| Auteur | Rechercher : Brisson, J.; Rechercher : Jennings, Harold |
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| Format | Texte, Article |
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| Sujet | antigens; antigens, bacterial; bacterial proteins; bacterial vaccines; binding; Canada; capsular polysaccharide; carbohydrates; carbohydrate sequence; coil; conformational; epitopes; Escherichia coli; flexibility; group B Streptococcus; helices; immunology; interaction; models, molecular; molecular sequence data; molecular structure; Neisseria meningitidis; NMR; nuclear magnetic resonance, biomolecular; oligosaccharides; pneumoniae; polysaccharides; polysaccharides, bacterial; proteins; saccharides; serology; solution; Streptococcus agalactiae; Streptococcus pneumoniae; vaccine |
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| Résumé | In order to characterize the conformational epitope of the group B meningococcal polysaccharide and of the type III group B Streptococcus capsular polysaccharide NMR measurements were done on a wide variety of native and modified polysaccharides and oligosaccharides. Since these saccharides are highly mobile and exist as random coils in solution, the analysis of the NMR data and molecular modeling was done to take into account this inherent flexibility. The conformational model of extended high-order helices being selected upon binding to a protein, although still hypothetical at this stage, has proven useful in explaining the serology for the conformational epitopes for polysaccharides of group B Neisseria meningitidis, group B Streptococcus type III and Streptococcus pneumoniae type 14 |
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| Date de publication | 2001 |
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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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| Numéro du CNRC | BRISSON2001 |
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| Numéro NPARC | 9377448 |
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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 | 08d4ef7e-cbd0-4b38-9990-7e9ea5a4ec56 |
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| Enregistrement créé | 2009-07-10 |
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| Enregistrement modifié | 2022-11-18 |
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