Fig. 6. Effects of sugars and pH on the binding of FimH to mouse urothelial plaques. The wells of 96-well plates were coated with purified mouse urothelial plaques, quenched with bovine serum albumin and incubated with biotinylated FimH-FimC, in the presence or absence of galactose or mannose and at various pHs. (A) Typical saturation curve for the binding of FimH-FimC to mouse urothelial plaques. The solid line represents a best fit from nonlinear regression. This is a typical curve representative of results from 
10 experiments, yielding Kd values in the range of 110-160 nM (correlation coefficient r=0.9948). (B) The binding is completely abolished by 
-D-mannose (
, but not by galactose (
). (C) Binding of the FimH to mouse urothelial plaques at pH 4.2-7.0. pH 4.2 (), 5.0 (
), 6.0 () and 7.0 (
). (D) Similar binding at pH 7-9. pH 7.0 (), 7.5 (), 8.0 () and 9.0 ().
