Sibille P, Strosberg A D
Institut Cochin de Génétique Moléculaire, Unité d'Immunopharmacologie moléculaire et génétique des virus, CNRS UPR 415, Paris, France.
Immunol Lett. 1997 Dec;59(3):133-7. doi: 10.1016/s0165-2478(97)00111-9.
Phage peptide libraries constitute powerful tools for the mapping of epitopes recognized by monoclonal antibodies. We report here the characterization of an antibody directed against a 20-residue peptide derived from the surface glycoprotein of the feline immunodeficiency virus. The isolation of the WRPDF consensus sequence from a phage display library defined the exact epitope recognized by the mAb. Compared with known immunogenic peptides of the FIV envelope, it corresponds to the most immunodominant peptide found in the whole molecule. Kinetic data describing the antibody-peptide interactions were obtained by surface plasmon resonance. The antibody binds the peptide with a KD in the nanomolar range.
噬菌体肽库是用于绘制单克隆抗体所识别表位的强大工具。我们在此报告一种针对源自猫免疫缺陷病毒表面糖蛋白的20个残基肽的抗体的特性。从噬菌体展示文库中分离出的WRPDF共有序列确定了该单克隆抗体所识别的确切表位。与已知的猫免疫缺陷病毒包膜免疫原性肽相比，它对应于整个分子中发现的最具免疫显性的肽。通过表面等离子体共振获得了描述抗体 - 肽相互作用的动力学数据。该抗体以纳摩尔范围内的解离常数（KD）结合该肽。
