Multivalent Antibody Fragments with High Functional Affinity for a Tumor-Associated Carbohydrate Antigen

Journal of Immunology

Volumn 157, Issue 7, 1996, Pages 2989-2997

  Rheinnecker, Michael ^a,b   Hardt, Christina ^b   Ilag, Leodevico L ^b   Kufer, Peter ^c   Gruber, Rudolf ^c   Hoess, Adolf ^b   Lupas, Andrei ^d   Rottenberger, Christine ^b   Plückthun, Andreas ^e   Pack, Peter ^b,f  

^a GRÜNENTHAL GMBH   (Germany)

^b MorphoSys GmbH   (Germany)

^c Institute for Immunology   (Germany)

^d MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^e UNIVERSITY OF ZURICH   (Switzerland)

^f MorphoSys GmbH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CANCER ANTIBODY; HYBRID PROTEIN; IMMUNOGLOBULIN FRAGMENT; IMMUNOGLOBULIN FV; IMMUNOGLOBULIN G; LEWIS Y ANTIGEN; PROTEIN P53; TUMOR ANTIGEN;

AMINO ACID SEQUENCE; ANIMAL; ANTIBODY AFFINITY; ARTICLE; BLOOD GROUP LEWIS SYSTEM; CARBOHYDRATE ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; ESCHERICHIA COLI; HUMAN; IMMUNOLOGY; MOLECULAR GENETICS; MOUSE; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, NEOPLASM; ANTIBODY AFFINITY; ANTIGENS, NEOPLASM; CARBOHYDRATE SEQUENCE; ESCHERICHIA COLI; HUMANS; IMMUNOGLOBULIN FRAGMENTS; IMMUNOGLOBULIN G; LEWIS BLOOD-GROUP SYSTEM; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; TUMOR SUPPRESSOR PROTEIN P53;

EID: 0030266707     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (58)

