A strategy for phage display selection of functional domain-exchanged immunoglobulin scaffolds with high affinity for glycan targets.

ABSTRACT: Monoclonal antibodies are essential reagents for deciphering gene or protein function and have been a fruitful source of therapeutic and diagnostic agents. However, the use of anticarbohydrate antibodies to target glycans for these purposes has been less successful. Glycans contain less hydrophobic functionality than do proteins or nucleic acids, thus individual glycan-antibody interactions are relatively weak. Information encoded by glycans often involves subtle variations of branched oligosaccharides that cannot be detected with conventional antibodies. Here we describe a new phage display selection strategy for identification of high-affinity and specific glycan antibodies. We designed and characterized a phage clone that functionally displays the unique architectural scaffold of 2G12,

SUBMITTER: Stewart A 

PROVIDER: S-EPMC3430726 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature