Glycosphingolipid binding specificities of Neisseria meningitidis and Haemophilus influenzae: Detection, isolation, and characterization of a binding-active glycosphingolipid from human oropharyngeal epithelium

Citation
S. Hugosson et al., Glycosphingolipid binding specificities of Neisseria meningitidis and Haemophilus influenzae: Detection, isolation, and characterization of a binding-active glycosphingolipid from human oropharyngeal epithelium, J BIOCHEM, 124(6), 1998, pp. 1138-1152
Citations number
79
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOCHEMISTRY
ISSN journal
0021-924X → ACNP
Volume
124
Issue
6
Year of publication
1998
Pages
1138 - 1152
Database
ISI
SICI code
0021-924X(199812)124:6<1138:GBSONM>2.0.ZU;2-R
Abstract
The glycosphingolipid binding specificities of Haemophilus influenzae and N eisseria meningitidis were investigated as to the binding of radiolabeled b acteria to glycosphingolipids on thin-layer chromatograms. Thereby, similar binding profiles, for the binding of the two bacteria to lactosylceramide, isoglobotriaosylceramide, gangliotriaosylceramide, gangliotetraosylceramid e, lactotetraosylceramide, neolactotetraosylceramide, and sialylneolactohex aosylceramide, were obtained. On a closer view the binding preferences of t he bacteria could be differentiated into three groups. The first specificit y is recognition of lactosylceramide, The second specificity is binding to gangliotriaosylceramide and gangliotetraosylceramide, since conversion of t he acetamido group of the N-acetylgalactosamine of gangliotriaosylceramide and gangliotetraosylceramide to an amine prevented the binding of the bacte ria, and thus the binding to these two glycosphingolipids represents a sepa rate specificity from lactosylceramide recognition. Preincubation of H, inf luenzae with neolactotetraose inhibited the binding to neolactotetraosylcer amide, while the binding to lactosylceramide, gangliotetraosylceramide, or lactotetraosylceramide was unaffected. Thus, the third binding specificity is represented by neolactotetraosylceramide, and involves recognition of ot her neolacto series glycosphingolipids with linear N-acetyllactosamine chai ns, such as sialyl-neolactohexaosylceramide. The relevance of the detected binding specificities for adhesion to target cells was addressed as to the binding of the bacteria to glycosphingolipids from human granulocytes, epit helial cells of human nasopharyngeal tonsils and human plexus choroideus, B inding-active neolactotetraosylceramide was thereby detected in human granu locytes and the oropharyngeal epithelium.