Saturation-transfer difference NMR studies for the epitope mapping of a carbohydrate-mimetic peptide recognized by an anti-carbohydrate antibody.
Saturation-transfer difference NMR spectroscopy (STD-NMR) experiments have been performed to analyze the topography or epitope of the octapeptide MDWNMHAA recognized by the anti-carbohydrate antibody SYA/J6 in solution; the antibody is directed against the Shigella flexneri Y O-antigen polysaccharide. The results permit a valuable comparison of solution versus crystal-structure data, and provide insight for the design of the next-generation binding ligands.
Johnson
Margaret A
MA
Departments of Chemistry and of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, BC, Canada V5A 1S6.
Pinto
B Mario
BM
D000907:Antibodies, Bacterial / Q000737:chemistry*; D001665:Binding Sites; D002241:Carbohydrates / Q000737:chemistry / Q000276:immunology*; D018604:Epitope Mapping / Q000379:methods*; D008070:Lipopolysaccharides / Q000737:chemistry / Q000276:immunology; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D018716:Molecular Mimicry; D019081:O Antigens / Q000737:chemistry / Q000276:immunology*; D009842:Oligopeptides / Q000737:chemistry / Q000276:immunology*; D012763:Shigella flexneri / Q000276:immunology
D000907:Antibodies, Bacterial; D002241:Carbohydrates; D008070:Lipopolysaccharides; D019081:O Antigens; D009842:Oligopeptides