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Volumn 255, Issue 1, 1996, Pages 86-97

Coupling protein design and in vitro selection strategies: Improving specificity and affinity of a designed β-protein IL-6 antagonist

Author keywords

Affinity selection; Hypervariable regions; Interleukin 6 antagonist; Phage display; Protein engineering

Indexed keywords

INTERLEUKIN 6;

EID: 0029994999     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0008     Document Type: Article
Times cited : (47)

References (54)
  • 2
    • 0028348564 scopus 로고
    • In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross reactivity
    • 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.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3809-3813
    • Barbas C.F. III1    Hu, D.2    Dunlop, N.3    Sawyer, L.4    Cababa, D.5    Hendry, R.M.6    Nara, P.L.7    Burton, D.R.8
  • 3
    • 0028197603 scopus 로고
    • High level expression and rational mutagenesis of a designed protein, the minibody: From an insoluble to a soluble molecule
    • Bianchi, E., Venturini, S., Pessi, A., Tramontano, A. & Sollazzo, M. (1994). High level expression and rational mutagenesis of a designed protein, the minibody: from an insoluble to a soluble molecule. J. Mol. Biol. 236, 649-659.
    • (1994) J. Mol. Biol. , vol.236 , pp. 649-659
    • Bianchi, E.1    Venturini, S.2    Pessi, A.3    Tramontano, A.4    Sollazzo, M.5
  • 7
    • 0029616481 scopus 로고
    • Monovalent phage display of human interleukin (hIL)-6: Selection of superbinder variants from a complex molecular repertoire in the hIL-6 D-helix
    • in the press
    • Cabibbo, A., Sporeno, E., Toniatti, C., Altamura, S., Savino, R., Paonessa, G. & Ciliberto, G. (1995). Monovalent phage display of human interleukin (hIL)-6: selection of superbinder variants from a complex molecular repertoire in the hIL-6 D-helix. Gene, in the press.
    • (1995) Gene
    • Cabibbo, A.1    Sporeno, E.2    Toniatti, C.3    Altamura, S.4    Savino, R.5    Paonessa, G.6    Ciliberto, G.7
  • 8
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson, M. (1987). Ribbon models of macromolecules. J. Mol. Graph. 5, 103-106.
    • (1987) J. Mol. Graph. , vol.5 , pp. 103-106
    • Carson, M.1
  • 9
    • 0029148418 scopus 로고
    • Random mutagenesis of two complementarity determining region amino acids yields an unexpectedly high frequency of antibodies with increased affinity for both cognate antigen and autoantigen
    • Casson, L. P. & Manser, T. (1995). Random mutagenesis of two complementarity determining region amino acids yields an unexpectedly high frequency of antibodies with increased affinity for both cognate antigen and autoantigen. J. Expt. Med. 182, 743-750.
    • (1995) J. Expt. Med. , vol.182 , pp. 743-750
    • Casson, L.P.1    Manser, T.2
  • 14
    • 0028100458 scopus 로고
    • Kunitz domain inhibitor of tissue-factor VIIa
    • Dennis, M. S. & Lazarus, R. A. (1994). Kunitz domain inhibitor of tissue-factor VIIa. J. Biol. Chem. 269, 22137-22144.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22137-22144
    • Dennis, M.S.1    Lazarus, R.A.2
  • 15
    • 0028926814 scopus 로고
    • Selection and application of human single chain Fv antibody fragments from a semi-synthetic phage antibody display library with designed CDR3 regions
    • de Kruif, J., Boel, E. & Logtenberg, T. (1995). 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. 248, 97-105.
    • (1995) J. Mol. Biol. , vol.248 , pp. 97-105
    • De Kruif, J.1    Boel, E.2    Logtenberg, T.3
  • 16
    • 0028831142 scopus 로고
    • Neutralizing recombinant human antibodies to a conformational V2- and CD4-binding site-sensitive epitope of HIV-1 gp120 isolated by using an epitope-masking procedure
