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Volumn 33, Issue 17-18, 1996, Pages 1301-1312

Design and expression of a stable bispecific scFv dimer with affinity for both glycoprotein and N9 neuraminidase

Author keywords

antibody fragments; BIAcore(TM); bisFv; bispecific single chain antibody dimer; diabody; glycophorin; neuraminidase; scFv

Indexed keywords

BISPECIFIC ANTIBODY; GLYCOPHORIN; IDIOTYPIC ANTIBODY; IMMUNOGLOBULIN FV FRAGMENT; SIALIDASE; UNCLASSIFIED DRUG;

EID: 0030434862     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0161-5890(96)00097-1     Document Type: Article
Times cited : (34)

References (49)
  • 2
    • 0028094123 scopus 로고
    • Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution
    • Brizzard B. L., Chubet R. G. and Vizard D. L. (1994) Immunoaffinity purification of FLAG epitope-tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution. BioTechniques 16, 730-734.
    • (1994) BioTechniques , vol.16 , pp. 730-734
    • Brizzard, B.L.1    Chubet, R.G.2    Vizard, D.L.3
  • 3
    • 0028672525 scopus 로고
    • Human antibodies from combinatorial libraries
    • Burton D. R. and Barbas C. F. (1994) Human antibodies from combinatorial libraries. Adv. Immun. 57, 191-280.
    • (1994) Adv. Immun. , vol.57 , pp. 191-280
    • Burton, D.R.1    Barbas, C.F.2
  • 5
    • 0022432255 scopus 로고
    • Improved oligonucleotide site directed mutagenesis using M13 vectors
    • Carter P., Bedouelle H. and Winter G. (1985) Improved oligonucleotide site directed mutagenesis using M13 vectors. Nucl. Acids Res. 13, 4431-4443.
    • (1985) Nucl. Acids Res. , vol.13 , pp. 4431-4443
    • Carter, P.1    Bedouelle, H.2    Winter, G.3
  • 6
    • 0029888585 scopus 로고    scopus 로고
    • Construction of recombinant extended single-chain antibody peptide conjugates for use in the diagnosis of HIV1 and HIV2
    • Coia G., Hudson P. J. and Lilley G. G. (1996) Construction of recombinant extended single-chain antibody peptide conjugates for use in the diagnosis of HIV1 and HIV2. J. Immun. Meth. 192, 13-23.
    • (1996) J. Immun. Meth. , vol.192 , pp. 13-23
    • Coia, G.1    Hudson, P.J.2    Lilley, G.G.3
  • 8
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S. C. and Hippel P. H. von (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 9
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilize immunoglobulin Fv fragments
    • Glockshuber R., Malia M., Pfitzinger I. and Plückthun A. (1990) A comparison of strategies to stabilize immunoglobulin Fv fragments. Biochemistry 29, 1362-1367.
    • (1990) Biochemistry , vol.29 , pp. 1362-1367
    • Glockshuber, R.1    Malia, M.2    Pfitzinger, I.3    Plückthun, A.4
  • 10
    • 0028302596 scopus 로고
    • Efficient tumor cell lysis mediated by a bispecific single chain antibody expressed in Escherichia coli
    • Gruber M., Schodin B. A., Wilson E. R. and Kranz D. M. (1994) Efficient tumor cell lysis mediated by a bispecific single chain antibody expressed in Escherichia coli. J. Immun. 152, 5368-5374.
    • (1994) J. Immun. , vol.152 , pp. 5368-5374
    • Gruber, M.1    Schodin, B.A.2    Wilson, E.R.3    Kranz, D.M.4
  • 11
    • 0027365756 scopus 로고
    • Determination of relative binding affinity of influenza virus N9 sialidases with the Fab fragment of monoclonal antibody NC41 using biosensor technology
    • Gruen L. C., Kortt A. A. and Nice E. (1993) Determination of relative binding affinity of influenza virus N9 sialidases with the Fab fragment of monoclonal antibody NC41 using biosensor technology. Eur. J. Biochem. 217, 319-325.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 319-325
    • Gruen, L.C.1    Kortt, A.A.2    Nice, E.3
  • 12
    • 3242793191 scopus 로고
    • Direct clone characterization from plaques and colonies by PCR
    • Gussow D. and Clackson T. (1989) Direct clone characterization from plaques and colonies by PCR. Nucl. Acids Res. 17, 4000.
    • (1989) Nucl. Acids Res. , vol.17 , pp. 4000
    • Gussow, D.1    Clackson, T.2
  • 13
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. (1983) Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166, 557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 14
    • 0027197493 scopus 로고
    • "Diabodies": Small bivalent and bispecific antibody fragments
    • Holliger P., Prospero T. and Winter G. (1993) "Diabodies": small bivalent and bispecific antibody fragments. Proc. natn. Acad. Sci. U.S.A. 90, 6444-6448.
