Identification of carbohydrate structures that are possible receptors for Neisseria gonorrhoeae

Proc Natl Acad Sci U S A. 1988 Jul;85(13):4902-6. doi: 10.1073/pnas.85.13.4902.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Bacterial Adhesion*
  • Bacterial Proteins / metabolism
  • Carbohydrate Sequence
  • Chlorocebus aethiops
  • Dogs
  • Fimbriae, Bacterial / metabolism
  • Glycolipids / metabolism*
  • Glycosphingolipids / metabolism*
  • Humans
  • Membrane Lipids / metabolism*
  • Mice
  • Neisseria gonorrhoeae / metabolism*
  • Rats
  • Receptors, Cell Surface / metabolism*

Substances

  • Bacterial Proteins
  • Glycolipids
  • Glycosphingolipids
  • Membrane Lipids
  • Receptors, Cell Surface