Proceedings of the National Academy of Sciences · 1988 · 86 citations · 22 references
Life SciencesBiochemistryMolecular BiologyCarbohydrate BiochemistryCarbohydrate ChemistryGlycobiologyCarbohydrate RecognitionCarbohydrate StructureGlycan RecognitionGlycan StructureGlycan-protein InteractionsLipid GlycosylationCarbohydrate Structural MotifsGlycan Receptor SpecificityGlycan-binding SpecificityGlycolipid CompositionGlycolipid Glycan StructureGlycolipid StructureReceptor Glycan SpecificityReceptors
Different strains and isogenic variants of Neisseria gonorrhoeae were assayed for their ability to bind glycolipids extracted from various sources. Among a large number of reference glycolipids, binding was observed only to lactosylceramide [Gal(beta 1-4)Glc(beta 1-1)Cer], isoglobotriaosylceramide [Gal(alpha 1-3)Gal(beta 1-4)Glc(beta 1-1)Cer], gangliotriaosylceramide [GalNAc(beta 1-4)Gal(beta 1-4)Glc(beta 1-1)Cer], and gangliotetraosylceramide [Gal(beta 1-3)GalNAc(beta 1-4)Gal(beta 1-4)Glc(beta 1-1)Cer]. The latter two glycolipids bound gonococci with the highest affinity. Lactosylceramide and gangliotriaosylceramide were found in glycolipid preparations from ME180 cells, an epithelial cell line derived from a human cervical carcinoma, and thus are possible receptors for gonococci. The gonococcal surface component that bound the above glycolipids is a protein distinct from pilin and protein II.
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Intragenic recombination leads to pilus antigenic variation in Neisseria gonorrhoeae
Per Hagblom, Ellyn D. Segal, E. Billyard et al. · Nature · 1985 · 347 citations
Localization of the receptor-binding protein adhesin at the tip of the bacterial pilus
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Pharmacy, Biochemistry, Chemistry +12
Role of chromosomal rearrangement in N. gonorrhoeae pilus phase variation
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