메뉴 건너뛰기




Volumn 9, Issue 1, 1996, Pages 39-51

Comparative interaction kinetics of two recombinant Fabs and of the corresponding antibodies directed to the coat protein of tobacco mosaic virus

Author keywords

BIAcore ; Cloning strategy; Filter screening; Kinetic rate constants; Peptide antibody interaction; Recombinant Fab; Tobacco mosaic virus protein

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; PEPTIDE FRAGMENT; PRIMER DNA; RECOMBINANT PROTEIN; VIRUS ANTIBODY;

EID: 0029717697     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1352(199601)9:1<39::AID-JMR239>3.0.CO;2-V     Document Type: Article
Times cited : (35)

References (50)
  • 1
    • 0001424318 scopus 로고
    • A major part of the polypeptide chain of tobacco mosaic virus protein is antigenic
    • Al Moudallal, Z., Briand, J.-P. and Van Regenmortel, M. H. V. (1985). A major part of the polypeptide chain of tobacco mosaic virus protein is antigenic. EMBO J. 4, 1231-1235.
    • (1985) EMBO J. , vol.4 , pp. 1231-1235
    • Al Moudallal, Z.1    Briand, J.-P.2    Van Regenmortel, M.H.V.3
  • 2
    • 0027894195 scopus 로고
    • Production and characterization of monoclonal antibodies recognizing defined regions of the human oestrogen receptor
    • Ali, S., Lutz, Y, Bellocq, J.-P., Chenard-Neu, M.-P., Rouyer, N. and Metzger, D. (1993). Production and characterization of monoclonal antibodies recognizing defined regions of the human oestrogen receptor. Hybridoma 12, 391-405.
    • (1993) Hybridoma , vol.12 , pp. 391-405
    • Ali, S.1    Lutz, Y.2    Bellocq, J.-P.3    Chenard-Neu, M.-P.4    Rouyer, N.5    Metzger, D.6
  • 4
    • 0026645486 scopus 로고
    • Determination of kinetic constants for the interaction between a monoclonal antibody and peptides using surface plasmon resonance
    • Altschuh, D., Dubs, M.-C., Weiss, E., Zeder-Lutz, G. and Van Regenmortel, M. H. V. (1992). Determination of kinetic constants for the interaction between a monoclonal antibody and peptides using surface plasmon resonance. Biochemistry 31, 6298-6304.
    • (1992) Biochemistry , vol.31 , pp. 6298-6304
    • Altschuh, D.1    Dubs, M.-C.2    Weiss, E.3    Zeder-Lutz, G.4    Van Regenmortel, M.H.V.5
  • 5
    • 0014440127 scopus 로고
    • The cross-linking of proteins with glutaraldehyde and its use for the preparation of immunoadsorbents
    • Avraméas, S. and Ternynck, T. (1969). The cross-linking of proteins with glutaraldehyde and its use for the preparation of immunoadsorbents. Immunochemistry 6, 53-66.
    • (1969) Immunochemistry , vol.6 , pp. 53-66
    • Avraméas, S.1    Ternynck, T.2
  • 6
    • 0025733795 scopus 로고
    • Measurement of affinity of viral monoclonal antibodies by ELISA titration of free antibody in equilibrium mixtures
    • Azimzadeh, A. and Van Regenmortel, M. H.V. (1991). Measurement of affinity of viral monoclonal antibodies by ELISA titration of free antibody in equilibrium mixtures. J. Immunol. Methods 141, 199-208.
    • (1991) J. Immunol. Methods , vol.141 , pp. 199-208
    • Azimzadeh, A.1    Van Regenmortel, M.H.V.2
  • 7
    • 44949280863 scopus 로고
    • Combinatorial immunoglobulin libraries on the surface of phage (Phabs): Rapid selection of antigen-specific Fabs
    • Barbas III, C. F. and Lerner, R. A. (1991). Combinatorial immunoglobulin libraries on the surface of phage (Phabs): rapid selection of antigen-specific Fabs. Methods: Companion Methods Enzymol. 2, 119-124.
    • (1991) Methods: Companion Methods Enzymol. , vol.2 , pp. 119-124
    • Barbas III, C.F.A.1    Lerner, R.A.2
  • 8
    • 0023922661 scopus 로고
    • Escherichia coli secretion of an active chimeric antibody fragment
    • Better, M., Chang, C. P., Robinson, R. R. and Horwitz, A. H. (1988). Escherichia coli secretion of an active chimeric antibody fragment. Science 240, 1041-1043.
    • (1988) Science , vol.240 , pp. 1041-1043
    • Better, M.1    Chang, C.P.2    Robinson, R.R.3    Horwitz, A.H.4
  • 9
    • 0026664254 scopus 로고
    • Kinetic analysis of recombinant antibody-antigen interactions: Relation between structural domains and antigen binding
    • Borrebaeck, C. A. K., Malmborg, A. C., Furebring, C., Michaelsson, A., Ward, S., Danielsson, L. and Ohlin, M. (1992). Kinetic analysis of recombinant antibody-antigen interactions: relation between structural domains and antigen binding. Bio/Technology 10, 697-698.
    • (1992) Bio/Technology , vol.10 , pp. 697-698
