메뉴 건너뛰기




Volumn 13, Issue 3, 2000, Pages 127-139

Effects on interaction kinetics of mutations at the VH-VL interface of Fabs depend on the structural context

Author keywords

Antibody engineering; Biacore ; Kinetic rate constants; Peptide antibody interaction; Recombinant Fab; Site directed mutagenesis; VH VL interface

Indexed keywords

AMINO ACID SUBSTITUTION; ANTIBODY SPECIFICITY; ANTIGEN BINDING; BINDING KINETICS; FAB FRAGMENT; MUTANT; MUTATION;

EID: 0004773096     PISSN: 09523499     EISSN: None     Source Type: Journal    
DOI: 10.1002/1099-1352(200005/06)13:3<127::AID-JMR495>3.0.CO;2-9     Document Type: Article
Times cited : (34)

References (37)
  • 2
    • 0001424318 scopus 로고
    • A major part of the polypeptide chain of tobacco mosaic virus protein is antigenic
    • Al Moudallal Z, Briand JP, Van Regenmortel MHV. 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
  • 3
  • 4
    • 0027433096 scopus 로고
    • High-affinity self-reactive human antibodies by design and selection: Targeting the integrin ligand binding site
    • Barbas CFd, Languino LR, Smith JW. 1993. High-affinity self-reactive human antibodies by design and selection: targeting the integrin ligand binding site. Proc. Natl Acad. Sci. USA 90: 10003-10007.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10003-10007
    • Barbas, C.1    Languino, L.R.2    Smith, J.W.3
  • 5
    • 0029717697 scopus 로고    scopus 로고
    • Comparative interaction kinetics of two recombinant Fabs and of the corresponding antibodies directed to the coat protein of tobacco mosaic virus
    • Chatellier J, Rauffer-Bruyère N, Van Regenmortel MH, Altschuh D, Weiss E. 1996a. Comparative interaction kinetics of two recombinant Fabs and of the corresponding antibodies directed to the coat protein of tobacco mosaic virus. J. Mol. Recognit. 9: 39-51X.
    • (1996) J. Mol. Recognit. , vol.9 , pp. 39-51X
    • Chatellier, J.1    Rauffer-Bruyère, N.2    Van Regenmortel, M.H.3    Altschuh, D.4    Weiss, E.5
  • 6
    • 0030598344 scopus 로고    scopus 로고
    • Functional mapping of conserved residues located at the VL and VH domain interface of a Fab
    • Chatellier J, Van Regenmortel MH, Vernet T, Altschuh D. 1996b. Functional mapping of conserved residues located at the VL and VH domain interface of a Fab. J. Mol. Biol. 264: 1-6X.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1-6X
    • Chatellier, J.1    Van Regenmortel, M.H.2    Vernet, T.3    Altschuh, D.4
  • 7
    • 0032553334 scopus 로고    scopus 로고
    • Crystal structures of a rat anti-CD52 (CAMPATH-1) therapeutic antibody Fab fragment and its humanized counterpart
    • Cheetham GM, Hale G, Waldmann H, Bloomer AC. 1998. Crystal structures of a rat anti-CD52 (CAMPATH-1) therapeutic antibody Fab fragment and its humanized counterpart. J. Mol. Biol. 284: 85-99.
    • (1998) J. Mol. Biol. , vol.284 , pp. 85-99
    • Cheetham, G.M.1    Hale, G.2    Waldmann, H.3    Bloomer, A.C.4
  • 8
    • 0024368992 scopus 로고
    • Significant structural and functional change of an antigen-binding site by a distant amino acid substitution: Proposal of a structural mechanism
    • Chien NC, Roberts VA, Giusti AM, Scharff MD, Getzoff ED. 1989. Significant structural and functional change of an antigen-binding site by a distant amino acid substitution: proposal of a structural mechanism. Proc. Natl Acad. Sci. USA 86: 5532-5536.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 5532-5536
    • Chien, N.C.1    Roberts, V.A.2    Giusti, A.M.3    Scharff, M.D.4    Getzoff, E.D.5
  • 9
    • 0032080047 scopus 로고    scopus 로고
    • Structural determinants in the sequences of immunoglobulin variable domain
    • Chothia C, Gelfand I, Kister A. 1998. Structural determinants in the sequences of immunoglobulin variable domain. J. Mol. Biol. 278: 457-479.
    • (1998) J. Mol. Biol. , vol.278 , pp. 457-479
    • Chothia, C.1    Gelfand, I.2    Kister, A.3
  • 10
    • 0033596904 scopus 로고    scopus 로고
    • Kinetic analysis of the effect on Fab binding of identical substitutions in a peptide and its parent protein
