人甲胎蛋白的表位作图

Epitope mapping of human alpha-fetoprotein.

作者信息

Yakimenko E F, Yazova A K, Goussev A I, Abelev G I

机构信息

Laboratory of Immunochemistry, Institute of Carcinogenesis, Blokhin Cancer Research Center, Russian Academy of Medical Sciences, Moscow, 115478, Russia.

出版信息

Biochemistry (Mosc). 2001 May;66(5):524-30. doi: 10.1023/a:1010258902421.

DOI:10.1023/a:1010258902421

PMID:11405888

Abstract

The epitope structure of human alpha-fetoprotein (AFP) was studied using more than 50 monoclonal antibodies (MAB) to human AFP. These MAB obtained from various world laboratories of the TD-2 AFP Workshops of the International Society for Oncodevelopmental Biology and Medicine (ISOBM-1996-1998-2000) were analyzed by competitive immunoaffinity electrochromatography (IAE) on nitrocellulose membranes (NCM). Five types of interaction of the AFP-MAB complex with the MAB fixed on NCM were found: 1) complete neutralization; 2) partial neutralization; 3) unidirectional neutralization; 4) enhanced binding; 5) lack of interaction. By IAE, 51 MAB were found to recognize 23 different epitopes in the AFP molecule. Based on these findings, an epitope map of AFP was designed which consists of eight epitope clusters and eight individual epitopes. The epitope location is considered with respect to the conformational state of the AFP molecule. Possible causes of the five types of interaction found on neutralization are discussed.

摘要

利用50多种抗人甲胎蛋白（AFP）的单克隆抗体（MAB）对人甲胎蛋白的表位结构进行了研究。这些单克隆抗体取自国际肿瘤发生生物学与医学协会（ISOBM - 1996 - 1998 - 2000）TD - 2甲胎蛋白研讨会的各个国际实验室，并通过在硝酸纤维素膜（NCM）上的竞争性免疫亲和电色谱法（IAE）进行分析。发现甲胎蛋白 - 单克隆抗体复合物与固定在NCM上的单克隆抗体存在五种相互作用类型：1）完全中和；2）部分中和；3）单向中和；4）增强结合；5）无相互作用。通过免疫亲和电色谱法发现，51种单克隆抗体识别甲胎蛋白分子中的23个不同表位。基于这些发现，设计了甲胎蛋白的表位图谱，该图谱由八个表位簇和八个单个表位组成。表位位置是根据甲胎蛋白分子的构象状态来考虑的。讨论了中和时发现的五种相互作用类型的可能原因。