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.
Shorrock
P J
PJ
Department of Pharmaceutical Sciences, Aston University, Birmingham, U.K.
Lambert
P A
PA
D000418:Albumins / Q000493:pharmacokinetics*; D001665:Binding Sites; D002462:Cell Membrane; D013293:Enterococcus faecalis / Q000378:metabolism*; D005353:Fibronectins / Q000493:pharmacokinetics*
D000418:Albumins; D005353:Fibronectins