Conformational differences between linear .alpha.(2.fwdarw.8)-linked homosialooligosaccharides and the epitope of the group B meningococcal polysaccharide

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DOIResolve DOI: http://doi.org/10.1021/bi00399a055
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TypeArticle
Journal titleBiochemistry
Volume26
Issue25
Pages83998405; # of pages: 7
Subject13C; 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
AbstractThe .alpha.(2.fwdarw.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
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Biological Sciences
Peer reviewedYes
NRC numberMICHON1987B
NPARC number9384255
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Record identifier6141d6e8-9443-4020-a147-1cdaf926b5fe
Record created2009-07-10
Record modified2016-05-09
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