    • Ditzel, H. J., Binley J. M., Moore, J. P., Sodroski, J., Sullivan, N., Sawyer, L. S. W., Hendry R. M., Yang, W. P., Barbas, C. F. III & Burton, D. R. (1995). Neutralizing recombinant human antibodies to a conformational V2- and CD4-binding site-sensitive epitope of HIV-1 gp120 isolated by using an epitope-masking procedure. J. Immunol. 154, 893-906.
    • (1995) J. Immunol. , vol.154 , pp. 893-906
    • Ditzel, H.J.1    Binley, J.M.2    Moore, J.P.3    Sodroski, J.4    Sullivan, N.5    Sawyer, L.S.W.6    Hendry, R.M.7    Yang, W.P.8    Barbas C.F. III9    Burton, D.R.10
  • 17
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • 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.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 19
    • 0027082901 scopus 로고
    • Antibody engineering by codon-based mutagenesis in a filamentous phage vector system
    • Glaser, S. M., Yelton, D. E. & Huse, W. D. (1992). Antibody engineering by codon-based mutagenesis in a filamentous phage vector system. J. Immunol. 149, 3903-3913.
    • (1992) J. Immunol. , vol.149 , pp. 3903-3913
    • Glaser, S.M.1    Yelton, D.E.2    Huse, W.D.3
  • 20
    • 0026535931 scopus 로고
    • In vitro selection and affinity maturation of antibodies from a naive combinatorial immunoglobulin library
    • Gram, H., Marconi, L.-A., Barbas, C. F. III, Collet, T. A., Lerner, R. A. & Kang, A. S. (1992). In vitro selection and affinity maturation of antibodies from a naive combinatorial immunoglobulin library. Proc. Natl Acad. Sci. USA, 89, 3576-3580.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3576-3580
    • Gram, H.1    Marconi, L.-A.2    Barbas C.F. III3    Collet, T.A.4    Lerner, R.A.5    Kang, A.S.6
  • 23
    • 0024357799 scopus 로고
    • A simple method for site-directed mutagenesis using the polymerase chain reaction
    • Hemsley A., Arnheim, N., Toney M. D., Cortopassi, G. & Galas, D. J. (1989). A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucl. Acids Res. 17, 6545-6551.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 6545-6551
    • Hemsley, A.1    Arnheim, N.2    Toney, M.D.3    Cortopassi, G.4    Galas, D.J.5
  • 24
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom, H. R., Griffiths, A. D., Johnson, K. S., Chiswell, D. J., Hudson, P. & 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.
    • (1991) Nucl. Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 25
    • 0028117163 scopus 로고
    • Cytokine signal transduction
    • Kishimoto, T., Taga, T. & Akira, S. (1994). Cytokine signal transduction. Cell, 76, 253-262.
    • (1994) Cell , vol.76 , pp. 253-262
    • Kishimoto, T.1    Taga, T.2    Akira, S.3
  • 26
    • 0029033034 scopus 로고
    • Alternate protein frameworks for molecular recognition
    • Ku, J. & Schultz, P. G. (1995). Alternate protein frameworks for molecular recognition. Proc. Natl Acad. Sci. USA, 92, 6552-6556.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6552-6556
    • Ku, J.1    Schultz, P.G.2
  • 27
    • 0026769413 scopus 로고
    • Identification of a receptor binding site in the carboxyl terminus of human interleukin 6
    • Leebeek, F. W. G., Kariya, K., Schwabe, M. & Fowlkes, D. (1992). Identification of a receptor binding site in the carboxyl terminus of human interleukin 6. J. Biol. Chem. 267, 14832-14838.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14832-14838
    • Leebeek, F.W.G.1    Kariya, K.2    Schwabe, M.3    Fowlkes, D.4
  • 28
    • 0026343486 scopus 로고
    • Selecting high-affinity binding proteins by monovalent phage display
    • 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.
    • (1991) Biochemistry , vol.30 , pp. 10832-10838
    • Lowman, H.B.1    Bass, S.H.2    Simpson, N.3    Wells, J.A.4