    • Choulier L, Rauffer-Bruyère N, Ben Khalifa M, Martin F, Vernet T, Altschuh D. 1999. Kinetic analysis of the effect on Fab binding of identical substitutions in a peptide and its parent protein. Biochemistry 38: 3530-3537.
    • (1999) Biochemistry , vol.38 , pp. 3530-3537
    • Choulier, L.1    Rauffer-Bruyère, N.2    Ben Khalifa, M.3    Martin, F.4    Vernet, T.5    Altschuh, D.6
  • 11
    • 0032483392 scopus 로고    scopus 로고
    • Improved stability and yield of a Fv-toxin fusion protein by computer design and protein engineering of the Fv. (in process citation.)
    • Chowdhury PS, Vasmatzis G, Beers R, Lee B, Pastan I. 1998. Improved stability and yield of a Fv-toxin fusion protein by computer design and protein engineering of the Fv. (In Process Citation.) J. Mol. Biol. 281: 917-928.
    • (1998) J. Mol. Biol. , vol.281 , pp. 917-928
    • Chowdhury, P.S.1    Vasmatzis, G.2    Beers, R.3    Lee, B.4    Pastan, I.5
  • 12
    • 0033558333 scopus 로고    scopus 로고
    • Functional characterization of the somatic hypermutation process leading to antibody D1.3, a high affinity antibody directed against lysozyme
    • England P, Nageotte R, Renard M, Page AL, Bedouelle H. 1999. Functional characterization of the somatic hypermutation process leading to antibody D1.3, a high affinity antibody directed against lysozyme. J. Immunol. 162: 2129-2136.
    • (1999) J. Immunol. , vol.162 , pp. 2129-2136
    • England, P.1    Nageotte, R.2    Renard, M.3    Page, A.L.4    Bedouelle, H.5
  • 13
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote J, Winter G. 1992. Antibody framework residues affecting the conformation of the hypervariable loops. J. Mol. Biol. 224: 487-499.
    • (1992) J. Mol. Biol. , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 14
    • 0028847036 scopus 로고
    • Analysis of the relation between the sequence and secondary and three- dimensional structures of immunoglobulin molecules
    • Gelfand IM, Kister AE. 1995. Analysis of the relation between the sequence and secondary and three- dimensional structures of immunoglobulin molecules. Proc. Natl Acad. Sci. USA 92: 10884-10888.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10884-10888
    • Gelfand, I.M.1    Kister, A.E.2
  • 15
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77: 51-59.
    • (1989) Gene. , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 16
    • 0030322783 scopus 로고    scopus 로고
    • Double-mutant cycles: A powerful tool for analyzing protein structure and function
    • Horovitz A. 1996. Double-mutant cycles: a powerful tool for analyzing protein structure and function. Fold Des. 1: R121-R126.
    • (1996) Fold Des. , vol.1
    • Horovitz, A.1
  • 17
    • 0030391262 scopus 로고    scopus 로고
    • Mechanism of HPV E6 proteins in cellular transformation
    • Huibregtse JM, Beaudenon SL 1996. Mechanism of HPV E6 proteins in cellular transformation. Sem. Cancer Biol. 7: 317-326.
    • (1996) Sem. Cancer Biol. , vol.7 , pp. 317-326
    • Huibregtse, J.M.1    Beaudenon, S.L.2
  • 19
    • 0030931016 scopus 로고    scopus 로고
    • Mutation matrices and physical-chemical properties: Correlations and implications
    • Koshi JM, Goldstein RA. 1997. Mutation matrices and physical-chemical properties: correlations and implications. Proteins 27: 336-344.
    • (1997) Proteins , vol.27 , pp. 336-344
    • Koshi, J.M.1    Goldstein, R.A.2
  • 20
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA 82: 488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 21
    • 0028965496 scopus 로고
    • Long-range, small magnitude nonadditivity of mutational effects in proteins
    • LiCata VJ, Ackers GK. 1995. Long-range, small magnitude nonadditivity of mutational effects in proteins. Biochemistry 34: 3133-3139.
    • (1995) Biochemistry , vol.34 , pp. 3133-3139
    • Licata, V.J.1    Ackers, G.K.2
  • 22
    • 0342301333 scopus 로고    scopus 로고
    • Use of plasmon resonance (BIAcore™) for the analysis of ligand-receptor interactions
    • CRC Press, Boca Raton, FL (Morel, G., ed.)