    • (1993) Proc. Natn. Acad. Sci. U.S.A. , vol.90 , pp. 6444-6448
    • Holliger, P.1    Prospero, T.2    Winter, G.3
  • 15
    • 0029932582 scopus 로고    scopus 로고
    • Specific killing of lymphoma cells by cytotoxic T-cells mediated by a bispecific diabody
    • Holliger P., Brissinck J., Williams R. L., Thielemans K. and Winter G. (1996) Specific killing of lymphoma cells by cytotoxic T-cells mediated by a bispecific diabody. Prot. Eng. 9, 299-305.
    • (1996) Prot. Eng. , vol.9 , pp. 299-305
    • Holliger, P.1    Brissinck, J.2    Williams, R.L.3    Thielemans, K.4    Winter, G.5
  • 17
    • 0011178176 scopus 로고
    • Structure and application of single-chain Fvs as diagnostic and therapeutic agents
    • (Edited by Zola H.), BIOS Scientific, Oxford, U.K.
    • Hudson P. (1995) Structure and application of single-chain Fvs as diagnostic and therapeutic agents. In: Monoclonal Antibodies: The Second Generation. (Edited by Zola H.), pp. 183-292. BIOS Scientific, Oxford, U.K.
    • (1995) Monoclonal Antibodies: The Second Generation , pp. 183-292
    • Hudson, P.1
  • 20
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal and antigen-antibody interactions with a new biosensor based analytical system
    • Karlsson R., Michelsson A. and Mattsson L. (1991) Kinetic analysis of monoclonal and antigen-antibody interactions with a new biosensor based analytical system. J. Immun. Meth. 145, 229-240.
    • (1991) J. Immun. Meth. , vol.145 , pp. 229-240
    • Karlsson, R.1    Michelsson, A.2    Mattsson, L.3
  • 23
    • 0028001154 scopus 로고
    • Recombinant single-chain Fv fragments carrying C-terminal cysteine residues: Production of bivalent and biotinylated miniantibodies
    • Kipriyanov S. M., Dübel S., Breitling F., Kontermann R. E. and Little M. (1994) Recombinant single-chain Fv fragments carrying C-terminal cysteine residues: production of bivalent and biotinylated miniantibodies. Mol. Immun. 31, 1047-1058.
    • (1994) Mol. Immun. , vol.31 , pp. 1047-1058
    • Kipriyanov, S.M.1    Dübel, S.2    Breitling, F.3    Kontermann, R.E.4    Little, M.5
  • 24
    • 0028294931 scopus 로고
    • Recombinant antineuraminidase single chain Fv antibody: Characterization, formation of dimer and higher molecular mass multimers and the solution of the crystal structure of the scFv-neuraminidase complex
    • Kortt A. A., Malby R. L., Caldwell J. B., Gruen L. C., Ivancic N., Lawrence M. C., Howlett G. J., Webster R. G., Hudson P. J. and Colman P. M. (1994) Recombinant antineuraminidase single chain Fv antibody: characterization, formation of dimer and higher molecular mass multimers and the solution of the crystal structure of the scFv-neuraminidase complex. Eur. J. Biochem. 221, 151-157.
    • (1994) Eur. J. Biochem. , vol.221 , pp. 151-157
    • Kortt, A.A.1    Malby, R.L.2    Caldwell, J.B.3    Gruen, L.C.4    Ivancic, N.5    Lawrence, M.C.6    Howlett, G.J.7    Webster, R.G.8    Hudson, P.J.9    Colman, P.M.10
  • 25
    • 0029069430 scopus 로고
    • Retargetting of CTL by an efficiently refolded bispecific single chain dimer produced in bacteria
    • Kurucz I., Titus J. A., Jost C. R., Jacobus C. M. and Segal D. M. (1995) Retargetting of CTL by an efficiently refolded bispecific single chain dimer produced in bacteria. J. Immun. 154, 4576-4582.
    • (1995) J. Immun. , vol.154 , pp. 4576-4582
    • Kurucz, I.1    Titus, J.A.2    Jost, C.R.3    Jacobus, C.M.4    Segal, D.M.5
  • 26
    • 0015853344 scopus 로고
    • Maturation of the heads of bacteriophage T4. I. DNA packaging events
    • Laemmli U. and Favre M. (1973) Maturation of the heads of bacteriophage T4. I. DNA packaging events. J. Mol. Biol. 80, 575-599.
    • (1973) J. Mol. Biol. , vol.80 , pp. 575-599
    • Laemmli, U.1    Favre, M.2
  • 27
    • 0028285385 scopus 로고
    • Recombined single chain antibody polypeptide conjugates expressed in E. coli for the rapid diagnosis of HIV
    • Lilley G. G., Dolezal O., Hillyard C. J., Bernard C. and Hudson P. J. (1994) Recombined single chain antibody polypeptide conjugates expressed in E. coli for the rapid diagnosis of HIV. J. Immun. Meth. 211, 211-226.
    • (1994) J. Immun. Meth. , vol.211 , pp. 211-226
    • Lilley, G.G.1    Dolezal, O.2    Hillyard, C.J.3    Bernard, C.4    Hudson, P.J.5
  • 28
    • 0029148633 scopus 로고
    • A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity
