Harnessing phage and ribosome display for antibody optimisation

被引:58
作者
Dufner, Patrick [1 ]
Jermutus, Lutz [1 ]
Minter, Ralph R. [1 ]
机构
[1] Cambridge Antibody Technol, Cambridge CB1 6GH, England
关键词
D O I
10.1016/j.tibtech.2006.09.004
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
Therapeutic antibodies have become a major driving force for the biopharmaceutical industry; therefore, the discovery and development of safe and efficacious antibody leads have become competitive processes. Phage and ribosome display are ideal tools for the generation of such molecules and have already delivered an approved drug as well as a multitude of clinical candidates. Because they are capable of searching billions of antibody variants in tailored combinatorial libraries, they are particularly applicable to potency optimisation. In conjunction with targeted, random or semi-rational mutagenesis strategies, they deliver large panels of potent antibody leads. This review introduces the two technologies, compares them with respect to their use in antibody optimisation and highlights how they can be exploited for the successful and efficient generation of putative drug candidates.
引用
收藏
页码:523 / 529
页数:7
相关论文
共 85 条
[1]   Upping the ante on antibodies [J].
Baker, M .
NATURE BIOTECHNOLOGY, 2005, 23 (09) :1065-1072
[2]   Optimal screening of surface-displayed polypeptide libraries [J].
Boder, ET ;
Wittrup, KD .
BIOTECHNOLOGY PROGRESS, 1998, 14 (01) :55-62
[3]   Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity [J].
Boder, ET ;
Midelfort, KS ;
Wittrup, KD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2000, 97 (20) :10701-10705
[4]   Antibodies from phage antibody libraries [J].
Bradbury, ARM ;
Marks, JD .
JOURNAL OF IMMUNOLOGICAL METHODS, 2004, 290 (1-2) :29-49
[5]  
Carmen Sara, 2002, Briefings in Functional Genomics & Proteomics, V1, P189, DOI 10.1093/bfgp/1.2.189
[6]   Selection and analysis of an optimized anti-VEGF antibody: Crystal structure of an affinity-matured Fab in complex with antigen [J].
Chen, Y ;
Wiesmann, C ;
Fuh, G ;
Li, B ;
Christinger, HW ;
McKay, P ;
de Vos, AM ;
Lowman, HB .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 293 (04) :865-881
[7]   Molecular dynamics and free-energy calculations applied to affinity maturation in antibody 48G7 [J].
Chong, LT ;
Duan, Y ;
Wang, L ;
Massova, I ;
Kollman, PA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1999, 96 (25) :14330-14335
[8]   Antibody humanization: a case of the 'Emperor's new clothes'? [J].
Clark, M .
IMMUNOLOGY TODAY, 2000, 21 (08) :397-402
[9]  
Colby DW, 2004, METHOD ENZYMOL, V388, P348
[10]   Considerations on antibody-phage display methodology [J].
Conrad, U ;
Scheller, J .
COMBINATORIAL CHEMISTRY & HIGH THROUGHPUT SCREENING, 2005, 8 (02) :117-126