CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range

Journal of Molecular Biology

Volumn 254, Issue 3, 1995, Pages 392-403

  Yang, Wei Ping ^a   Green, Kimberly ^a   Pinz Sweeney, Sally ^a   Briones, Amelia T ^a   Burton, Dennis R ^a   Barbas, Carlos F ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Additivity effects; Human immunodeficiency virus; Passive immunization; Phage display; Structure function

Indexed keywords

EID: 0029564921     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1995.0626     Document Type: Article

References (37)

1. Barbas, C. F., III & Wagner, J. (1995). Synthetic human antibodies: selecting and evolving functional proteins. Methods, 8, 94-103.
2. Barbas, C. F., III, Kang, A. S., Lerner, R. A. & Benkovic, S. J. (1991). Assembly of combinatorial antibody libraries on phage surfaces: The gene III site. Proc. Natl Acad. Sci. USA, 88, 7978-7982.
3. Barbas, C. F., III, Bain, J. D., Hoekstra, D. M. & Lerner, R. A. (1992a). Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem. Proc. Natl Acad. Sci. USA, 89, 4457-4461.
4. Barbas, C. F., III, Bjorling, E., Chiodi, F., Dunlop, N., Cababa, D., Jones, T. M., Zebedee, S. L., Persson, M. A. A., Nara, P. L., Norrby, E. & Burton, D. R. (1992b). Recombinant human Fab fragments neutralize human type 1 immunodeficiency virus in vitro. Proc. Natl Acad. Sci. USA, 89, 9339-9343.
5. Barbas, C. F., III, Amberg, W., Simoncsits, A., Jones, T. M. & Lerner, R. A. (1993a). Selection of human anti-hapten antibodies from semisynthetic libraries. Gene, 137, 57-62.
6. Barbas, C. F., III, Collet, T. A., Amberg, W., Roben, P., Binley J. M., Hoekstra, D., Cababa, D., Jones, T. M., Williamson, R. A., Pilkington, G. R., Haigwood, N. L., Cabezas, E., Satterthwait, A. C., Sanz, I. & Burton, D. R. (1993b). Molecular profile of an antibody response to HIV-1 as probed by combinatorial libraries. J. Mol. Biol. 230, 812-823.
7. Barbas, C. F., III, Hu, D., Dunlop, N., Sawyer, L., Cababa, D., Hendry, R. M., Nara, P. L. & Burton, D. R. (1994). In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity. Proc. Natl Acad. Sci. USA, 91, 3809-3813.
8. Barbas, S. M. & Barbas, C. F., III (1994). Filamentous phage display Fibrinolysis, 8, 245-252.
9. Behring, E. A. (1893). Die Geschichte der Diphtherie. pp. 186-187. Thieme, Leipzig.
10. Burton, D. R. & Barbas, C. F., III (1994). Human antibodies from combinatorial libraries. Advan. Immunol. 57, 191-280.
11. Burton, D. R., Pyati, J., Koduri, R., Sharp, S. J., Thornton, G. B., Parren, P. W. H. I., Sawyer, L. S. W., Hendry R. M., Dunlop, N., Nara, P. L., Lamacchia, M., Garratty E., Stiehm, E. R., Bryston, Y. J., Cao, Y., Moore, J. P., Ho, D. D. & Barbas, C. F., III (1994). Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody. Science, 266, 1024-1027.
12. Capon, D. J., Chamow, S. M., Mordenti, J., Marsters, S. A., Gregory T., Mitsuya, H., Byrn, R. A., Lucas, C., Wurm, F. M., Groopman, J. E., Broder, S. & Smith, D. H. (1989). Designing CD4 immunoadhesins for AIDS therapy. Nature, 337, 525-531.
13. Carter, P, Kelley R. F., Rodrigues, M. L., Snedecor, B., Covarrubias, M., Velligan, M. D., Wong, W. L. T., Rowland, A. M., Kotts, C. E., Carver, M. E., Yang, M., Bourell, J. H., Shepard, H. M. & Henner, D. (1991). High level Escherichia coli expression and production of a bivalent humanized antibody fragment. Bio/Tech-nology, 10, 163-167.
14. Chothia, C., Lesk, A. M., Tramontano, A., Levitt, M., Smith-Gill, S. J., Air, G., Sheriff, S., Padlan, E. A., Davies, D., Tulip, W. R., Colman, P. M., Spinelli, S., Alzari, P M. & Poljak, R. J. (1989). Conformations of immunoglobulin hypervariable regions. Nature, 342, 877-883.
15. Chothia, C., Lesk, A. M., Gherardi, E., Tomlinson, I. M., Walter, G., Marks, J. M., Llewelyn, M. B. & Winter, G. (1992). The structural repertiore of human VH segments. J. Mol. Biol. 227, 799-817.
