| Autre titre | Conformational differences between linear .alpha.(2.fwdarw.8)-linked homosialooligosaccharides and the epitope of the group B meningococcal polysaccharide |
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| Téléchargement | - Voir la version finale : Conformational differences between linear α(2➝8)-linked homosialooligosaccharides and the epitope of the group B meningococcal polysaccharide (PDF, 1.6 Mio)
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| DOI | Trouver le DOI : https://doi.org/10.1021/bi00399a055 |
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| Auteur | Rechercher : Michon, Francis1; Rechercher : Brisson, J. R.1; Rechercher : Jennings, Harold J.1 |
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| Affiliation | - Conseil national de recherches du Canada
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| Format | Texte, Article |
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| Sujet | 13C; 13C NMR; 1H; acid; alpha; anomeric; antibodies; antibody; assignment; bacterial; Canada; carbohydrate conformation; carbon; chemical; chemical shift; chemical-shifts; conformation; conformational; difference; disaccharides; epitopes; group-B; heterogeneity; immunology; linear; linkages; magnetic resonance spectroscopy; methods; models,molecular; Neisseria meningitidis; NMR; NMR-spectra; oligosaccharides; one-dimensional; polysaccharides; polysaccharides,bacterial; residues; shifts; sialic; sialic-acid; signals; site; spectra; trisaccharide |
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| Résumé | The α(2➝8)-linked sialic acid oligosaccharides (NeuAc)n exhibit an unusual degree of heterogeneity in the conformation of their linkages. This was diagnosed by observation in their 13C NMR spectra of an equivalent and unique heterogeneity in the chemical shifts of their anomeric carbons and subsequently confirmed by more comprehensive 1H and 13C NMR studies. In these studies both one-dimensional and two-dimensional experiments were carried out on the trisaccharide (NeuAc)₃ and colominic acid. In addition to the unambiguous assignment of the signals in the spectra, these experiments demonstrated that both linkages of (NeuAc)₃ differed in conformation from each other and from the inner linkages of colominic acid. The NMR data indicate that these conformational differences extend to both terminal disaccharides of oligosaccharides larger than (NeuAc)₅, a result that has considerable physical and biological significance. In the context of the group B meningococcal polysaccharide, it provides an explanation for the conformational epitope of the group B meningococcal polysaccharide, which was proposed on the evidence that (NeuAc)₁₀, larger than the optimum size of an antibody site, was the smallest oligosaccharide able to bind to group B polysaccharide specific antibodies. Because the two terminal disaccharides of (NeuAc)₁₀ differ in conformation to its inner residues, the immunologically functional part of (NeuAc)₁₀ resides in its inner six residues. This number of residues is now consistent with the maximum size of an antibody site |
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| Date de publication | 1987-12-15 |
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| Maison d’édition | American Chemical Society |
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| Dans | |
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| Langue | anglais |
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| Publications évaluées par des pairs | Oui |
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| Identificateur | NRC-IBS-MICHON1987B |
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| Numéro NPARC | 9384255 |
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| Exporter la notice | Exporter en format RIS |
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| Signaler une correction | Signaler une correction (s'ouvre dans un nouvel onglet) |
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| Identificateur de l’enregistrement | 6141d6e8-9443-4020-a147-1cdaf926b5fe |
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| Enregistrement créé | 2009-07-10 |
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| Enregistrement modifié | 2020-05-27 |
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