Inadequate Reference Datasets Biased toward Short Non-epitopes Confound B-cell Epitope Prediction.

ABSTRACT: X-ray crystallography has shown that an antibody paratope typically binds 15-22 amino acids (aa) of an epitope, of which 2-5 randomly distributed amino acids contribute most of the binding energy. In contrast, researchers typically choose for B-cell epitope mapping short peptide antigens in antibody binding assays. Furthermore, short 6-11-aa epitopes, and in particular non-epitopes, are over-represented in published B-cell epitope datasets that are commonly used for development of B-cell epitope prediction approaches from protein antigen sequences. We hypothesized that such suboptimal length peptides result in weak antibody binding and cause false-negative results. We tested the influence of peptide antigen length on antibody binding by analyzing data on more than 900 peptides used for B-c

SUBMITTER: Rahman KhS 

PROVIDER: S-EPMC4938180 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature