Bacterial expression and characterization of recombinant biologically active anti-tyrosine kinase receptor antibody forms

DNA and Cell Biology

Volumn 17, Issue 12, 1998, Pages 1031-1040

  Peterson, Norman C ^a   Greene, Mark I ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; MONOCLONAL ANTIBODY; RECEPTOR ANTIBODY; RECOMBINANT PROTEIN; TYROSINE KINASE RECEPTOR;

ARTICLE; BINDING AFFINITY; CELL LYSATE; DIMERIZATION; GENE OVEREXPRESSION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION;

EID: 0032442577     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/dna.1998.17.1031     Document Type: Article

References (57)

1. BEERLI, R., WELS, W., and HYNES, N. (1994). Autocrine inhibition of the epidermal growth factor receptor by intracellular expression of a single-chain antibody. Biochem. Biophys. Res. Commun. 204, 666-672.
2. BIRD, R., HARDMAN, K.D., JACOBSON, J.W., JOHNSON, S., KAUFMAN, B.M., LEE, S.-M., LEE, T., POPE, S.H., RIORDAN, G.S., and WHITLOW, M. (1988). Single-chain antigen-binding proteins. Science 242, 423-426.
3. BLOTTIERE, H.M., STEPLEWSKI, Z., HERLYN, D., and DOUILLARD, J.Y. (1991). Human anti-murine immunoglobulin responses and immune functions in cancer patients receiving murine monoclonal antibody therapy. Hum. Antibodies Hybridomas 2, 16-25.
4. CABILLY, S. (1989). Growth at sub-optimal temperatures allows the production of functional, antigen-binding Fab fragments in Escherichia coli. Gene 85, 553-557.
5. CARTER, P., PRESTA, L., GORMAN, C.M., RIDGWAY, J.B.B., HENNER, D., WONG, W.L.T., ROWLAND, A.M., KOTTS, C., CARVER, M.E., and SHEPARD, H.M. (1992). Humanization of an anti-p185/HER2 antibody for human cancer therapy. Proc. Natl. Acad. Sci. USA 89, 4285-4289.
6. CHOMCZYNISKI, P., and SACCHI N. (1987). Single step method of RNA isolation by acid guanidinium thiocyanate phenol chloroform extraction. Anal. Biochem. 162, 156-159.
7. COLOMA, M., LARRICK, J., AYALA, M., and GAVILONDO-COWLEY, J. (1991). Primer design for the cloning of immunoglobulin heavy chain leader-variable regions from mouse hybridoma cells using PCR. BioTechniques 11, 152-156.
8. DAVIES, J., and RIECHMANN, L. (1994). Camelising human antibody fragments: NMR studies on VH domains. FEBS Lett. 339, 285-290.
9. DREBIN, J., STERN, D., LINK, V., WEINBERG, R., and GREENE, M. (1984). Monoclonal antibodies identify a cell-surface antigen associated with an activated cellular oncogene. Nature 312, 545-548.
10. DREBIN, J.A., LINK, V.C., and GREENE, M.I. (1988). Monoclonal antibodies specific for the neu oncogene product directly mediate anti-tumor effects in vivo. Oncogene 2, 387-394.
11. DREBIN, J.A., LINK, V.C., STERN, D.F., WEINBERG, R.A., and GREENE, M.I. (1985). Downmodulation of an oncogene protein product and reversion of the transformed phenotype by monoclonal antibodies. Cell 41, 695-706.
12. DREBIN, J.A., LINK, V.C., WEINBERG, R.A., and GREENE, M.I. (1986). Inhibition of tumor growth by a monoclonal antibody reactive with an oncogene-encoded tumor antigen. Proc. Natl. Acad. Sci. USA 83, 9129-9133.
13. FREUND, C., ROSS, A., GUTH, B., PLUCKTHUN, A., and HOLAK, T.A. (1993). Characterization of the linker peptide of the single-chain Fv fragment on antibody by NMR spectroscopy. FEBS Lett. 320, 97-100.
14. GHRAYEB, J., KIMURA, H., JAKAHARA, M., HSIUNG, H., MASUI, Y., and INOUYE, M. (1984). Secretion cloning vectors in Escherichia coli. EMBO J. 3, 2437-2442.
15. GILL, G.N., KAWAMOTO, T., COCHET, C., LE, A., SATO, J.D., MASUI, H., MCLEOD, C., and MENDELSOHN, J. (1984). Monoclonal anti-epidermal growth factor receptor antibodies which are inhibitors of epidermal growth factor binding and antagonists of epidermal growth factor-stimulated tyrosine protein kinase activity. J. Biol. Chem. 259, 7755-7760.
16. GRIFFITHS, A.D., MALMQVIST, M., MARKS, J.D., BYE, J.M., EMBLETON, M.J., MCCAFFERTY, J., BAIER, M., HOLLIGER, K.P., GORICK, B.D., and HUGHES, J.N.C. (1993). Human anti-self antibodies with high specificity from phage display libraries. EMBO J. 12, 725-734.
