Isolation of high-affinity monomeric human anti-c-erbB-2 single chain Fv using affinity-driven selection

Journal of Molecular Biology

Volumn 255, Issue 1, 1996, Pages 28-43

  Schier, Robert ^a   Bye, Jacqueline ^b   Apell, Gerald ^c   McCall, Adrian ^d   Adams, Gregory P ^d   Malmqvist, Magnus ^e   Weiner, Louis M ^d   Marks, James D ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b Blood Transfusion Service   (United Kingdom)

^c NOVARTIS PHARMA AG   (Switzerland)

^d FOX CHASE CANCER CENTER   (United States)

^e BIACORE AB   (Sweden)

Author keywords

Affinity maturation; c erbB 2; Chain shuffling; Phage antibody libraries; Single chain Fv

Indexed keywords

CANCER ANTIBODY; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; MUTANT PROTEIN; ONCOPROTEIN; TUMOR ANTIGEN;

ANTIBODY AFFINITY; ARTICLE; BACTERIOPHAGE; CONTROLLED STUDY; DIMERIZATION; HUMAN; HYBRIDOMA; IMMUNOGENICITY; IMMUNOGLOBULIN GENE; NONHUMAN; ONCOGENE C ERB; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN ISOLATION;

EID: 0029989324     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0004     Document Type: Article

References (71)

