Cryptic B-cell epitope identification through informational analysis of protein sequences.

A comparison of the location of B-cell epitopes and information structure (IS) of protein sequences was attempted. Analysis of 62 known B-cell epitopes located in five different proteins showed that they concentrated in IS sites with increased degree of information coordination. Based on the analysis of IS six peptides from two proteins were selected and produced in a recombinant form as yeast virus-like particles (VLPs). Immunization of mice with recombinant VLP-peptides has induced the production of IgG capable of recognizing full-length antigens. This result suggests that the analysis of IS of proteins can be useful in the selection of peptides possessing cryptic B-cell epitope activity.