Ability of various oral bacteria to bind human plasma fibronectin.
The present study describes the ability of various oral bacteria to bind human plasma fibronectin (PFN). Avid binding of 125I-PFN was found for Streptococcus mutans (serotypes a to h), Streptococcus sanguis, group A Streptococcus pyogenes and Staphylococcus aureus, while other gram-positive bacterial species tested demonstrated only weak or negligible PFN binding ability. Two gram-negative bacterial species, Bacteroides gingivalis and Escherichia coli, did not significantly bind PFN. 125I-PFN binding to S. mutans 6715 cells was decreased by pretreatment with unlabeled PFN, and the radiolabeled PFN bound to the cell surface was released on addition of unlabeled PFN. Strong inhibition of 125I-PFN binding to S. mutans 6715 cells was obtained by protease pretreatment, while partial inhibition was also observed following treatment with acid, alkali, lipase, and monoclonal anti-polyglycerophosphate. These results suggest that PFN binding to S. mutans cells is reversible and that PFN receptors on the cell surface appear to be heat-stable multiple proteins.
D001419:Bacteria / Q000378:metabolism*; D005353:Fibronectins / Q000097:blood / Q000378:metabolism*; D006801:Humans; D009055:Mouth / Q000382:microbiology; D011485:Protein Binding; D013211:Staphylococcus aureus / Q000378:metabolism; D013295:Streptococcus mutans / Q000378:metabolism*; D013297:Streptococcus pyogenes / Q000378:metabolism; D013298:Streptococcus sanguis / Q000378:metabolism
D005353:Fibronectins