17. HAKIMI, J., CHIZZONITE, R., and LUKE, D.R. (1991). Reduced immunogenicity and improved pharmacokinetics of humanized anti-tac in Cynamologous monkeys. J. Immunol. 147, 1352-1359.
18. HAMERS-CASTERMAN, C., ATARHOUCH, S., MUYLERMANS, S., ROBINSON, G., HAMERS, C., SONGA, E., BENDAHMAN, N., and HAMERS, R. (1993). Naturally occurring antibodies devoid of light chains. Nature 363, 446-448.
19. HARWERTH, I.-M., WELS, W., MARTE, B.M., HYNES, N.E. (1992). Monoclonal antibodies against the extracellular domain of the erbB-2 receptor function as partial ligand agonists. J. Biol. Chem. 267, 15160-15167.
20. HOOGENBOOM, H.R., VOLCKAERT, G., and RAUS, J.C. (1991). Construction and expression of antibody-tumor necrosis factor fusion proteins. Mol. Immunol. 28, 1027-1037.
21. HUSE, W., and LERNER, R. (1989). Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda. Science 246, 1275-1281.
22. ISAACS, J.D. (1990). The antiglobulin response to therapeutic antibodies. Semin. Immunol. 2, 449-456.
23. JOHNSON, S., and BIRD, R.E. (1991). Construction of single-chain Fv derivatives of monoclonal antibodies and their production in Escherichia coli. Methods Enzymol. 203, 88-98.
24. KABAT, E., WU, T., PERRY, H., GOTTESMAN, K., and FOELLER, C. (1991). Sequences of Proteins of Immunological Interest. U.S. Public Health Service National Institutes of Health, No. 5.
25. KABAT, E.A., and WU, T.T. (1991). Identical V region amino acid sequences and segments of sequences in antibodies of different specificities. J. Immunol. 147, 1709-1719.
26. KNAPPIK, A., and PLUCKTHUN, A. (1995). Engineered turns of a recombinant antibody improve its in vivo folding. Protein Eng. 8, 81-89.
27. KOKAI, Y., MYERS, J.N., WADA, T., BROWN, V.I., LEVEA, C.M., DAVIS, J.G., DOBASHI, K., and GREENE, M.I. (1989). Synergistic interaction of p185c-neu and the EGF receptor leads to transformation of rodent fibroblasts. Cell 58, 287-292.
28. LEDERMANN, J.A., BEGENT, R.H., MASSOF, C., KELLY, A.M., ADAM, T., and BAGSHAWE, K.D. (1991). A Phase-I study of repeated therapy with radiolabeled antibody to carcinoembryonic antigen using intermittent or continuous administration of cyclosporin A to suppress the immune response. Int. J. Cancer 47, 659-664.
29. LEVI, M., SALLBERG, M., RUDEN, U., HERLYN, D., MARUYAMA, H., WIGZELL, H., MARKS, J., and WAHREN, B. (1993). A complementarity-determining region synthetic peptide acts as a miniantibody and neutralizes human-immunodeficiency-virus type-1 in vitro. Proc. Natl. Acad. Sci. USA 90, 4374-4378.
30. LEVY, R., MILLER, R.A. (1983). Biological and clinical implications of lymphocyte hybridomas: tumor therapy with monoclonal antibodies. Ann. Intern. Med. 14, 1352-1359.
31. MARKS, J.D., OUWEHAND, W.H., BYE, J.M., FINNERA, R., GORIK, B.D., VOAK, D., THORPE, S.J., HUGHES-JONE, N.C., and WINTER, G. (1993). Human antibody fragments specific for human blood group antigens from a phage display library. Bio/Technology 11, 1145-1149.
32. MARKS, J., TRISTEN, M., KARPAS, A., and WINTER, G. (1991). Oligonucleotide primers for polymerase chain reaction amplification of human immunoglobulin variable genes and design of family specific oligonucleotide probes. Eur. J. Immunol. 21, 985-991.
33. MCKENZIE, S.J., MARKS, P.J., LAM, T., MORGAN, J., PANICALI, D.L., TRIMPE, K.L., and CARNEY, W.P. (1989). Generation and characterization of monoclonal antibodies specific for the human neu oncogene product, p185. Oncogene 4, 543-548.
34. MURTHY, U., BASU, A., RODECK, U., HERLYN, M., ROSS, A.H., and DAS, M. (1987). Binding of an antagonistic monoclonal antibody to an impact and fragmented EGF-receptor polypeptide. Arch. Biochem. Biophys. 252, 549-560.
35. PACK, P., and PLUCKTHUN, A. (1992). Miniantibodies: use of anphipathic helices to produce functional, flexibility linked dimeric Fv fragments with high avidity in Escherichia coli. Biochemistry 31, 1579-1584.
36. PETERSON, N.C., and GREENE, M.I. (1994). Considerations in the design and production of small anti-receptor antibody forms: optimizing gains while reducing size. Therap. Immunol. 1, 289-295.