1. Adams, G. P., McCartney J. E., Tai, M.-S., Oppermann, H., Huston, J. S., Stafford, W. F., Bookman, M. A., Fand, I., Houston, L. L. & Weiner, L. M. (1993). Highly specific in vivo tumor targeting by monovalent and divalent forms of 741F8 anti-c-erbB-2 single chain Fv. Cancer Res. 53, 4026-4034.
2. Barbas, C. F., Collet, T. A., Amberg, W., Roben, P., Binley J. M., Hoekstra, D., Cababa, D., Jones, T. M., Williamson, A., Pilkington, G. R., Haigwood, N. L., Cabezas, E., Satterthwait, A. C., Sanz, I. & Burton, D. R. (1993). Molecular profile of an antibody response to HIV-1 as probed by combinatorial libraries. J. Mol. Biol. 230, 812-823.
3. Barbas, C. F., Hu, D., Dunlop, N., Sawyer, L., Cabara, 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, 1, 3809-3813.
4. Berek, C. & Milstein, C. (1987). Mutation drift and repertoire shift in the maturation of the immune response. Immunol. Rev. 96, 23-41.
5. Bird, R. E., Hardman, K. D., Jacobson, J. W., Johnson, S., Kaufman, B. M., Lee, S. M., Lee, T., Pope, S. H., Riordan, G. S. & Whitlow, M. (1988). Single-chain antigen-binding proteins. Science, 42(4877), 423-426.
6. Breitling, S. D., Seehaus, T., Klewinghaus, I. & Little, M. (1991). A surface expression vector for antibody screening. Gene, 104, 147-153.
7. HER2 antibody for human cancer therapy. Proc. Natl Acad. Sci. USA, 89, 4285-4289.
8. Chothia, C., Novotny J., Bruccoleri, R. & Karplus, M. (1985). Domain association in immunoglobulin molecules. The packing of variable domains. J. Mol. Biol. 186, 651-663.
9. Clackson, T., Hoogenboom, H. R., Griffiths, A. D. & Winter, G. (1991). Making antibody fragments using phage display libraries. Nature, 352, 624-628.
10. Clauss, M. A. & Jain, R. K. (1990). Interstitial transport of rabbit and sheep antibodies in normal and neoplastic tissues. Cancer Res. 50, 3487-3492.
11. Colcher, D., Minelli, F. M., Roselli, M., Muraro, R., Simpson-Milenic, D. & Schlom, J. (1988). Radioimmunolocalization of human carcinoma xenografts with B72.3 second generation monoclonal antibodies. Cancer Res. 48, 4597-4603.
12. Collet, T. A., Roben, P., O'Kennedy R., Barbas III, C. F., Burton, D. R. & Lerner, R. A. (1992). A binary plasmid system for shuffling combinatorial antibody libraries. Proc. Natl Acad. Sci. USA, 89, 10026-10030.
13. Crothers, D. M. & Metzger, H. (1972). The influence of polyvalency on the binding properties of antibodies. Immunochemistry, 9, 341-357.
14. De Bellis, D. & Schwartz, I. (1990). Regulated expression of foreign genes fused to lac: control by glucose levels in growth medium. Nucl. Acids Res. 18, 1311.
15. Deng, S., MacKenzie, C. R., Sadowska, J., Michniewicz, J., Young, N. M., Bundle, D. R. & Narang, S. A. (1994). Selection of antibody single-chain variable fragments with improved carbohydrate binding by phage display. J. Biol. Chem. 269, 9533-9538.
16. Deng, S.-J., MacKenzie, C. R., Hirama, T., Brousseau, R., Lowary T. L., Young, N. M., Bundle, D. R. & Narang, S. A. (1995). Basis for selection of improved carbohydrate-binding single-chain antibodies from synthetic gene libraries. Proc. Natl Acad. Sci. USA, 92, 4992-4996.
17. Dower, W. J., Miller, J. F. & Ragsdale, C. W. (1988). High efficiency transformation of E. coli by high voltage electroporation. Nucl Acids Res. 16, 6127-6145.
18. Figini, M., Marks, J. D., Winter, G. & Griffiths, A. D. (1994). In vitro assembly of repertoires of antibody chains on the surface of phage by renaturation. J. Mol. Biol. 239, 68-78.
19. Foote, J. & Eisen, H. N. (1995). Kinetic and affinity limits on antibodies produced during immune responses. Proc. Natl Acad. Sci. USA, 92, 1254-1256.
20. Foote, J. & Milstein, C. (1991). Kinetic maturation of an immune response. Nature, 352, 530-532.
21. Friguet, B., Chaffotte, A. F., Djavadi-Ohaniance, L. & Goldberg, M. E. (1985). Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods, 77, 305-319.
22. Gibson, T. J. (1984). Studies on the Epstein-Barr virus genome. Ph.D. thesis, University of Cambridge.
23. Glockshuber, R., Malia, M., Pfitzinger, I. & Pluckthun, A. (1990). A comparison of strategies to stabilize immunoglobulin Fv-fragments. Biochemistry, 29, 1362-1367.
24. Griffiths, A. D., Malmqvist, M., Marks, J. D., Bye, J. M., Embleton, M. J., McCafferty J., Baier, M., Holliger, K. P., Gorick, B. D., Hughes-Jones, N. C., Hoogenboom, H. R. & Winter, G. (1993). Human anti-self antibodies with high specificity from phage display libraries. EMBO J. 12, 725-734.
25. Gussow, D. & Clackson, T. (1989). Direct clone characterization from plaques and colonies by the polymerase chain reaction. Nucl. Acids Res. 17, 4000.
26. 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.
27. 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.
28. Hirsh, D. & Gold, L. (1971). Translation of the UGA triplet in vitro by tryptophan transfer RNAs. J. Mol. Biol. 58, 459-468.
29. Hochuli, E., Bannwarth, W., Dobeli, H., Gentz, R. & Stuber, D. (1988). Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent. Bio/Technology, 6, 1321-1325.
30. Holliger, P., Prospero, T. & Winter, G. (1993). "Diabodies": small bivalent and bispecific antibody fragments. Proc. Natl Acad. Sci. USA, 90, 6444-6448.
31. Hoogenboom, H. R. & Winter, G. (1992). Bypassing immunisation: human antibodies from synthetic repertoires of germ line VH-gene segments rearranged in vitro. J. Mol. Biol. 227, 381-388.
32. Hoogenboom, H. R., Griffiths, A. D., Johnson, K. S., Chiswell, D. J., Hudson, R & Winter, G. (1991). Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucl Acids Res. 19, 4133-4137.
33. L. J. Immunol. 129, 660-664.
34. Hughes-Jones, N. C., Gorick, B. D., Bye, J. M., Finnern, R., Scott, M. L., Voak, D., Winter, G., Marks, J. D. & Ouwehand, W. H. (1994). Characterisation of human blood group scFv antibodies derived from a V-gene phage display library. Br. J. Haematol. 88, 180-186.
35. Huston, J. S., Levinson, D., Mudgett, H. M., Tai, M. S., Novotny J., Margolies, M. N., Ridge, R. J., Bruccoleri, R. E., Haber, E., Crea, R. & Oppermann, H. (1988). Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc. Natl Acad. Sci. USA, 85, 5879-5883.
36. Huston, J. S., Mudgett-Hunter, M., Mei-Sheng, T., McCartney J., Warren, F., Haber, E. & Opperman, H. (1991). Protein engineering of single-chain Fv analogs and fusion proteins. Methods Enzymol. 203, 46-88.
37. Johnsson, B., Löfås, S. & Lindqvist, G. (1991). Immobilization of proteins to a carboxymethyldextran modified gold surface for BIAcore in surface plasmon resonance. Anal. Biochem. 198, 268-277.
38. Jones, T. A., Zou, J. Y, Cowan, S. W. & Kjeldgaard, M. (1991). Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
39. Kabat, E. A., Wu, T. T., Reid-Miller, M., Perry, H. M. & Gottesman, K. S. (1987). Sequences of Proteins of Immunological Interest, 4th edit., US Department of Health and Human Services, Public Health Service, Bethesda, MD.
40. Kang, A. S., Jones, T. M. & Burton, D. R. (1991). Antibody redesign by chain shuffling from random combinatorial immunoglobulin libraries. Proc. Natl Acad. Sci. USA, 88, 11120-11123.
41. Karlsson, R., Michaelsson, A. & Mattsson, L. (1991). Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods, 145, 229-240.
42. Karlsson, R., Fagerstam, L., Nilshans H. & Persson, B. (1993). Analysis of active antibody concentration. Separation of affinity and concentration parameters. J. Immunol. Methods, 166, 75-84.
43. Knappik, A., Krebber, C. & Pluckthun, A. (1993). The effects of folding catalysts on the in vivo folding process of different antibody fragments expressed in Escherichia coli. Bio/Technology, 11, 77-83.
44. Kortt, A. A., Malby R. L., Caldwell, J. B., Gruen, L. C., Ivancic, N., Lawrence, M. C., Howlett, J. J., Webster, R. G., Hudson, R J. & Colman, P. M. (1994). Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex. Eur. J. Biochem. 221, 151-157.
45. Marks, J. D., Hoogenboom, H. R., Bonnert, T. P., McCafferty J., Griffiths, A. D. & Winter, G. (1991). By-passing immunization: Human antibodies from V-gene libraries displayed on phage. J. Mol. Biol. 222, 581-597.
46. Marks, J. D., Griffiths, A. D., Malmqvist, M., Clackson, T., Bye, J. M. &Winter, G. (1992). Bypassing immunisation: high affinity human antibodies by chain shuffling. Bio/Technology, 10, 779-783.
47. Marks, J. D., Ouwehand, W H., Bye, J. M., Finnern, R., Gorick, B. D., Voak, D., Thorpe, S., Hughes-Jones, N. C. & Winter, G. (1993). Human antibody fragments specific for blood group antigens from a phage display library. Bio/Technology, 11, 1145-1149.
