Abstract

Identification of the most relevant epitopes is the initial challenge of peptide-based vaccine design. Chimeric conserved epitopes of the Group A Streptococcus (GAS) M-protein were used in the development of an anti-GAS vaccine candidate. Previously, these epitopes have incorporated a GCN4 peptide from yeast to maintain their native helical structure. Here, we designed a new peptide epitope based on the minimal B-cell epitope from GAS M-protein. This new epitope was able to adopt the desired helical conformation without the need for the foreign GCN4 flanking sequence. The selected epitope induced significant immune responses upon administration with external adjuvant, and when incorporated into the Lipid Core Peptide (LCP) system. Moreover, the antibodies produced against this epitope were able to recognize the native p145 sequence from M-protein.

Keywords: lipid core peptide, adjuvant, Group A streptococcus, B-cell epitope, self-assembly, conformational epitope, peptide vaccine