Specific binding of lactoferrin to Escherichicr coli isolated from human intestinal infections. APMIS 99: 1142-1 150, 1991.The degrees of human lactoferrin (HLf) and bovine lactoferrin (BLf) binding in 169 Esclierichiu c.01; strains isolated from human intestinal infections. and in an additional 68 strains isolated from healthy individuals. were examined in a ''51-labelled protein binding assay. The binding was expressed as a percentage calculated from the total labelled ligand added to bacteria. The HLf and BLf binding to E. coli was in the range 3.7 to 73.4% and 4.8 to 61.6'%,, respectively. Enterotoxigenic strains demonstrated a significantly higher HLf binding (median = 19%) than enteropathogenic, enteroinvasive, enterohaemorrhagic strains or normal intestinal E. coli isolates (medians 6 to 9). Enteropathogenic strains belonging to serotypes 0 4 4 and 01 27 demonstrated significantly higher HLf binding compared to 026. 0 5 5 , 01 1 I , 01 19 and 0126. No significant differences in the degree of HLf or BLf binding were found between aerobactin-producing and non-producing strains. The interaction was further characterized in a high Lf-binding EPEC strain, E34663 (serotype 0127). The binding was stable in the pH range 4.0 to 7.5, did not dissociate in the presence of 2M NaCl or 2M urea, and reached saturation within two h. Unlabelled HLf and BLf displaced the '"I-HLf binding to E34663 in a dosedependent manner. Apo-and iron-saturated forms of Lf demonstrated similar binding to E34663. Among various unlabelled subepithelial matrix proteins and carbohydrates tested (in 1O4-fold excess) only fibronectin and fibrinogen caused a moderate inhibition of '"I-HLf binding. According to Scatchard plot analysis. 5,400 HLf-binding sitesicell, with an affinity constant (K,) of 1.4 x lo-' M, were estimated in strain E34663. These data establish the presence of a specific Lf-binding mechanism in E. coli.