Carbonell X, Benito A, Villaverde A
Institut de Biologia Fonamental and Departament de Genètica i Microbiologia, Universitat Autònoma de Barcelona, Bellaterra, Spain.
FEBS Lett. 1996 Nov 18;397(2-3):169-72. doi: 10.1016/s0014-5793(96)01169-6.
A peptide reproducing the G-H loop amino acid sequence of foot-and-mouth disease virus VP1 protein was fused to the solvent-exposed C-terminus of the bacteriophage P22 tailspike protein [Carbonell and Villaverde (1996) Gene, in press], a homotrimeric polypeptide with a strong beta-helical structure. This fusion does not interfere with the biological activities of the phage tail. The antigenic profile of the complex antigenic site A within the G-H loop has been determined by competitive ELISA with a panel of monoclonal antibodies directed against different overlapping B-cell epitopes. The antigenic data have been compared with those obtained with a set of 12 chimeric beta-galactosidases displaying the G-H loop on different exposed regions. A high coincidence has been evidenced between the antigenicity of the viral peptide fused to the phage protein and that of some peptides inserted in an exposed loop of the activating interface of beta-galactosidase. This indicates that completely different structural frameworks of carrier proteins can provide similar constraints that allow the recombinant peptide to successfully mimic the antigenicity, and probably conformational features, of the natural peptide on the virion surface.
将一段复制口蹄疫病毒VP1蛋白G-H环氨基酸序列的肽段，融合到噬菌体P22尾钉蛋白的溶剂暴露C末端[Carbonell和Villaverde（1996年），《基因》，即将发表]，该尾钉蛋白是一种具有强β-螺旋结构的同三聚体多肽。这种融合不干扰噬菌体尾部的生物学活性。通过与一组针对不同重叠B细胞表位的单克隆抗体进行竞争性ELISA，确定了G-H环内复合抗原位点A的抗原谱。已将这些抗原数据与用一组12种在不同暴露区域展示G-H环的嵌合β-半乳糖苷酶获得的数据进行了比较。已证明，与噬菌体蛋白融合的病毒肽的抗原性与插入β-半乳糖苷酶激活界面暴露环中的一些肽的抗原性高度一致。这表明，载体蛋白完全不同的结构框架可以提供相似的限制条件，使重组肽能够成功模拟病毒体表面天然肽的抗原性，可能还有构象特征。