    • Borrebaeck, C.A.K.1    Malmborg, A.C.2    Furebring, C.3    Michaelsson, A.4    Ward, S.5    Danielsson, L.6    Ohlin, M.7
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitatiort of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitatiort of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 0021813905 scopus 로고
    • Synthetic peptides as antigens: Pitfalls of conjugation methods
    • Briand, J.-P., Muller, S. and Van Regenmortel M. H. V. (1985). Synthetic peptides as antigens: pitfalls of conjugation methods. J. Immunol. Methods 78, 59-69.
    • (1985) J. Immunol. Methods , vol.78 , pp. 59-69
    • Briand, J.-P.1    Muller, S.2    Van Regenmortel, M.H.V.3
  • 12
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock, W. O., Fernandez, J. M. and Short, J. M. (1987). XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. Bio Techniques 5, 376-378.
    • (1987) Bio Techniques , vol.5 , pp. 376-378
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 14
    • 0022339938 scopus 로고
    • Domain association in immunoglobulin molecules. the packing of variable domains
    • Chothia, C., Novotny, J., Bruccoleri, R. and Karplus, M. (1985). Domain association in immunoglobulin molecules. The packing of variable domains. J. Mol. Biol. 186, 651-663.
    • (1985) J. Mol. Biol. , vol.186 , pp. 651-663
    • Chothia, C.1    Novotny, J.2    Bruccoleri, R.3    Karplus, M.4
  • 15
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia, C. and Lesk, A. M. (1987). Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196, 901-917.
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 17
    • 0023484601 scopus 로고
    • Immunochemical studies of tobacco mosaic virus-VII. Use of comparative surface accessibility of residues in antigenically related viruses for delineating epitopes recognized by monoclonal antibodies
    • Dore, I., Aitschuh, D., Al Moudallal, Z. and Van Regenmortel, M. H. V. (1987). Immunochemical studies of tobacco mosaic virus-VII. Use of comparative surface accessibility of residues in antigenically related viruses for delineating epitopes recognized by monoclonal antibodies. Mol. Immunol. 24, 1351-1358.
    • (1987) Mol. Immunol. , vol.24 , pp. 1351-1358
    • Dore, I.1    Aitschuh, D.2    Al Moudallal, Z.3    Van Regenmortel, M.H.V.4
  • 18
    • 0025825576 scopus 로고
    • Colony assays for antibody fragments expressed in bacteria
    • Dreher, M. L., Gherardi, E., Skerra, A. and Milstein, C. (1991). Colony assays for antibody fragments expressed in bacteria. J. Immunol. Methods 139, 197-205.
    • (1991) J. Immunol. Methods , vol.139 , pp. 197-205
    • Dreher, M.L.1    Gherardi, E.2    Skerra, A.3    Milstein, C.4
  • 19
    • 0027411585 scopus 로고
    • SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange
    • Felder, S., Zhou, M., Hu, P., Urena, J., Ullrich, A., Chaudhuri, M., White, M., Shoelson, S. E. and Schlessinger, J. (1993). SH2 domains exhibit high-affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell. Biol. 13, 1449-1455.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1449-1455
    • Felder, S.1    Zhou, M.2    Hu, P.3    Urena, J.4    Ullrich, A.5    Chaudhuri, M.6    White, M.7    Shoelson, S.E.8    Schlessinger, J.9
  • 20
    • 0001953670 scopus 로고
    • Degradation of tobacco mosaic virus with acetic acid
    • Fraenkel-Conrat, H. (1957). Degradation of tobacco mosaic virus with acetic acid. Virology 4, 1-4.
    • (1957) Virology , vol.4 , pp. 1-4
    • Fraenkel-Conrat, H.1
  • 21
    • 0027198367 scopus 로고
    • Antigen-antibody binding and mass transport by convection and diffusion to a surface: A two-dimensional computer model of binding and dissociation kinetics
    • 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, 152-161.
    • (1993) Anal. Biochem. , vol.213 , pp. 152-161
    • Glaser, R.W.1
  • 23
    • 0024329804 scopus 로고
    • Three-dimensional structure of a fluorescein-Fab complex crystallized in 2-methyl-2,4-pentanediol
    • Herron, J. N., He, X. M., Mason, M. L., Voss, E. W., Jr. and Edmundson, A. B. (1989). Three-dimensional structure of a fluorescein-Fab complex crystallized in 2-methyl-2,4-pentanediol. Proteins 5, 271-280.
    • (1989) Proteins , vol.5 , pp. 271-280
    • Herron, J.N.1    He, X.M.2    Mason, M.L.3    Voss Jr., E.W.4    Edmundson, A.B.5
  • 24
    • 0028556362 scopus 로고
    • Comparison of crystal structures of two homologous proteins: structural origin of altered domain interactions in immunoglobulin light-chain dimers
