Molecular analysis of carbohydrate-antibody interactions: case study using a Bacillus anthracis tetrasaccharide.
The process for selecting potent and effective carbohydrate antigens is not well-established. A combination of synthetic glycan microarray screening, surface plasmon resonance analysis, and saturation transfer difference NMR spectroscopy was used to dissect the antibody-binding surface of a carbohydrate antigen, revealing crucial binding elements with atomic-level detail. This analysis takes the first step toward uncovering the rules for structure-based design of carbohydrate antigens.
Oberli
Matthias A
MA
Department of Biomolecular Systems, Max-Planck Institute for Colloids and Interfaces, 14476 Potsdam, Germany.
Tamborrini
Marco
M
Tsai
Yu-Hsuan
YH
Werz
Daniel B
DB
Horlacher
Tim
T
Adibekian
Alexander
A
Gauss
Dominik
D
Möller
Heiko M
HM
Pluschke
Gerd
G
Seeberger
Peter H
PH
D000906:Antibodies / Q000737:chemistry / Q000276:immunology*; D001408:Bacillus anthracis / Q000737:chemistry / Q000276:immunology*; D001666:Binding Sites, Antibody; D018604:Epitope Mapping / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D046228:Microarray Analysis / Q000379:methods; D008958:Models, Molecular; D009844:Oligosaccharides / Q000737:chemistry / Q000276:immunology*; D020349:Surface Plasmon Resonance / Q000379:methods
D000906:Antibodies; D009844:Oligosaccharides