A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments

被引：80

作者：

Huls, GA

Heijnen, IAFM

Cuomo, ME

Koningsberger, JC

Wiegman, L

Boel, E

de Vries, ARV

Loyson, SAJ

Helfrich, W

Henegouwen, GPV

van Meijer, M

de Kruif, J

Logtenberg, T ^{[1
]}

机构：

[1] Univ Utrecht Hosp, Dept Immunol, Utrecht, Netherlands

[2] Univ Utrecht Hosp, Dept Gastroenterol, Utrecht, Netherlands

[3] Univ Utrecht Hosp, Dept Pathol, Utrecht, Netherlands

[4] Univ Utrecht Hosp, Dept Microbiol, Utrecht, Netherlands

[5] Univ Utrecht Hosp, Utrecht Biotechnol Syst, Utrecht, Netherlands

[6] Univ Groningen Hosp, Dept Clin Immunol, NL-9713 EZ Groningen, Netherlands

来源：

NATURE BIOTECHNOLOGY | 1999年 / 17卷 / 03期

关键词：

phage display; Ep-CAM; single-chain Fv; immunotherapy; recombinant antibodies;

D O I：

10.1038/7023

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

A single-chain Fv antibody fragment specific for the tumor-associated Ep-CAM molecule was isolated from a semisynthetic phage display library and converted into an intact, fully human IgG1 monoclonal antibody (huMab), The purified huMab had an affinity of 5 nM and effectively mediated tumor cell killing in: in vitro and in vivo assays. These experiments show that nonimmunized phage antibody display libraries can be used to obtain high-affinity, functional, and clinically applicable huMabs directed against a tumor-associated antigen.

引用

页码：276 / 281

页数：6

共 45 条

[1] Cytoplasmic tail regulates the intercellular adhesion function of the epithelial cell adhesion molecule [J].