48. 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 Å and 1.9 Å resolution. J. Mol. Biol. 141, 369-391.
49. McCafferty J., Griffiths, A. D., Winter, G. & Chiswell, D. J. (1990). Phage antibodies: filamentous phage displaying antibody variable domains. Nature, 348, 552-554.
50. 2 made by protein folding and bonded through C-terminal cysteinyl peptides. Protein Eng. 8, 301-314.
51. Milenic, D. E., Yokota, T., Filpula, D. R., Finkelman, M. A. J., Dodd, S. W, Wood, J. F., Whitlow, M., Snow, R & Schlom, J. (1991). Construction, binding properties, metabolism, and targeting of a single-chain Fv derived from the pancarcinoma monoclonal antibody CC49. Cancer Res. 51, 6363-6371.
52. Miller, J. H. (1972). Experiments in Molecular Genetics, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
53. Munro, S. & Pelham, H. R. B. (1986). An Hsp-like protein in the ER: Identity with the 78kd glucose regulated protein and immunoglobulin heavy chain binding protein. Cell, 46, 291-300.
54. Nissim, A., Hoogenboom, H. R., Tomlinson, I. M., Flynn, G., Midgley C., Lane, D. & Winter, G. (1994). Antibody fragments from a "single pot" phage display library as immunochemical reagents. EMBO J. 13, 692-698.
55. 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.
56. Riethmuller, G., Schneider-Gadicke, E. & Johnson, J. P. (1993). Monoclonal antibodies in cancer therapy. Curr. Opin. Immunol. 5, 732-739.
57. HER2 Fv-β-lactamase fusion protein for activation of a cephalosporin doxorubicin prodrug. Cancer Res. 55, 63-70.
58. Gln identity from glutamine to tryptophan. Proc. Natl Acad. Sci. USA, 89, 3463-3467.
59. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1990). Molecular Cloning: A Laboratory Manual 2nd edit., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
60. Sanger, F., Nicklen, S. & Coulson, A. R. (1977). DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA, 74, 5463-5467.
61. Schier, R., Marks, J. D., Wolf, E. J., Appell, G., Huston, J. S., Weiner, L. M. & Adams, G. P. (1995). In vitro and in vivo characterization of a human anti-c-erbB-2 single-chain Fv isolated from a filamentous phage antibody library Immunotechnology, 1, 73-81.
62. Sharkey R. M., Gold, D. V., Aninipot, R., Vagg, R., Ballance, C., Newman, E. S., Ostella, F., Hansen, H. J. & Goldenberg, D. M. (1990). Comparison of tumor targeting in nude mice by murine monoclonal antibodies directed against different human colorectal antigens. Cancer Res. 50, 828-834.
63. Stevens, F. J. (1987). Modification of an ELISA-based procedure for affinity determination: correction necessary for use with bivalent antibody. Mol. Immunol. 24, 1055-1060.
64. Tomlinson, I. M., Walter, G., Marks, J. D., Llewelyn, M. B. & Winter, G. (1992). The repertoire of human germline VH sequences reveals about fifty groups of VH segments with different hypervariable loops. J. Mol. Biol. 227, 776-798.
65. Tomlinson, I. M., Williams, S. C., Corbett, S. J., Cox, J. P. L. & Winter, G. (1995). VBASE sequence directory. MRC Centre for Protein Engineering, Cambridge, UK.
66. Weidner, K. M., Denzin, L. K. & Voss, E. W (1992). Molecular stabilization effects of interactions between anti-metatype antibodies and liganded antibodies. J. Biol. Chem. 267, 10281-10288.
67. Wells, J. A. (1990). Additivity of mutational effects in proteins. Biochemistry, 29, 8509-8517.
68. Whitlow, M., Filpula, D., Rollence, M. L., Feng, S.-L. & Wood, J. F. (1994). Multivalent Fvs: characterization of single-chain Fv oligomers and preparation of a bispecific Fv. Protein Eng. 7, 1017-1026.
69. Williams, S. C. & Winter, G. (1993). Cloning and sequencing of human immunoglobulin V lambda gene segments. Eur. J. Immunol. 23, 1456-1461.
70. Yokota, T., Milenic, D., Whitlow, M. & Schlom, J. (1992). Rapid tumor penetration of a single-chain Fv and comparsion with other immunoglobulin forms. Cancer Res. 52, 3402-3408.
71. Zinoni, F., Birkmann, A., Leinfelder, W. & Bock, A. (1987). Cotranslational insertion of selenocysteine into formate dehydrogenase from Escherichia coli directed by a UGA codon. Proc. Natl Acad. Sci. USA, 4, 3156-3160.