The University of Queensland, School of Chemistry and Molecular Biosciences, St. Lucia, Qld 4072, Australia.
Curr Drug Deliv. 2013 Feb;10(1):39-45. doi: 10.2174/1567201811310010007.
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.
鉴定最相关的表位是基于肽的疫苗设计的初始挑战。在开发抗 A 群链球菌(GAS)疫苗候选物时,使用了 GAS M 蛋白的嵌合保守表位。此前,这些表位已掺入来自酵母的 GCN4 肽以保持其天然螺旋结构。在这里,我们设计了一种基于 GAS M 蛋白最小 B 细胞表位的新型肽表位。这个新的表位能够采用所需的螺旋构象,而不需要外来的 GCN4 侧翼序列。在外加佐剂给药时,选择的表位诱导出显著的免疫反应,并且当被整合到脂质核心肽(LCP)系统中时也是如此。此外,针对该表位产生的抗体能够识别 M 蛋白中的天然 p145 序列。