Coulon Stephane, Metais Jean-Yves, Chartier Martine, Briand Jean-Paul, Baty Daniel
The Scripps Research Institute, Department of Molecular Biology, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
J Pept Sci. 2004 Nov;10(11):648-58. doi: 10.1002/psc.574.
A 10-mer random peptide library displayed on filamentous bacteriophage was used to determine the molecular basis of the interaction between the monoclonal anti-colicin A antibody 1C11 and its cognate epitope. Previous studies established that the putative epitope recognized by 1C11 antibody is composed of amino acid residues 19-25 (RGSGPEP) of colicin A. Using the phage display technique it was confirmed that the epitope of 1C11 antibody was indeed restricted to residues 19-25 and the consensus motif RXXXPEP was identified. Shorter consensus sequences (RXXPEP, RXXEP, KXXEP) were also selected. It was also demonstrated that the disulfide bond found in one group of the selected peptides was crucial for 1C11 antibody recognition. It was shown that cyclization of the peptides by disulfide bond formation could result in a structure that mimics the natural epitope of colicin A.
一个展示在丝状噬菌体上的10肽随机肽库被用于确定单克隆抗大肠杆菌素A抗体1C11与其同源表位之间相互作用的分子基础。先前的研究表明，1C11抗体识别的假定表位由大肠杆菌素A的氨基酸残基19 - 25（RGSGPEP）组成。利用噬菌体展示技术证实，1C11抗体的表位确实局限于残基19 - 25，并鉴定出共有基序RXXXPEP。还选择了较短的共有序列（RXXPEP、RXXEP、KXXEP）。还证明了在一组选定肽中发现的二硫键对于1C11抗体的识别至关重要。结果表明，通过形成二硫键使肽环化可产生一种模拟大肠杆菌素A天然表位的结构。
