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Glycosphingolipid b...
Glycosphingolipid binding specificities of Neisseria meningitidis and Haemophilus influenzae: detection, isolation, and characterization of a binding-active glycosphingolipid from human oropharyngeal epithelium.
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Hugosson, S (författare)
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- Ångström, Jonas, 1950 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry
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Olsson, B M (författare)
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visa fler...
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- Bergström, Jörgen, 1953 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry
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Fredlund, H (författare)
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Olcén, P (författare)
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- Teneberg, Susann, 1955 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för medicinsk och fysiologisk kemi,Institute of Medical Biochemistry
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visa färre...
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(creator_code:org_t)
- 1998
- 1998
- Engelska.
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Ingår i: Journal of biochemistry. - 0021-924X. ; 124:6, s. 1138-52
- Relaterad länk:
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https://gup.ub.gu.se...
Abstract
Ämnesord
Stäng
- The glycosphingolipid binding specificities of Haemophilus influenzae and Neisseria meningitidis were investigated as to the binding of radiolabeled bacteria to glycosphingolipids on thin-layer chromatograms. Thereby, similar binding profiles, for the binding of the two bacteria to lactosylceramide, isoglobotriaosylceramide, gangliotriaosylceramide, gangliotetraosylceramide, lactotetraosylceramide, neolactotetraosylceramide, and sialylneolactohexaosylceramide, were obtained. On a closer view the binding preferences of the bacteria could be differentiated into three groups. The first specificity is recognition of lactosylceramide. The second specificity is binding to gangliotriaosylceramide and gangliotetraosylceramide, since conversion of the acetamido group of the N-acetylgalactosamine of gangliotriaosylceramide and gangliotetraosylceramide to an amine prevented the binding of the bacteria, and thus the binding to these two glycosphingolipids represents a separate specificity from lactosylceramide recognition. Preincubation of H. influenzae with neolactotetraose inhibited the binding to neolactotetraosylceramide, while the binding to lactosylceramide, gangliotetraosylceramide, or lactotetraosylceramide was unaffected. Thus, the third binding specificity is represented by neolactotetraosylceramide, and involves recognition of other neolacto series glycosphingolipids with linear N-acetyllactosamine chains, 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, epithelial cells of human nasopharyngeal tonsils and human plexus choroideus. Binding-active neolactotetraosylceramide was thereby detected in human granulocytes and the oropharyngeal epithelium.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Andra medicinska och farmaceutiska grundvetenskaper (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Other Basic Medicine (hsv//eng)
Nyckelord
- Animals
- Bacterial Adhesion
- Carbohydrate Sequence
- Chromatography
- Affinity
- Chromatography
- Thin Layer
- Epithelial Cells
- chemistry
- Gangliosides
- metabolism
- Glycosphingolipids
- chemistry
- isolation & purification
- metabolism
- Haemophilus influenzae
- chemistry
- drug effects
- metabolism
- Humans
- Lactose
- pharmacology
- Lectins
- chemistry
- metabolism
- Mass Spectrometry
- Molecular Sequence Data
- Neisseria meningitidis
- chemistry
- drug effects
- metabolism
- Oropharynx
- chemistry
- Plant Lectins
- Rabbits
- Structure-Activity Relationship
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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