메뉴 건너뛰기




Volumn 48, Issue 6, 2009, Pages 1390-1398

Association energetics of cross-reactive and specific antibodies

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; ASSOCIATION REACTIONS; DISSOCIATION; ENZYMES; PLASMONS; SURFACE PLASMON RESONANCE; THERMODYNAMICS;

EID: 64349108978     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801901d     Document Type: Article
Times cited : (26)

References (44)
  • 1
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L., Chothia, C., and Janin, J. (1999) The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285, 2177-2198.
    • (1999) J. Mol. Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 2
    • 0028299082 scopus 로고
    • The energetics of antigen-antibody binding
    • Mariuzza, R. A., Poljak, R. J., and Schwarz, F. P. (1994) The energetics of antigen-antibody binding. Res. Immunol. 145, 70-72.
    • (1994) Res. Immunol , vol.145 , pp. 70-72
    • Mariuzza, R.A.1    Poljak, R.J.2    Schwarz, F.P.3
  • 3
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antibody-antigen complexes
    • Sundberg, E. J., and Mariuzza, R. A. (2002) Molecular recognition in antibody-antigen complexes. Adv. Protein Chem. 61, 119-160.
    • (2002) Adv. Protein Chem , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 4
    • 0026575333 scopus 로고
    • Experimental analysis by site-directed mutagenesis of somatic mutation effects on affinity and fine specificity in antibodies specific for lysozyme
    • Lavoie, T. B., Drohan, W. N., and Smith-Gill, S. J. (1992) Experimental analysis by site-directed mutagenesis of somatic mutation effects on affinity and fine specificity in antibodies specific for lysozyme. J. Immunol. 148, 503-513.
    • (1992) J. Immunol , vol.148 , pp. 503-513
    • Lavoie, T.B.1    Drohan, W.N.2    Smith-Gill, S.J.3
  • 6
    • 0038103565 scopus 로고    scopus 로고
    • X-ray snapshots of the maturation of an antibody response to a protein antigen
    • Li, Y., Li, H., Yang, F., Smith-Gill, S. J., and Mariuzza, R. A. (2003) X-ray snapshots of the maturation of an antibody response to a protein antigen. Nat. Struct. Biol. 10, 482-488.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 482-488
    • Li, Y.1    Li, H.2    Yang, F.3    Smith-Gill, S.J.4    Mariuzza, R.A.5
  • 7
    • 0026442095 scopus 로고
    • Patterns of antibody specificity during the BALB/c immune response to hen eggwhite lysozyme
    • Newman, M. A., Mainhart, C. R., Mallett, C. P., Lavoie, T. B., and Smith-Gill, S. J. (1992) Patterns of antibody specificity during the BALB/c immune response to hen eggwhite lysozyme. J. Immunol. 149, 3260-3272.
    • (1992) J. Immunol , vol.149 , pp. 3260-3272
    • Newman, M.A.1    Mainhart, C.R.2    Mallett, C.P.3    Lavoie, T.B.4    Smith-Gill, S.J.5
  • 9
    • 0035916256 scopus 로고    scopus 로고
    • Mutations of an epitope hot-spot residue alter rate limiting steps of antigen-antibody protein-protein associations
    • Li, Y., Lipschultz, C. A., Mohan, S., and Smith-Gill, S. J. (2001) Mutations of an epitope hot-spot residue alter rate limiting steps of antigen-antibody protein-protein associations. Biochemistry 40, 2011-2022.
    • (2001) Biochemistry , vol.40 , pp. 2011-2022
    • Li, Y.1    Lipschultz, C.A.2    Mohan, S.3    Smith-Gill, S.J.4
  • 10
    • 0034426852 scopus 로고    scopus 로고
    • Experimental design for analysis of complex kinetics using surface plasmon resonance
    • Lipschultz, C. A., Li, Y., and Smith-Gill, S. (2000) Experimental design for analysis of complex kinetics using surface plasmon resonance. Methods 20, 310-318.
    • (2000) Methods , vol.20 , pp. 310-318
    • Lipschultz, C.A.1    Li, Y.2    Smith-Gill, S.3
  • 11
    • 0036006150 scopus 로고    scopus 로고
    • Temperature differentially affects encounter and docking thermodynamics of antibody-antigen association
    • Lipschultz, C. A., Yee, A., Mohan, S., Li, Y., and Smith-Gill, S. J. (2002) Temperature differentially affects encounter and docking thermodynamics of antibody-antigen association. J. Mol. Recognit. 15, 44-52.
    • (2002) J. Mol. Recognit , vol.15 , pp. 44-52
    • Lipschultz, C.A.1    Yee, A.2    Mohan, S.3    Li, Y.4    Smith-Gill, S.J.5
  • 12
    • 0036890316 scopus 로고    scopus 로고
    • Electrostatics in protein binding and function
    • Sinha, N., and Smith-Gill, S. J. (2002) Electrostatics in protein binding and function. Curr. Protein Pept. Sci. 3, 601-614.
