Multivalent binding of K99 fimbriae to the N-glycolyl-GM3 ganglioside receptor.
The ganglioside N-glycolyl-GM3 binds laterally at numerous positions to K99 fimbriae, as shown by electron microscopic detection and erythrocyte-binding activity. The data demonstrate the multivalent nature of K99 fimbriae with respect to their receptor-binding sites.
Willemsen
P T
PT
Department of Molecular Microbiology, Faculty of Biology, Vrije Universiteit, Amsterdam, The Netherlands.
de Graaf
F K
FK
D000818:Animals; D001422:Bacterial Adhesion; D001665:Binding Sites; D004912:Erythrocytes / Q000378:metabolism; D004926:Escherichia coli / Q000472:pathogenicity; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D005679:G(M3) Ganglioside / Q000378:metabolism*; D006736:Horses; D066298:In Vitro Techniques; D008854:Microscopy, Electron; D011956:Receptors, Cell Surface / Q000378:metabolism
D005679:G(M3) Ganglioside; D011956:Receptors, Cell Surface