Binding inhibition of type 1 fimbriae to human granulocytes: a flow cytometric inhibition assay using trivalent cluster mannosides.
The binding of type 1 fimbriae from Escherichia coli to vital human neutrophilic granulocytes was inhibited by synthetic trivalent cluster mannosides. Binding of type 1 fimbriae was measured in a flow cytometric assay. Based on the molarity of mannosyl residues, the clusters exceed the inhibitory potency of methyl alpha-D-mannoside by a factor of more than 1,000 and the inhibitory potency of p-nitrophenyl alpha-D-mannoside by a factor of more than 10. The inhibition studies indicate that the trivalent cluster mannosides are very potent inhibitors of the binding of type 1 fimbriae to human neutrophilic granulocytes. Based on their defined structure, cluster mannosides are well suited for characterizing the molecular interactions of mannose-sensitive fimbriae with their cell membrane receptors.
Horst
A K
AK
University Hospital Eppendorf, Department of Clinical Chemistry, Hamburg, Germany. ahorst@med.mcgill.ca
Kötter
S
S
Lindhorst
T K
TK
Ludwig
A
A
Brandt
E
E
Wagener
C
C
D001422:Bacterial Adhesion / Q000187:drug effects*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D010861:Fimbriae, Bacterial / Q000235:genetics / Q000378:metabolism*; D005434:Flow Cytometry / Q000379:methods*; D006098:Granulocytes / Q000378:metabolism*; D006801:Humans; D008362:Mannosides / Q000737:chemistry / Q000494:pharmacology*; D015394:Molecular Structure; D009504:Neutrophils / Q000378:metabolism
D008362:Mannosides