  • 29
  • 31
    • 0029120867 scopus 로고
    • Tendamistat as a scaffold for conformationally constrained phage peptide libraries
    • McConnell, S. J. & Hoess, R. H. (1995). Tendamistat as a scaffold for conformationally constrained phage peptide libraries. J. Mol. Biol. 250, 460-470.
    • (1995) J. Mol. Biol. , vol.250 , pp. 460-470
    • McConnell, S.J.1    Hoess, R.H.2
  • 33
    • 0028915369 scopus 로고
    • Four-helix bundle growth factors and their receptors: Protein-protein interactions
    • Mott, H. R. & Campbell, I. D. (1995). Four-helix bundle growth factors and their receptors: protein-protein interactions. Curr. Opin. Struct. Biol. 5, 114-121.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 114-121
    • Mott, H.R.1    Campbell, I.D.2
  • 34
    • 0028168145 scopus 로고
    • Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
    • Muyldermans, S., Atarhouch, T., Saldanha, J., Barbosa, J. A. R. G. & Hamers, R. (1994). Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 7, 1129-1135.
    • (1994) Protein Eng. , vol.7 , pp. 1129-1135
    • Muyldermans, S.1    Atarhouch, T.2    Saldanha, J.3    Barbosa, J.A.R.G.4    Hamers, R.5
  • 35
    • 0028945817 scopus 로고
    • High affinity antigen binding by chelating recombinant antibodies (CRAbs)
    • Neri, D., Momo, M., Prospero, T. & Winter, G. (1995). High affinity antigen binding by chelating recombinant antibodies (CRAbs). J. Mol. Biol. 246, 367-373.
    • (1995) J. Mol. Biol. , vol.246 , pp. 367-373
    • Neri, D.1    Momo, M.2    Prospero, T.3    Winter, G.4
  • 36
    • 0028157937 scopus 로고
    • Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: A critique of the surface plasmon resonance literature
    • O'Shannessy D. J. (1994). Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature. Curr. Opin. Biotechnol. 5, 65-71.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 65-71
    • O'Shannessy, D.J.1
  • 40
    • 0026568164 scopus 로고
    • Directed evolution of a protein: Selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage
    • Roberts, B. L., Markland, W., Ley, A. C., Kent, R. B., White, D. W., Guterman, S. K. & Ladner, R. C. (1992). Directed evolution of a protein: selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage. Proc. Natl Acad. Sci. USA, 89, 2429-2433.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2429-2433
    • Roberts, B.L.1    Markland, W.2    Ley, A.C.3    Kent, R.B.4    White, D.W.5    Guterman, S.K.6    Ladner, R.C.7
  • 41
    • 0029005234 scopus 로고
    • CNTF variants with increased biological potency and receptor selectivity define a functional site of receptor interaction
    • Saggio, I., Cloaguen, I., Poiana, G. & Laufer, R. (1995). CNTF variants with increased biological potency and receptor selectivity define a functional site of receptor interaction. EMBO J. 14, 3045-3054.
    • (1995) EMBO J. , vol.14 , pp. 3045-3054
    • Saggio, I.1    Cloaguen, I.2    Poiana, G.3    Laufer, R.4
  • 42
    • 0028274976 scopus 로고
    • Design of protein structures: Helix bundles and beyond
    • Sander, C. (1994). Design of protein structures: helix bundles and beyond. Trends Biotechnol. 12, 163-167.
    • (1994) Trends Biotechnol. , vol.12 , pp. 163-167
    • Sander, C.1
  • 43
    • 0027252635 scopus 로고
    • Saturation mutagenesis of the human interleukin-6 receptor-binding site: Implications for its three-dimensional structure
    • Savino, R., Lahm, A., Giorgio, M., Cabibbo, A., Tramontano, A. & Ciliberto, G. (1993). Saturation mutagenesis of the human interleukin-6 receptor-binding site: implications for its three-dimensional structure. Proc. Natl Acad. Sci. USA, 90, 4067-4071.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4067-4071
