We have developed a novel method for rapid determination of fine conformational epitopes in antibody-antigen interactions. This platform technology involves (i.) generation of a high quality saturation mutagenesis library of an antigen; (ii.) displaying antigenic variants on the surface of yeast; (iii.) sorting yeast libraries by cell sorting; (iv.) deep sequencing entire libraries before and after selection; and (v.)  analysis of sequencing results for automatic determination of the epitope. I will present benchmakring results on antibody-antigen interactions with known structure. Then, I will present determination of critical (and previously unknown) neutralizing epitopes for pertussis toxin and a breast and colorectal cancer target. Furthermore, I will discuss methodological improvements in throughput and cost needed to integrate epitope mapping upstream in candidate antibody selection. Implications for structural vaccine design will also be discussed.<br/>

High-throughput conformational epitope mapping by deep sequencing for antibody discovery

251st National Meeting (2016)

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