An Insertion Mutation That Distorts Antibody Binding Site Architecture Enhances Function of a Human Antibody

Krause, J.C., et al., 2(1), e00345-10, MBio, 2011

The authors demonstrate that a naturally occurring three-amino-acid insertion within the influenza virus-specific human monoclonal antibody 2D1 heavy-chain variable region reconfigures the antibody-combining site and contributes to its high potency against the 1918 and 2009 pandemic H1N1 influenza viruses. Comparison of Octet QK system binding data for wild-type 2D1 and del 2D1 mutant binding to hemagglutinin showed that the mutant not harboring the insertion had a 35-fold faster dissociation rate. HIS-tagged hemagglutinin protein was immobilized with anti-Penta-HIS biosensors for these mesurements.

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