A New Strategy for Epitope Mapping by Yeast Surface Display System

被引：1
|
作者：
Jia Jun-Ying [1 ,2 ]
Wang Yun-Bo [1 ]
Tang Jie [1 ]
机构：
[1] Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China
[2] Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
来源：
PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS | 2009年 / 36卷 / 03期
关键词：
yeast display; MIF; epitope mapping; homologous recombination; NECROSIS-FACTOR-ALPHA; ANTIBODIES; FRAGMENTS; PROTEINS;
D O I：
10.3724/SP.J.1206.2008.00446
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
As an effective method of studying soluble protein-protein interactions, yeast display system is now widely used for affinity maturation of single-chain antibodies. Due to the strong homology recombination machinery of yeast and the high-throughput nature of FACS detection, a rapid scan for interaction between antigen-antibody pairs could be easily achieved. Based on this system, a novel and reliable method for determining conformational epitopes was developed. Different fragments of macrophage migration inhibitory factor (MIF) and several point mutations of MIF were displayed on yeast cell surface using homologous recombination technology. Three MIF monoclonal antibodies, 100, 2A12 and 41310, were screened for their binding affinity to each displayed peptide. Utilizing this technology, the key amino acids of MIF that bind to the MIF monoclonal antibodies were easily identified.
引用
收藏
页码：305 / 310
页数：6
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