Pilin independent binding of Neisseria gonorrhoeae to immobilized glycolipids.
The adherence process in pathogenesis involves the attachment of bacteria to structures present on eukaryotic cell surfaces. To investigate components necessary for this interaction, we have characterized the binding of N. gonorrhoeae to eukaryotic glycolipids immobilized on thin layer chromatograms. The gonococci specifically bind to a subset of glycolipids consisting of lactosylceramide, gangliotriosylceramide, and gangliotetraosylceramide. This binding was identified in both piliated and nonpiliated cells, and is postulated to be mediated by a nonpilin lectin-like adhesin protein.
D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism*; D002855:Chromatography, Thin Layer; D036781:Fimbriae Proteins; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D005732:Gangliosides; D006017:Glycolipids / Q000378:metabolism*; D006028:Glycosphingolipids / Q000378:metabolism; D007790:Lactosylceramides / Q000378:metabolism; D009344:Neisseria gonorrhoeae / Q000378:metabolism* / Q000648:ultrastructure
D001425:Bacterial Outer Membrane Proteins; C011258:G(A1) ganglioside; D005732:Gangliosides; D006017:Glycolipids; D006028:Glycosphingolipids; D007790:Lactosylceramides; D036781:Fimbriae Proteins; C038244:ganglio-N-triaosylceramide