Recombinant antibody libraries and selection technologies

New Biotechnology

Volumn 28, Issue 5, 2011, Pages 448-452

  Zhou, Heyue ^a   Zhang, Yan Liang ^a   Lu, Guodi ^a   Ji, Henry ^a   Rodi, Charles P ^a  

^a SORRENTO THERAPEUTICS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY LIBRARY; ANTIBODY THERAPEUTICS; HUMAN HEALTH; PASSIVE IMMUNIZATION; RAPID SCREENING; RECOMBINANT ANTIBODY;

IMMUNIZATION; MONOCLONAL ANTIBODIES;

LIBRARIES;

COMPLEMENTARY DNA; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; RECOMBINANT ANTIBODY; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

ACTIVE IMMUNIZATION; DRUG PROTEIN BINDING; DRUG SCREENING; GENE MUTATION; HUMAN; LYMPHOCYTE; NONHUMAN; PRIORITY JOURNAL; REVIEW;

ANIMALS; ANTIBODIES; GENE LIBRARY; HUMANS; IMMUNOLOGIC TECHNIQUES; RECOMBINANT PROTEINS;

EID: 80052796242     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2011.03.013     Document Type: Review

References (32)

1. Smith G.P. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 1985, 228:1315-1317.
2. Parmley S.F., Smith G.P. Antibody-selectable filamentous fd phage vectors: affinity purification of target genes. Gene 1988, 73:305-318.
3. Barbas C.F., et al. Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:7978-7982.
4. Breitling F., et al. A surface expression vector for antibody screening. Gene 1991, 104:147-153.
5. Clackson T., et al. Making antibody fragments using phage display libraries. Nature 1991, 352:624-628.
6. Hoogenboom H.R., et al. Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 1991, 19:4133-4137.
7. Kang A.S., et al. Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces. Proc. Natl. Acad. Sci. U.S.A. 1991, 88:4363-4366.
8. Marks J.D., et al. Bypassing immunization. Human antibodies from V-gene libraries displayed on phage. J. Mol. Biol. 1991, 222:581-597.
9. McCafferty J., et al. Phage antibodies: filamentous phage displaying antibody variable domains. Nature 1990, 348:552-554.
10. de Haard H.J., et al. A large nonimmunized human Fab fragment phage library that permits rapid isolation and kinetic analysis of high affinity antibodies. J. Biol. Chem. 1999, 274:18218-18230.
11. Glanville J., et al. Precise determination of the diversity of a combinatorial antibody library gives insight into the human immunoglobulin repertoire. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:20216-20221.
12. Pelat T., et al. High-affinity, human antibody-like antibody fragment (single-chain variable fragment) neutralizing the lethal factor (LF) of Bacillus anthracis by inhibiting protective antigen-LF complex formation. Antimicrob. Agents Chemother. 2007, 51:2758-2764.
13. Pelat T., Thullier P. Non-human primate immune libraries combined with germline humanization. MAbs 2009, 1:377-381.
14. Barbas C.F., et al. Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem. Proc. Natl. Acad. Sci. U.S.A. 1992, 89:4457-4461.
15. de Kruif J., et al. Selection and application of human single chain Fv antibody fragments from a semi-synthetic phage antibody display library with designed CDR3 regions. J. Mol. Biol. 1995, 248:97-105.
16. Pini A., et al. Design and use of a phage display library. Human antibodies with subnanomolar affinity against a marker of angiogenesis eluted from a two-dimensional gel. J. Biol. Chem. 1998, 273:21769-21776.
17. Hoet R.M., et al. Generation of high-affinity human antibodies by combining donor-derived and synthetic complementarity-determining-region diversity. Nat. Biotechnol. 2005, 23:344-348.
18. Knappik A., et al. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J. Mol. Biol. 2000, 296:57-86.
19. Nahary, L. and Benhar, I. (2009) Design of a human synthetic combinatorial library of single-chain antibodies. In Therapeutic Antibodies: Methods and Protocols, (vol. 525) (Dmitrov ed), Methods Mol. Biol., Springer. pp. 61-80.
20. Cobaugh C.W., et al. Synthetic antibody libraries focused towards peptide ligands. J. Mol. Biol. 2008, 378:622-633.
21. Gao C., et al. Making artificial antibodies: a format for phage display of combinatorial heterodimeric arrays. Proc. Natl. Acad. Sci. U.S.A. 1999, 96:6025-6030.
22. Harvey B.R., et al. Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:9193-9198.
23. Mazor Y., et al. Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli. Nat. Biotechnol. 2007, 25:563-565.
24. Boder E.T., et al. Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:10701-10705.
25. Feldhaus M.J., Siegel R.W. Yeast display of antibody fragments: a discovery and characterization platform. J. Immunol. Methods 2004, 290:69-80.
26. Ho M., et al. Isolation of anti-CD22 Fv with high affinity by Fv display on human cells. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:9637-9642.
27. Ho M., Pastan I. Display and selection of scFv antibodies on HEK-293T cells. Methods Mol. Biol. 2009, 562:99-113.
28. Hanes J., et al. Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display. Nat. Biotechnol. 2000, 18:1287-1292.
29. Fukuda I., et al. Nucleic Acids Res. 2006, 34:e127.
30. de Wildt R.M.T., et al. Antibody arrays for high-throughput screening of antibody-antigen interactions. Nat. Biotechnol. 2000, 18:989-994.
31. Bowley D.R., et al. Libraries against libraries for combinatorial selection of replicating antigen-antibody pairs. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:1380-1385.
32. Vaccines for Biodefense and Emerging and Neglected Diseases 2009, Elsevier/Academic Press. first ed. A.D.T. Barrett, L.R. Stanberry (Eds.).