Format

Send to

Choose Destination
Biochem Biophys Res Commun. 1995 Nov 22;216(3):785-92.

Fibronectin binding domain of P. gingivalis fimbriae.

Author information

1
Department of Oral Biology, School of Dental Medicine, State University of New York at Buffalo 14214, USA.

Abstract

P. gingivalis fimbriae play an important role in attachment of bacteria to various salivary components as well as to host cells and matrix proteins including fibronectin. In the present study, we investigated the binding domain of P. gingivalis fimbriae to fibronectin using synthetic peptides. A series of 20 mer fimbrillin peptides were used. Binding of fibronectin to purified fimbriae and synthetic peptides was assayed using polyclonal fibronectin antibodies as well as iodinated fibronectin. Purified fimbriae and peptide 126-146 (RMAFTEIKVQMSAAYDNIYTF) showed high levels of binding to fibronectin, while peptide 318-337(HLNVQCTVAEWVLVGQNATW) showed low but statistically significant binding. Our results suggest V-Q-X-X-X-A or V-X-X-X A common domain/domains present in both peptides might be involved in protein-protein interaction between P. gingivalis fimbriae and fibronectin.

PMID:
7488194
DOI:
10.1006/bbrc.1995.2690
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center