37. PLUCKTHUN, A. (1991). Strategies for the expression of antibody fragments in Escherichia coli. Methods: A Companion to Methods in Enzymology 2, 88-96.
38. PLUCKTHUN, A. (1992). Mono-and bivalent antibody fragments produced in Escherichia coli: engineering, folding and antigen binding. Immunol. Rev. 130, 150-188.
39. PLUCKTHUN, A., and SKERRA, A. (1989). Expression of functional antibody Fv and Fab fragments in Escherichia coli. Methods Enzymol. 178, 497-515.
40. REINS, H.-A., STEINHILBER, G., FREIBERG, B., and ANDERER, F.A. (1993). Anti-epidermal growth factor receptor monoclonal antibodies affecting signal transduction. J. Cell. Biochem. 51, 236-248.
41. RIECHMANN, L. (1996). Rearrangement of the former VL interface in the solution structure of a camelised, single antibody VH domain. J. Mol. Biol. 259, 957-969.
42. RODECK, U., WILLIAMS, N., MURTHY, U., and HERLYN, M. (1990). Monoclonal antibody 425 inhibits growth stimulation of carcinoma cells by exogenous EGF and tumor-derived EGF/TGF-α. J. Cell. Biochem. 44, 69-79.
43. SARAGOVI, H.U., GREENE, M.I., CHRUSCIEL, R.A., and KAHN, M. (1992). Loops and secondary structure mimetics: development and applications in basic science and rational drug design. Bio/Technology 10, 773-778.
44. SARAGOVI, H.U., and GREENE, M.I. (1992). Constrained peptides and mimetics as probes of protein secondary structure. Immunol. Methods 1, 1-5.
45. SKERRA, A., PFITZINGER, I., and PLUCKTHUN, A. (1991). The functional expression of antibody Fv fragments in Escherichia coli: improved vectors and a generally applicable purification technique. Bio/Technology 9, 273-278.
46. SUNADA, H., MAGUN, B.E., MENDELSOHN, J., and MACLEOD, C.L. (1986). Monoclonal antibody against epidermal growth factor receptor is internalized with stimulating receptor phosphorylation. Proc. Natl. Acad. Sci. USA 83, 3825-3829.
47. TAUB, R., and GREENE, M.I. (1992). Functional validation of ligand mimicry by anti-receptor antibodies: structural and therapeutic implications. Biochemistry 31, 7431-7435.
48. TERSKIKH, A., LE DOUSSAL, J., CRAMERI, R., FISCH, I., MACH, J., and KAJAVA, A. (1997). Peptabody: a new type of high avidity binding protein. Proc. Natl. Acad. Sci. USA 94, 1663-1668.
49. WADA, T., MYERS, J.N., KOKAI, Y., BROWN, V.I., HAMURO, J., LEVEA, C.M., and GREENE, M.I. (1990). Anti-receptor antibodies reverse the phenotype of cells transformed by two interacting protooncogenic encoded receptor proteins. Oncogene 4, 489-494.
50. WEINER, L.M., HARVEY, E., PADAVIC, S.K., WILLSON, J.K., WALSH, C., LACRETA, F., KHAZAELI, M.B., KIRKWOOD, J.M., and HALLER, D.G. (1993). Phase II multicenter evaluation of prolonged murine monoclonal antibody 17-1A therapy in pancreatic carcinoma. J. Immunother. 13, 110-116.
51. WELS, W., HARWERTH, I., ZWICKL, M., HARDMAN, N., GRONER, B., and HYNES, N. (1992a). Construction, bacterial expression and characterization of a bifunctional single-chain antibody-phosphatase fusion protein targeted to the human ErbB-2 receptor. Bio/Technology 10, 1128-1132.
52. WELS, W., HARWERTH, I.M., MUELLER, M., GRONER, B., and HYNES, N.E. (1992b). Selective inhibition of tumor cell growth by a recombinant single-chain antibody-toxin specific for the erbB-2 receptor. Cancer Res. 52, 6310-6317.
53. WHITLOW, M., and FILPULA, D. (1991). Single-chain Fv proteins and their fusion proteins. Methods: A Companion to Methods in Enzymology 2, 97-105.
54. WILLIAMS, W.V., KIEBER-EMMONS, T., VONFELDT, J., GREENE, M.I., and WEINER, D.B. (1991). Design of bioactive peptides based on antibody hypervariable region structures. J. Biol. Chem. 266, 5182-5190.
55. WILLIAMS, W.V., WEINER, D.B., COHEN, J.C., and GREENE, M.I. (1989). Development and use of receptor binding peptides derived from anti-receptor antibodies. Bio/Technology 7, 471-475.
56. WILSON, I.A., and STANFIELD, R.L. (1993). Antibody-antigen interactions. Curr. Opin. Struct. Biol. 3, 113-118.
57. YON, J., and FRIED, M. (1989). Precise gene fusion by PCR. Nucleic Acids Res. 17, 4895.