| Author | Search for: Brisson, J.; Search for: Jennings, Harold |
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| Format | Text, Article |
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| Subject | 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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| Abstract | 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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| Publication date | 2001 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NRC number | BRISSON2001 |
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| NPARC number | 9377448 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | 08d4ef7e-cbd0-4b38-9990-7e9ea5a4ec56 |
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| Record created | 2009-07-10 |
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| Record modified | 2022-11-18 |
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