    • Savino, R.1    Lahm, A.2    Giorgio, M.3    Cabibbo, A.4    Tramontano, A.5    Ciliberto, G.6
  • 45
    • 0029105369 scopus 로고
    • From protein engineering to drug design: Imitating how antibodies do it
    • Sollazzo, M. (1995). From protein engineering to drug design: imitating how antibodies do it. Immunologist, 3, 5-11.
    • (1995) Immunologist , vol.3 , pp. 5-11
    • Sollazzo, M.1
  • 46
    • 0028301594 scopus 로고
    • Oncostatin M binds directly to gp130 and behaves as interleukin-6 antagonist on a cell line expressing gp130 but lacking functional oncostatin M receptors
    • Sporeno, E., Paonessa, G., Salvati, A. L., Graziani, R., Delmastro, P., Ciliberto, G. & Toniatti, C. (1994). Oncostatin M binds directly to gp130 and behaves as interleukin-6 antagonist on a cell line expressing gp130 but lacking functional oncostatin M receptors. J. Biol. Chem. 269, 10991-10995.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10991-10995
    • Sporeno, E.1    Paonessa, G.2    Salvati, A.L.3    Graziani, R.4    Delmastro, P.5    Ciliberto, G.6    Toniatti, C.7
  • 47
    • 0029001752 scopus 로고
    • Searching sequence space
    • Stemmer, W. P. C. (1995). Searching sequence space. Bio/Technology, 13, 549-553.
    • (1995) Bio/Technology , vol.13 , pp. 549-553
    • Stemmer, W.P.C.1
  • 48
    • 0028385766 scopus 로고
    • The making of the minibody: An engineered β-protein for the display of conformationally-constrained peptides
    • Tramontano, A., Bianchi, E., Venturini, S., Martin, F., Pessi, A. & Sollazzo, M. (1994). The making of the minibody: an engineered β-protein for the display of conformationally-constrained peptides. J. Mol. Recogn. 7, 9-24.
    • (1994) J. Mol. Recogn. , vol.7 , pp. 9-24
    • Tramontano, A.1    Bianchi, E.2    Venturini, S.3    Martin, F.4    Pessi, A.5    Sollazzo, M.6
  • 49
    • 0029060153 scopus 로고
    • Codominance and toxins: A path to drugs of nearly unlimited selectivity
    • Varshavsky, A. (1995). Codominance and toxins: A path to drugs of nearly unlimited selectivity. Proc. Natl Acad. Sci. USA, 92, 3663-3667.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3663-3667
    • Varshavsky, A.1
  • 50
    • 0027948727 scopus 로고
    • Phage display of the minibody: A β-scaffold for the selection of conformationally-constrained peptides
    • Venturini S., Martin, F. & Sollazzo, M. (1994). Phage display of the minibody: a β-scaffold for the selection of conformationally-constrained peptides. Protein Pept. Letters, 1, 70-75.
    • (1994) Protein Pept. Letters , vol.1 , pp. 70-75
    • Venturini, S.1    Martin, F.2    Sollazzo, M.3
  • 51
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • Ward, S. E., Güssow, D., Griffiths, A. D., Jones, P. T. & Winter, G. (1989). Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature, 341, 544-546.
    • (1989) Nature , vol.341 , pp. 544-546
    • Ward, S.E.1    Güssow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 52
    • 0026905448 scopus 로고
    • Rapid evolution of peptide and protein binding in vitro
    • Wells, J. A. & Lowman, H. B. (1992). Rapid evolution of peptide and protein binding in vitro. Curr. Opin. Biotechnol. 3, 355-362.
    • (1992) Curr. Opin. Biotechnol. , vol.3 , pp. 355-362
    • Wells, J.A.1    Lowman, H.B.2
  • 53
    • 0028606741 scopus 로고
    • Antibody-antigen interactions: New structures and new conformational changes
    • Wilson, I. A. & Stanfield, R. L. (1994). Antibody-antigen interactions: new structures and new conformational changes. Curr. Opin. Struct. Biol. 4, 857-867.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 857-867
    • Wilson, I.A.1    Stanfield, R.L.2


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