1. Karush, F. 1970. Affinity and the immune response. Ann. NY Acad. Sci. 169:56.
2. Karush, F. 1978. The affinity of antibody: range, variability, and the role of multivalence. In Comprehensive Immunology, Vol. 5. G. W. Litman and R. W. Good, eds. Plenum Press, New York, pp. 85-116.
3. Hornick, C. L., and F. Karush. 1972. Antibody affinity. III. The role of multivalence. Immunochemistry 9:325.
4. Crothers, D. M., and H. Metzger. 1972. The influence of polyvalency on the binding properties of antibodies. Immunochemistry 9:341.
5. Verrey, F., and K. Drickamer. 1993. Determinants of oligomeric structure in the chicken liver glycoprolein receptor. Biochem. J. 292:149.
6. Lee, R. T., Y. Ichikawa, T. Kawasaki, K. Drickamer, and Y. C. Lee. 1992. Multivalent ligand binding by serum mannose-binding protein. Arch. Biochem. Biophys. 299:129.
7. Hammarström, S. 1973. Binding of Helix Pomatia A hemagglutinin to human erythrocytes and their cells: influence of multivalent interaction on affinity. Scand. J. Immunol. 2:53.
8. Toone, E. J. 1994. Structure and energetics of protein-carbohydrate complexes. Curr. Op. Struct. Biol. 4:719.
9. Elkins, K., and E. S. Metcalf. 1984. Monoclonal antibodies demonstrate multiple epitopes on the O antigens of Salmonella typhimurium LPS. J. Immunol. 133:2255.
10. Greenspan, N. S., and L. J. Cooper. 1992. Intermolecular cooperativity: a clue to why mice have IgG3? Immunol. Today 13:164.
11. Hsu, D. K., R. I. Zuberi, and F. T. Liu. 1992. Biochemical and biophysical characterization of human recombinant IgE binding protein, an S-type animal lectin. J. Biol. Chem. 267:14167.
12. Andersen, O., P. Friis, N. E. Holm, K. Vilsgaard, R. G. Leslie, and S. E. Svehag. 1992. Purification, subunit characterization and ultrastructure of three soluble bovine lectins: conglutinin, mannose-binding protein and the pentraxin serum amyloid P-component. J. Struct. Biol. 109:201.
13. Feizi, T. 1985. Demonstration by monoclonal antibodies that carbohydrate structures of glycoproteins and glycolipids are onco-developmental antigens. Nature 314:53.
14. Hakomori, S. 1984. Tumor-associated carbohydrate antigens. Annu. Rev. Immunol. 2:103.
15. Bundle, D. R., and N. M. Young. 1992. Carbohydrate-protein interactions in antibodies and lectins. Curr. Op. Struct. Biol. 2:666.
16. Brummell, D. A., V. P. Sharma, N. N. Anand, D. Bilous, G. Dubuc, J. Michniewicz, C. R. MacKenzie, J. Sadowska, B. W. Sigurskjold, B. Sinnott, N. M. Young, D. R. Bundle, and S. A. Narang. 1993. Probing the combining site of an anti-carbohydrate antibody by saturation-mutagenesis: role of the heavy-chain CDR3 residues. Biochemistry 32:1180.
17. Deng, S., R. MacKenzie, J. Sadowska, J. Michniewicz, M. N. Young, D. R. Bundle, and S. A. Narang. 1994. Selection of antibody single-chain variable fragments with improved carbohydrate binding by phage display. J. Biol. Chem. 269:9533.
18. b, X and Y blood group antigens in human colonic tumors and normal tissue and in human tumor-derived cell lines. Cancer Res. 46:1553.
19. Kim, Y. S., M. Yuan, S. H. Itzkowitz, Q. Sun, T. Kaizu, A. Palekar, B. F. Trump, and S. Hakomori. 1986. Expression of LeY and extended LeY blood group-related antigens in human malignant, premalignant and nonmalignant colonic tissues. Cancer Res. 46:5985.
20. Schlimok, G., K. Pantel, and G. Riethmüller. 1994. Minimal residual metastatic tumor cells as targets for antibody-based adjuvant therapy of cancer. In European Association for Cancer Research, EACR XIII Programme and Abstract Book, pp. 75-82.
21. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. A Laboratory Manual, 2nd Ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
22. Ge, L., A. Knappik, P. Pack, C. Freund, and A. Plückthun. 1995. Expressing antibodies in Escherichia coil. In Antibody Engineering, 2nd Ed. C. A. K. Borrebaeck, ed. Oxford University Press, Oxford, pp. 229-266.
23. Knappik, A., and A. Plückthun. 1994. An improved affinity tag based on the FLAG peptide for the detection and purification of recombinant antibody fragments. Biotechniques 17:754.
24. Lindner, P., B. Guth, C. Wülfing, C. Krebber, B. Steipe, F. Müller, and A. Plückthim. 1992. Purification of native proteins from the cytoplasm and periplasm of Escherichia coli using IMAC and histidine tails: a comparison of proteins and protocols. Methods 4:41.
25. Pack, P., M. Kujau, V. Schroeckh, U. Knüpfer, R. Wenderoth, D. Riesenberg, and A. Plückthun. 1993. Improved bivalent mini-antibodies, with identical avidity as whole antibodies, produced by high cell density fermentation of Escherichia coli. Biotechnology 11:1271.
26. Dangl, J. L., T. G. Wensel, S. L. Morrison, L. Stryer, L. A. Herzenberg, and T. Oi. 1988. Segmental flexibility and complement fixation of genetically engineered chimeric human, rabbit and mouse antibodies. EMBO J. 7:1989.
27. Clore, G. M., J. G. Omichinski, K. Sakaguchi, N. Zambrano, H. Sakamoto, E. Appella, and A. M. Gronenborn. 1995. Interhelical angles in the solution structure of the oligomerization domain of p53: correction. Science 267:1515.
28. Jeffrey, P. D., S. Gorina, and N. P. Pavletich. 1995. Crystal structure of the tetramerization domain of the p53 tumor suppressor at 1.7 angstroms. Science 267:1498.
29. Sakamoto, H., M. S. Lewis, H. Kodama, E. Appella, and K. Sakaguchi. 1994. Specific sequences from the carboxyl terminus of the human p53 gene product form anti-parallel tetramers in solution. Proc. Natl. Acad. Sci. USA 91:8974.
30. Prodromou, C., and L. H. Pearl. 1992. Recursive PCR: a novel technique for total gene synthesis. Protein Eng. 5:827.