    • Lortat-Jacob H, Ricard-Blum S. 1997. Use of plasmon resonance (BIAcore™) for the analysis of ligand-receptor interactions. In Visualization of receptors - Methods in Light and Electron Microscopy CRC Press, Boca Raton, FL (Morel, G., ed.), pp. 161-180.
    • (1997) Visualization of Receptors - Methods in Light and Electron Microscopy , pp. 161-180
    • Lortat-Jacob, H.1    Ricard-Blum, S.2
  • 25
    • 0027359747 scopus 로고
    • Bacterially expressed fabs of monoclonal antibodies neutralizing tumour necrosis factor alpha in vitro retain full binding and biological activity
    • Orfanoudakis G, Karim B, Bourel D, Weiss E. 1993. Bacterially expressed Fabs of monoclonal 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
  • 30
    • 0027248706 scopus 로고
    • Engineering multiple properties of a protein by combinatorial mutagenesis
    • Sandberg WS, Terwilliger TC. 1993. Engineering multiple properties of a protein by combinatorial mutagenesis. Proc. Natl Acad. Sci. USA 90: 8367-8371.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 8367-8371
    • Sandberg, W.S.1    Terwilliger, T.C.2
  • 31
    • 0030575802 scopus 로고    scopus 로고
    • Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site
    • Schier R, McCall A, Adams GP, Marshall KW, Merritt H, Yim M, Crawford RS, Weiner LM, Marks C, Marks JD. 1996. Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site. J. Mol. Biol. 263: 551-567.
    • (1996) J. Mol. Biol. , vol.263 , pp. 551-567
    • Schier, R.1    McCall, A.2    Adams, G.P.3    Marshall, K.W.4    Merritt, H.5    Yim, M.6    Crawford, R.S.7    Weiner, L.M.8    Marks, C.9    Marks, J.D.10
  • 32
    • 0029056922 scopus 로고
    • Energetics of protein-protein interactions: Analysis of the barnase-barstar interface by single mutations and double mutant cycles
    • Schreiber G, Fersht AR. 1995. Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles. J. Mol. Biol. 248: 478-486.
    • (1995) J. Mol. Biol. , vol.248 , pp. 478-486
    • Schreiber, G.1    Fersht, A.R.2
  • 33
    • 0025358376 scopus 로고
    • Structural correlates of high antibody affinity: Three engineered amino acid substitutions can increase the affinity of an anti-p- azophenylarsonate antibody 200-fold
    • Sharon J. 1990. Structural correlates of high antibody affinity: three engineered amino acid substitutions can increase the affinity of an anti-p- azophenylarsonate antibody 200-fold. Proc. Natl Acad. Sci. USA 87: 4814-4817.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4814-4817
    • Sharon, J.1
  • 34
    • 0031660079 scopus 로고    scopus 로고
    • Contributions of a highly conserved VH/VL hydrogen bonding interaction to scfv folding stability and refolding efficiency
    • Tan PH, Sandmaier BM, Stayton PS. 1998. Contributions of a highly conserved VH/VL hydrogen bonding interaction to scFv folding stability and refolding efficiency. Biophys. J. 75: 1473-1482.
    • (1998) Biophys. J. , vol.75 , pp. 1473-1482
    • Tan, P.H.1    Sandmaier, B.M.2    Stayton, P.S.3
  • 35
    • 0028865817 scopus 로고
    • Framework residues 71 and 93 of the chimeric B72.3 antibody are major determinants of the conformation of heavy-chain hypervariable loops
    • Xiang J, Sha Y, Jia Z, Prasad L, Delbaere LT. 1995. Framework residues 71 and 93 of the chimeric B72.3 antibody are major determinants of the conformation of heavy-chain hypervariable loops. J. Mol. Biol. 253: 385-390.
    • (1995) J. Mol. Biol. , vol.253 , pp. 385-390
    • Xiang, J.1    Sha, Y.2    Jia, Z.3    Prasad, L.4    Delbaere, L.T.5
  • 36
    • 0029564921 scopus 로고
    • Cdr walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range
    • Yang WP, Green K, Pinz-Sweeney S, Briones AT, Burton DR, Barbas CF III. 1995. CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J. Mol. Biol. 254: 392-403.
    • (1995) J. Mol. Biol. , vol.254 , pp. 392-403
    • Yang, W.P.1    Green, K.2    Pinz-Sweeney, S.3    Briones, A.T.4    Burton, D.R.5    Barbas C.F. III6
  • 37
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C, Vieira J, 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.