National Institute of Diagnostics and Vaccine Development in Infectious Diseases, The Key Laboratory of the Ministry of Education for Cell Biology and Tumor Cell Engineering, School of Life Sciences, Xiamen University, Xiamen 361005, China.
Vet Microbiol. 2010 Sep 28;145(1-2):17-22. doi: 10.1016/j.vetmic.2010.02.032. Epub 2010 Mar 3.
A sub-library based on peptide mimic 125 was designed and constructed, and 18 phagotopes specifically binding 8H5mAb were isolated. Antisera against three phagotopes, containing peptide 12MH-1, 12MH-5 and 12MH-8 reacted with 3 different H5N1 virus strains, but not with 2 H1N1 and 2 H3N2 viruses by Dot blots. The affinity of 12MH-8 was approximately eight times more than 12MH-1 or 12MH-5 or parent peptide 125. Furthermore, synthesized 12MH-1 and 12MH-8 could block the 8H5mAb binding with 4 H5N1 virus strains via hemagglutinin inhibition. These results suggest that these 3 mimotopes closely mimics the native 8H5 epitopes.
设计并构建了一个基于肽模拟物 125 的子库，并分离出了 18 个特异性结合 8H5mAb 的噬菌体肽。针对三种噬菌体肽 12MH-1、12MH-5 和 12MH-8 的抗血清与 3 种不同的 H5N1 病毒株反应，但与 2 种 H1N1 和 2 种 H3N2 病毒株无反应，通过斑点印迹法。12MH-8 的亲和力大约比 12MH-1 或 12MH-5 或亲本肽 125 高 8 倍。此外，合成的 12MH-1 和 12MH-8 可以通过血凝素抑制阻断 8H5mAb 与 4 种 H5N1 病毒株的结合。这些结果表明这 3 个模拟表位非常类似于天然的 8H5 表位。
