Binding of fibronectin and albumin to Enterococcus (Streptococcus) faecalis.

Binding of human fibronectin (FN) and albumin to Enterococcus (Streptococcus) faecalis was investigated. Scatchard analysis showed that the cells could bind a maximum of 1300 molecules of FN with an association constant of 4.8 x 10(6) M-1. Binding did not appear to involve lipoteichoic acid. Heating the cells or pretreatment with protease or periodate reduced the binding, suggesting the involvement of protein and/or carbohydrate-containing components as the surface receptor. The cells could bind a maximum of 50,000 molecules of albumin but with a much lower affinity than FN (association constant 10.8 x 10(3) M-1). Surface hydrophobicity of E. faecalis was markedly decreased by albumin but not by FN.