Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 3013-3019 |
| Number of pages | 7 |
| Journal | Biomaterials |
| Volume | 24 |
| Issue number | 18 |
| DOIs | |
| Publication status | Published - Aug 2003 |
Fingerprint
Keywords
- Bacterial adhesion
- Dynamic force spectroscopy
- Fibronectin
- Heparin
- Implant infections
- Staphylococcus epidermidis
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Biomedical Engineering
Cite this
Staphylococcus epidermidis-fibronectin binding and its inhibition by heparin. / Arciola, Carla Renata; Bustanji, Yasser; Conti, Matteo; Campoccia, Davide; Baldassarri, Lucilla; Samorì, Bruno; Montanaro, Lucio.
In: Biomaterials, Vol. 24, No. 18, 08.2003, p. 3013-3019.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Staphylococcus epidermidis-fibronectin binding and its inhibition by heparin
AU - Arciola, Carla Renata
AU - Bustanji, Yasser
AU - Conti, Matteo
AU - Campoccia, Davide
AU - Baldassarri, Lucilla
AU - Samorì, Bruno
AU - Montanaro, Lucio
PY - 2003/8
Y1 - 2003/8
N2 - 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.
AB - 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.
KW - Bacterial adhesion
KW - Dynamic force spectroscopy
KW - Fibronectin
KW - Heparin
KW - Implant infections
KW - Staphylococcus epidermidis
UR - http://www.scopus.com/inward/record.url?scp=0041670862&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0041670862&partnerID=8YFLogxK
U2 - 10.1016/S0142-9612(03)00133-9
DO - 10.1016/S0142-9612(03)00133-9
M3 - Article
VL - 24
SP - 3013
EP - 3019
JO - Biomaterials
JF - Biomaterials
SN - 0142-9612
IS - 18
ER -