16. D’Souza, M. P, Geyer, S. J., Hanson, C. V., Hendry M., Milman, G. & Collaborating Investigators (1994). Evaluation of monoclonal antibodies to HIV-1 by neutralization and binding assays: an international collaboration. AIDS, 8, 169-181.
17. Foote, J. & Winter, G. (1992). Antibody framework residues affecting the conformation of the hypervariable loops. J. Mol. Biol. 224, 487-499.
18. Hawkins, R. E., Russell, S. J. & Winter, G. (1992). Selection of phage antibodies by binding affinity mimicking affinity maturation. J. Mol. Biol. 226, 889-896.
19. Hawkins, R. E., Russell, S. J., Baier, M. & Winter, G. (1993). The contribution of contact and non-contact residues of antibody in the affinity of binding to antigen. J. Mol. Biol. 234, 958-964.
20. Kabat, E. A., Wu, T. T., Perry, H. M., Gottesman, K. S. & Foeller, C. (1991). Sequences of Proteins of Immunological Interest. 5th edit., US Department of Health and Human Services, Public Health Service, National Institutes of Health (NIH Publication no. 91-3242).
21. Karlsson, R., Michaelsson, A. & Mattson, A. (1991). Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods, 145, 229-240.
22. Kelley R. F. & O’connell, M. P. (1993). Thermodynamic analysis of an antibody functional epitope. Biochemistry, 32, 6828-6835.
23. Lerner, R. A., Benkovic, S. J. & Schultz, P G. (1991). At the crossroads of chemistry and immunology: catalytic antibodies. Science, 252, 659-667.
24. LiCata, V. J. & Ackers, G. K. (1995). Long-range, small magnitude nonadditivity of mutational effects in proteins. Biochemistry, 34, 3133-3139.
25. Lowman, H. B. & Wells, J. A. (1993). Affinity maturation of human growth hormone by monovalent phage display. J. Mol. Biol. 234, 564-578.
26. Lowman, H. B., Bass, S. H., Simpson, N. & Wells, J. A. (1991). Selecting high-affinity binding proteins by monovalent phage display. Biochemistry, 30, 10832-10838.
27. Marquart, M., Deisenhofer, J., Huber, R. & Palm, W. (1980). Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 A and 1.9 A resolution. J. Mol. Biol. 141, 369-391.
28. Nakamura, G. R., Byrn, R., Wiles, D. M., Fox, J. A., Hobbs, M. R., Hastings, R., Wessling, H. C., Norcross, M. A., Fendly B. M. & Berman, P W. (1993). Strain specificity and binding affinity requirements of neutralizing monoclonal antibodies to the C4 domain of gp120 from human immunodeficiency virus type I. J. Virol. 67, 6179-6191.
29. Padlan, E. A. (1994). Anatomy of the antibody molecule. Mol. Immunol. 31, 169-217.
30. Riechmann, L. & Weill, M. (1993). Phage display and selection of a site-directed randomized single-chain antibody Fv fragment for its affinity improvement. Biochemistry, 32, 8848-8855.
31. Roben, P, Moore, J. P, Thali, M., Sodroski, J., Barbas, C. F., III & Burton, D. R. (1994). Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. J. Virol. 68, 4821-4828.
32. Ryu, S.-E., Kwong, P. D., Truneh, A., Porter, T. G., Arthos, J., Rosenberg, M., Dai, X., Xuong, N.-H., Axel, R., Sweet, R. W. & Hendrickson, W. A. (1990). Crystal structure of an HIV-binding recombinant fragment of human CD4. Nature, 348, 419-426.
33. Sanz, I. (1991). Multiple mechanisms participate in the generation of diversity of human H chain CDR3 regions. J. Immunol. 147, 1720-1729.
34. van der Merwe, P A., Brown, M. H., Davis, S. J. & Barclay A. N. (1993). Affinity and kinetic analysis of the interaction of the cell adhesion molecules rat CD2 and CD48. EMBO J. 12, 4945-4954.
35. Wells, J. A. (1990). Perspectives in biochemistry: additivity of mutational effects in proteins. Biochemistry, 29, 8509-8517.
36. Wilson, I. A. & Stanfield, R. L. (1993). Antibody-antigen interactions. Curr. Opinion Struct. Biol. 3, 113-118.
37. Wu, T. T., Johnson, G. & Kabat, E. A. (1993). Length distribution of CDRH3 in antibodies. Protein: Struct. Funct. Genet. 16, 1-7.