    • Huang, D.-B., Chang, C.-H., Ainsworth, C., Brünger, A. T., Eulitz, M., Solomon, A., Stevens, F. J. and Schiffer, M. (1994). Comparison of crystal structures of two homologous proteins: structural origin of altered domain interactions in immunoglobulin light-chain dimers. Biochemistry 33, 14848-14857.
    • (1994) Biochemistry , vol.33 , pp. 14848-14857
    • Huang, D.-B.1    Chang, C.-H.2    Ainsworth, C.3    Brünger, A.T.4    Eulitz, M.5    Solomon, A.6    Stevens, F.J.7    Schiffer, M.8
  • 26
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • Johnsson, B., Löfas, S. and Lindqvist, G. (1991). Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors. Anal. Biochem. 198, 268-277.
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Löfas, S.2    Lindqvist, G.3
  • 28
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson, R., Michaelsson, A. and Mattsson, L. (1991). Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods 145, 229-240.
    • (1991) J. Immunol. Methods , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3
  • 29
    • 0000771742 scopus 로고
    • Measurement of antibody affinity
    • ed. by M. H. V. Van Regenmortel, CRC Press, Boca Raton, FL
    • Karlsson, R., Altschuh, D. and Van Regenmortel, M. H. V. (1992). Measurement of antibody affinity. In Structure of Antigens I, ed. by M. H. V. Van Regenmortel, pp. 127-148. CRC Press, Boca Raton, FL.
    • (1992) Structure of Antigens I , pp. 127-148
    • Karlsson, R.1    Altschuh, D.2    Van Regenmortel, M.H.V.3
  • 31
    • 0000439564 scopus 로고
    • Thermodynamics of protein-protein interaction studied by using BIAcore and single-site mutagenesis
    • Kelley, R. F. (1994). Thermodynamics of protein-protein interaction studied by using BIAcore and single-site mutagenesis. Methods: Companion Methods Enzymol. 6, 111-120.
    • (1994) Methods: Companion Methods Enzymol. , vol.6 , pp. 111-120
    • Kelley, R.F.1
  • 32
    • 0027526906 scopus 로고
    • The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in Escherichia coli.
    • Knappik, A., Krebber, C. and Pluïckthun, A. (1993). The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in Escherichia coli. Bio/Technology 11, 77-83.
    • (1993) Bio/Technology , vol.11 , pp. 77-83
    • Knappik, A.1    Krebber, C.2    Pluïckthun, A.3
  • 33
    • 0026244229 scopus 로고
    • MOLSCRIPT. a program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT. a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
    • (1991) J. Appl. Cryst. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0027286137 scopus 로고
    • Surface plasmon resonance for detection and measurement of antibody-antigen affinity and kinetics
    • Maimqvist, M. (1993). Surface plasmon resonance for detection and measurement of antibody-antigen affinity and kinetics. Curr. Opin. Immunol. 5, 282-286.
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 282-286
    • Maimqvist, M.1
  • 36
    • 0028360038 scopus 로고
    • Effect of HIV-1 peptide presentaion on the affinity constants of two monoclonal antibodies determined by BIAcore™ technology
    • Mani, J.-C., Marchi, V. and Cucurou, C. (1994). Effect of HIV-1 peptide presentaion on the affinity constants of two monoclonal antibodies determined by BIAcore™ technology. Mol. Immunol. 31, 439-444.
    • (1994) Mol. Immunol. , vol.31 , pp. 439-444
    • Mani, J.-C.1    Marchi, V.2    Cucurou, C.3
  • 37
    • 0022343664 scopus 로고
    • Structural invariants of antigen binding: Comparison of immunoglobulin VL-VH and VL-VL domain dimers
    • Novotny, J. and Haber, E. (1985). Structural invariants of antigen binding: comparison of immunoglobulin VL-VH and VL-VL domain dimers. Proc. Natl Acad. Sci. USA 82, 4592-4596.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 4592-4596
    • Novotny, J.1    Haber, E.2
  • 38
    • 0027359747 scopus 로고
    • Bacterially expressed Fabs of monclonal antibodies neutralizing tumour necrosis factor alpha in vitro retain full binding and biological activity
    • Orfanoudakis, G., Karim, B., Bourel, D. and Weiss, E. (1993). Bacterially expressed Fabs of monclonal antibodies neutralizing tumour necrosis factor alpha in vitro retain full binding and biological activity. Mol. Immunol. 30, 1519-1528.
    • (1993) Mol. Immunol. , vol.30 , pp. 1519-1528
    • Orfanoudakis, G.1    Karim, B.2    Bourel, D.3    Weiss, E.4