31. Perry, M., and H. Kirby. 1990. Monoclonal antibodies and their fragments. In Protein Purification Applications. E. L. V. Harris and S. Angal, eds., IRL Press, Oxford, p. 147.
32. Gill, S. T., and P. H. von Hippel. 1989. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182:319.
33. Johnsson, U., L. Fägerstam, B. Ivarsson, B. Johnsson, R. Karlsson, K. Lundh, S. Löfas, B. Persson, H. Roos, I. Rönnberg, S. Sjölander, E. Stenberg, R. Stahlberg, C. Urbaniczy, H. Ostlin, and M. Malmqvist. 1991. Real time biospecific interaction analysis surface plasmon resonance and a sensor chip technology. Biotechniques 11:620.
34. Co, M. S., and H. Loibner. 1992. European Patent # 0 528 767 A1, filed August 18, 1992.
35. McAndrew, S. J., L. K. Gilliland, K. M. Ervin, S. M. Webb, H. Wan, H. P. Fell, K. E. Hellström, I. Hellström, and W. L. Cosand. 1996. The carcinoma-reactive monoclonal antibody BR96: cloning, expression and characterization of a single-chain antibody fragment. Mol. Immunol. In press.
36. Brinkmann, U., L. H. Pai, D. J. FitzGerald, M. Willingham, and I. Pastan. 1991. B3(Fv)-PE38KDEL, a single-chain immunotoxin that causes complete regression of a human carcinoma in mice. Proc. Natl. Acad. Sci. USA 88:8616.
37. Kaneko, T., Y. Iba, K. Zenita, K. Shigeta, K. Nakano, W. Itoh, Y. Kurosawa, R. Kannagi, and K. Yasukawa. 1993. Preparation of mouse-human chimeric antibody to an embryonic carbohydrate antigen, Lewis Y. J. Biochem. 113:114.
38. Chothia, C., and A. M. Lesk. 1987. Canonical structures for the hypervariable regions of immunoglobulins. J Mol. Biol. 196:901.
39. Pack, P., and A. Plückthun. 1992. Mini-antibodies: use of amphipathic helices to produce functional, flexibly linked dimeric Fv fragments with high avidity in Escherichia coli. Biochemistry 31:1579.
40. Pack, P., K. Müller, R. Zahn, and A. Plückthun. 1995. Tetravalent mini-antibodies with high avidity assembling in Escherichia coli. J. Mol. Biol. 246:28.
41. Hill, C. P., D. H. Anderson, L. Wesson, W. F. deGrado, and D. Eisenberg. 1990. Crystal structure of alpha 1: implications for protein design. Science 294:543.
42. Whitlow, M., B. A. Bell, S. L. Feng, D. Filpula, K. D. Hardman, S. L. Hubert, M. L. Rollence, J. F. Wood, M. E. Schott, and D. E. Milenic. 1994. An improved linker for single chain Fv with reduced aggregation and enhanced proteolytic stability. Protein Eng. 7:1017.
43. Holliger, P., and G. Winter. 1993. Engineering bispecific antibodies. Curr. Op. Biotech. 4:446.
44. Karlsson, R., A. Michaelsson, and L. Mattson. 1991. Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor-based analytical system. J. Immunol. Methods 145:229.
45. Glaser, R. W. 1993. Antigen-antibody binding and mass transport by convection and diffusion to a surface: a two-dimensional computer model of binding and dissociation kinetics. Anal. Biochem. 213:152.
46. Wolff, E. A., J. Esselstyn, G. Maloney, and H. V. Raff. 1992. Human monoclonal antibody homodimers: effect of valency on in vitro and in vivo antibacterial activity. J. Immunol. 148:2469.
47. Shopes, B. 1992. A genetically engineered human IgG mutant with enhanced cytolytic activity. J. Immunol. 148:2918.
48. Shuford, W., H. V. Raff, J. W. Finley, J. Esselstyn, and L. J. Harris. 1991. Effect of light chain V region duplication on IgG oligomerization and in vivo efficacy. Science 252:724.
49. Perisic, O., P. A. Webb, P. Holliger, G. Winter, and R. Williams. 1994. Crystal structure of a diabody, a dimeric antibody fragment. Structure 2:1217.
50. Ito, W., and Y. Kurosawa. 1993. Development of an artificial antibody system with multiple valency using an Fv fragment fused to a fragment of protein A. J. Biol. Chem. 268:20668.
51. Carter, P., R. F. Kelley, M. L. Rodrigues, B. Snedecor, M. Covarrubias, M. D. Velligan, W. L. T. Wong, A. M. Rowland, C. E. Kotts, M. E. Carver, M. Yang, J. H. Bourell, H. M. Shepard, and D. Henner. 1992. High level Escherichia coli expression and production of a dimeric humanized antibody fragment. Biotechnology 10:163.
52. Cumber, A. J., E. S. Ward, G. Winter, G. D. Parnell, and E. J. Wawrzynczak. 1992. Comparative stabilities in vitro and in vivo of a recombinant mouse FvCys fragment and a bisFvCys conjugate. J. Immunol. 149:120.
53. Cook, A. G., and P. J. Wood. 1994. Chemical synthesis of bispecific monoclonal antibodies: potential advantages in immunoassay systems. J. Immunol. Methods 171:227.
54. Arévalo, J. H., E. A. Stura, M. J. Taussig, and I. A. Wilson. 1993. Three-dimensional structure of an anti-steroid Fab′ and progesterone-Fab′ complex. J. Mol. Biol. 231:10.
55. Nieba, L., A. Krebber, and A. Plückthun. 1996. Competition BIAcore for measuring true affinities: large differences to values determined from binding kinetics. Anal. Biochem. 234:155.
56. Thomas, G. D., M. J. Chappell, P. W. Dykes, D. B. Ramsden, K. R. Godfrey, J. R. M. Ellis, and A. R. Bradwell. 1989. Effect of dose, molecular size, affinity, and protein uptake of antibody or ligand: a biomathematical model. Cancer Res. 49:3290.
57. Haunschild, J., H. P. Faro, P. Pack, and A. Plückthun. 1995. Pharmacokinetic properties of bivalent mini-antibodies and comparison to other immunoglobulin forms. Antibody, Immunoconjugates & Radiopharmaceuticals 8:111.
58. Trail, P. A., D. Willner, S. J. Lasch, A. J. Henderson, S. Hofstead, A. M. Casazza, R. A. Firestone, I. Hellström, and K. E. Hellström. 1993. Cure of xenografted human carcinomas by BR96-doxorubicin immunoconjugates. Science 261:212.