Sundell Gustav N, Ivarsson Ylva
Department of Chemistry-BMC, Uppsala University, P.O. Box 576, 751 23 Uppsala, Sweden.
Biomed Res Int. 2014;2014:176172. doi: 10.1155/2014/176172. Epub 2014 Sep 11.
Phage display is a powerful technique for profiling specificities of peptide binding domains. The method is suited for the identification of high-affinity ligands with inhibitor potential when using highly diverse combinatorial peptide phage libraries. Such experiments further provide consensus motifs for genome-wide scanning of ligands of potential biological relevance. A complementary but considerably less explored approach is to display expression products of genomic DNA, cDNA, open reading frames (ORFs), or oligonucleotide libraries designed to encode defined regions of a target proteome on phage particles. One of the main applications of such proteomic libraries has been the elucidation of antibody epitopes. This review is focused on the use of proteomic phage display to uncover protein-protein interactions of potential relevance for cellular function. The method is particularly suited for the discovery of interactions between peptide binding domains and their targets. We discuss the largely unexplored potential of this method in the discovery of domain-motif interactions of potential biological relevance.
噬菌体展示是一种用于分析肽结合域特异性的强大技术。当使用高度多样化的组合肽噬菌体文库时，该方法适用于鉴定具有抑制潜力的高亲和力配体。此类实验还可为全基因组扫描潜在生物学相关配体提供共有基序。一种互补但探索较少的方法是在噬菌体颗粒上展示基因组DNA、cDNA、开放阅读框（ORF）或旨在编码目标蛋白质组特定区域的寡核苷酸文库的表达产物。此类蛋白质组文库的主要应用之一是阐明抗体表位。本综述聚焦于利用蛋白质组噬菌体展示来揭示与细胞功能潜在相关的蛋白质-蛋白质相互作用。该方法特别适用于发现肽结合域与其靶标之间的相互作用。我们讨论了这种方法在发现具有潜在生物学相关性的结构域-基序相互作用方面尚未充分探索的潜力。