  • 39
    • 1542698957 scopus 로고
    • Cloning immunoglobulin variable domains for expression by the polymerase chain reaction
    • Orlandi, R., Güssow, D. H., Jones, P. T. and Winter, G. (1989). Cloning immunoglobulin variable domains for expression by the polymerase chain reaction. Proc. Natl Acad. Sci. USA 86, 3833-3837.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 3833-3837
    • Orlandi, R.1    Güssow, D.H.2    Jones, P.T.3    Winter, G.4
  • 40
    • 0026675126 scopus 로고
    • Immobilization chemistries suitable for use in the BIAcore surface plasmon resonance detector
    • O'Shannessy, D. J., Brigham-Burke, M. and Peck. K. (1992). Immobilization chemistries suitable for use in the BIAcore surface plasmon resonance detector., Anal. Biochem. 205, 132-136.
    • (1992) Anal. Biochem. , vol.205 , pp. 132-136
    • O'Shannessy, D.J.1    Brigham-Burke, M.2    Peck, K.3
  • 41
    • 0027293351 scopus 로고
    • Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: Use of nonlinear least squares analysis methods
    • O'Shannessy, D. J., Brigham-Burke, M., Soneson, K. K., Hensley, P. and Brooks, I. (1993). Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods. Anal. Biochem. 212, 457-468.
    • (1993) Anal. Biochem. , vol.212 , pp. 457-468
    • O'Shannessy, D.J.1    Brigham-Burke, M.2    Soneson, K.K.3    Hensley, P.4    Brooks, I.5
  • 42
    • 77957060270 scopus 로고
    • Improved vectors for plant transformation: Expression cassette vectors and new selectable markers
    • Rogers, S. G., Klee, H. J., Horsch, R. B. and Fraley, R. T. (1987). Improved vectors for plant transformation: expression cassette vectors and new selectable markers. Methods Enzymol. 153, 253-277.
    • (1987) Methods Enzymol. , vol.153 , pp. 253-277
    • Rogers, S.G.1    Klee, H.J.2    Horsch, R.B.3    Fraley, R.T.4
  • 44
    • 0026500080 scopus 로고
    • In vitro activity of the transciption activation functions of the progesterone receptor. Evidence for intermediary factors
    • Shemshedini, L., Ji, J., Brou, C., Chambon, P. and Gronemeyer, H. (1992). In vitro activity of the transciption activation functions of the progesterone receptor. Evidence for intermediary factors. J. Biol. Chem. 267, 1834-1839.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1834-1839
    • Shemshedini, L.1    Ji, J.2    Brou, C.3    Chambon, P.4    Gronemeyer, H.5
  • 46
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
    • Skerra, A. and Plückthun, A. (1988). Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science 240, 1038-1041.
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Plückthun, A.2
  • 47
    • 0025783791 scopus 로고
    • Filter screening of antibody Fab fragments secreted from individual bacterial colonies: Specific detection of antigen binding with a two-membrane system
    • Skerra, A., Dreher, M. L. and Winter, G. (1991). Filter screening of antibody Fab fragments secreted from individual bacterial colonies: specific detection of antigen binding with a two-membrane system. Anal. Biochem. 196, 151-155.
    • (1991) Anal. Biochem. , vol.196 , pp. 151-155
    • Skerra, A.1    Dreher, M.L.2    Winter, G.3
  • 48
    • 0028276873 scopus 로고
    • Human-engineered monoclonal antibodies retain full specific binding activity by preserving non-CDR complementarity-modulating residues
    • Studnicka, G. M., Scares, S., Better, M., Williams, R. E., Nadell, R. and Horwitz, A. H. (1994). Human-engineered monoclonal antibodies retain full specific binding activity by preserving non-CDR complementarity-modulating residues. Prot. Eng. 7, 805-814.
    • (1994) Prot. Eng. , vol.7 , pp. 805-814
    • Studnicka, G.M.1    Scares, S.2    Better, M.3    Williams, R.E.4    Nadell, R.5    Horwitz, A.H.6
  • 49
    • 0028518518 scopus 로고
    • In vivo biotinylated antibodies: Construction, characterisation and application of a bifunctional Fab-BCCP fusion protein produced in E. coli.
    • Weiss, E., Chatellier, J. and Orfanoudakis, G. (1994). In vivo biotinylated antibodies: construction, characterisation and application of a bifunctional Fab-BCCP fusion protein produced in E. coli. Prot. Express. Purif. 5, 509-517.
    • (1994) Prot. Express. Purif. , vol.5 , pp. 509-517
    • Weiss, E.1    Chatellier, J.2    Orfanoudakis, G.3
  • 50
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J. and Messing, J. (1985). Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.