    • Mack M., Riethmuller G. and Kufer P. (1995) A small bispecific antibody construct expressed as a functional single-chain molecule with high tumor cell cytotoxicity. Proc. natn. Acad. Sci. U.S.A. 92, 7021-7025.
    • (1995) Proc. Natn. Acad. Sci. U.S.A. , vol.92 , pp. 7021-7025
    • Mack, M.1    Riethmuller, G.2    Kufer, P.3
  • 30
    • 0028774037 scopus 로고
    • The structure of a complex between the NC10 antibody and the influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody
    • Malby R. L., Tulip W. R., Harley V. R., McKimm-Breschin J. L., Laver W. G., Webster R. G. and Colman P. M. (1994) The structure of a complex between the NC10 antibody and the influenza virus neuraminidase and comparison with the overlapping binding site of the NC41 antibody. Structure 2, 733-746.
    • (1994) Structure , vol.2 , pp. 733-746
    • Malby, R.L.1    Tulip, W.R.2    Harley, V.R.3    McKimm-Breschin, J.L.4    Laver, W.G.5    Webster, R.G.6    Colman, P.M.7
  • 31
    • 0028140247 scopus 로고
    • Construction, expression and activity of a bivalent bispecific single chain antibody
    • Mallender W. D. and Voss E. W. (1994) Construction, expression and activity of a bivalent bispecific single chain antibody. J. Biol. Chem. 269, 199-206.
    • (1994) J. Biol. Chem. , vol.269 , pp. 199-206
    • Mallender, W.D.A.1    Voss, E.W.2
  • 34
    • 0028208743 scopus 로고
    • Spontaneous assembly of bivalent single chain antibody fragments in Escherichia coli
    • McGregor D. P., Molloy P. E., Cunningham C. and Harris W. J. (1994) Spontaneous assembly of bivalent single chain antibody fragments in Escherichia coli. Mol. Immun. 31, 219-226.
    • (1994) Mol. Immun. , vol.31 , pp. 219-226
    • McGregor, D.P.1    Molloy, P.E.2    Cunningham, C.3    Harris, W.J.4
  • 36
    • 0025105580 scopus 로고
    • (Edited by Osterhaus A. D. M. E. and Uytdellaag F. G. C. M.), Elsevier B. V.
    • Metzger D. W. and Webster R. G. (1990). In: Idiotype Networks in Biology and Medicine (Edited by Osterhaus A. D. M. E. and Uytdellaag F. G. C. M.), pp. 257-267, Elsevier B. V.
    • (1990) Idiotype Networks in Biology and Medicine , pp. 257-267
    • Metzger, D.W.1    Webster, R.G.2
  • 37
    • 0028945817 scopus 로고
    • High-affinity antigen binding by chelating recombinant antibodies
    • Neri D., Momo M., Prospero T. and Winter G. (1995) High-affinity antigen binding by chelating recombinant antibodies. 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
  • 38
    • 0028949091 scopus 로고
    • Tetravalent minibodies with high avidity assembling in E. coli
    • Pack P., Muller K., Zahn P. and Plückthun A. (1995) Tetravalent minibodies with high avidity assembling in E. coli. J. Mol. Biol. 246, 28-34.
    • (1995) J. Mol. Biol. , vol.246 , pp. 28-34
    • Pack, P.1    Muller, K.2    Zahn, P.3    Plückthun, A.4
  • 39
    • 0028774708 scopus 로고
    • Crystal structure of a diabody, a bivalent antibody fragment
    • Perisic O., Webb P. A., Holliger P., Winter G. and Williams R. L. (1994) Crystal structure of a diabody, a bivalent antibody fragment. Structure 2, 1218-1226.
    • (1994) Structure , vol.2 , pp. 1218-1226
    • Perisic, O.1    Webb, P.A.2    Holliger, P.3    Winter, G.4    Williams, R.L.5
  • 42
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications
    • Towbin H., Staehlin T. and Gordon J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications. Proc. natn. Acad. Sci. U.S.A. 76, 4350-4354.
    • (1979) Proc. Natn. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehlin, T.2    Gordon, J.3
  • 43
    • 0030003654 scopus 로고    scopus 로고
    • Btag: A novel six-residue epitope tag for surveillance and purification of recombinant proteins
    • Wang L.-F., Yu M., White J. R. and Eaton B. T. (1996) Btag: a novel six-residue epitope tag for surveillance and purification of recombinant proteins. Gene 169, 53-58.
    • (1996) Gene , vol.169 , pp. 53-58
    • Wang, L.-F.1    Yu, M.2    White, J.R.3    Eaton, B.T.4
  • 44
    • 0028074723 scopus 로고
    • Multivalent Fvs: Characterisation of single-chain Fv oligomers and preparation of a bispecific Fv
    • Whitlow M., Filpula D., Rollence M. L., Feng S. L. and Woods J. F. (1994) Multivalent Fvs: characterisation of single-chain Fv oligomers and preparation of a bispecific Fv. Prot. Eng. 7, 1017-1026.
    • (1994) Prot. Eng. , vol.7 , pp. 1017-1026
    • Whitlow, M.1    Filpula, D.2    Rollence, M.L.3    Feng, S.L.4    Woods, J.F.5
  • 49


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