inhibited by heparin.