Binding characteristics of purified Escherichia coli K88ab fimbriae to guinea pig erythrocyte membrane.
The characteristics of the binding of biotinylated E. coli K88ab fimbriae to guinea pig erythrocyte membranes, as a possible model of the target host cell were studied. Binding showed sigmoidal dependence, with an apparent saturation at about 0.8 ng of fimbriae. Hill coefficient values (h) were about 2-2.4, which indicated that the receptor population showed positive cooperativity with at least three binding sites. Apparent binding constants to the first and third binding sites (1K3 and 3K3) were determined. Three K88ab binding proteins, of 67, 63 and 48 kDa, were identified on solubilized erythrocyte membranes and were recovered mainly in a detergent phase, suggesting a possible integral localization of the receptors.
Caloca
M J
MJ
Departamento de Bioquimica y Biologia Molecular, Universidad de Leon, Spain.
Suarez
S
S
Soler
J
J
D018829:Adhesins, Bacterial / Q000032:analysis; D000818:Animals; D001422:Bacterial Adhesion / Q000502:physiology*; D001710:Biotin; D015153:Blotting, Western; D002352:Carrier Proteins / Q000097:blood / Q000302:isolation & purification; D004910:Erythrocyte Membrane / Q000502:physiology*; D004926:Escherichia coli / Q000502:physiology*; D010861:Fimbriae, Bacterial / Q000502:physiology*; D006168:Guinea Pigs; D007700:Kinetics
D018829:Adhesins, Bacterial; D002352:Carrier Proteins; D001710:Biotin