    • (2002) Curr. Protein Pept. Sci , vol.3 , pp. 601-614
    • Sinha, N.1    Smith-Gill, S.J.2
  • 13
    • 0021238906 scopus 로고
    • Antigenic regions defined by monoclonal antibodies correspond to structural domains of avian lysozyme
    • Smith-Gill, S. J., Lavoie, T. B., and Mainhart, C. R. (1984) Antigenic regions defined by monoclonal antibodies correspond to structural domains of avian lysozyme. J. Immunol. 133, 384-393.
    • (1984) J. Immunol , vol.133 , pp. 384-393
    • Smith-Gill, S.J.1    Lavoie, T.B.2    Mainhart, C.R.3
  • 15
    • 0028280409 scopus 로고
    • Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody HyHEL-5
    • Hibbits, K. A., Gill, D. S., and Willson, R. C. (1994) Isothermal titration calorimetric study of the association of hen egg lysozyme and the anti-lysozyme antibody HyHEL-5. Biochemistry 33, 3584-3590.
    • (1994) Biochemistry , vol.33 , pp. 3584-3590
    • Hibbits, K.A.1    Gill, D.S.2    Willson, R.C.3
  • 16
    • 34247124903 scopus 로고
    • The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme
    • Shugar, D. (1952) The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme. Biochim. Biophys. Acta 8, 302-309.
    • (1952) Biochim. Biophys. Acta , vol.8 , pp. 302-309
    • Shugar, D.1
  • 17
    • 0014595905 scopus 로고
    • Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 25 degrees
    • Aune, K. C., and Tanford, C. (1969) Thermodynamics of the denaturation of lysozyme by guanidine hydrochloride. I. Dependence on pH at 25 degrees. Biochemistry 8, 4579-4585.
    • (1969) Biochemistry , vol.8 , pp. 4579-4585
    • Aune, K.C.1    Tanford, C.2
  • 18
    • 0014503198 scopus 로고
    • Lysozymes: A chapter of molecular biology
    • Jolles, P. (1969) Lysozymes: a chapter of molecular biology. Angew. Chem., Int. Ed. Engl. 8, 227-239.
    • (1969) Angew. Chem., Int. Ed. Engl , vol.8 , pp. 227-239
    • Jolles, P.1
  • 19
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C., and von Hippel, P. H. (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
  • 21
    • 0031919676 scopus 로고    scopus 로고
    • Association and dissociation kinetics of anti-hen egg lysozyme monoclonal antibodies HyHEL-5 and HyHEL-10
    • Xavier, K. A., and Willson, R. C. (1998) Association and dissociation kinetics of anti-hen egg lysozyme monoclonal antibodies HyHEL-5 and HyHEL-10. Biophys. J. 74, 2036-2045.
    • (1998) Biophys. J , vol.74 , pp. 2036-2045
    • Xavier, K.A.1    Willson, R.C.2
  • 22
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J. F., and Lin, L. N. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137.
    • (1989) Anal. Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 23
    • 42149188818 scopus 로고    scopus 로고
    • Conformational flexibility and kinetic complexity in antibody-antigen interactions
    • Kourentzi, K., Srinivasan, M., Smith-Gill, S. J., and Willson, R. C. (2008) Conformational flexibility and kinetic complexity in antibody-antigen interactions. J. Mol. Recognit. 21, 114-121.
    • (2008) J. Mol. Recognit , vol.21 , pp. 114-121
    • Kourentzi, K.1    Srinivasan, M.2    Smith-Gill, S.J.3    Willson, R.C.4
  • 24
    • 0026052762 scopus 로고
    • Direct calorimetric analysis of the enzymatic activity of yeast cytochrome c oxidase
    • Morin, P. E., and Freire, E. (1991) Direct calorimetric analysis of the enzymatic activity of yeast cytochrome c oxidase. Biochemistry 30, 8494-8500.
    • (1991) Biochemistry , vol.30 , pp. 8494-8500
    • Morin, P.E.1    Freire, E.2
  • 25
    • 0029706920 scopus 로고    scopus 로고
    • The effect of water activity on the association constant and the enthalpy of reaction between lysozyme and the specific antibodies D1.3 and D44.1
    • Goldbaum, F. A., Schwarz, F. P., Eisenstein, E., Cauerhff, A., Mariuzza, R. A., and Poljak, R. J. (1996) The effect of water activity on the association constant and the enthalpy of reaction between lysozyme and the specific antibodies D1.3 and D44.1. J. Mol. Recognit. 9, 6-12.
    • (1996) J. Mol. Recognit , vol.9 , pp. 6-12
    • Goldbaum, F.A.1    Schwarz, F.P.2    Eisenstein, E.3    Cauerhff, A.4    Mariuzza, R.A.5    Poljak, R.J.6
  • 26
    • 0038813750 scopus 로고    scopus 로고
    • The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction
    • Yokota, A., Tsumoto, K., Shiroishi, M., Kondo, H., and Kumagai, I. (2003) The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction. J. Biol. Chem. 278, 5410-5418.
    • (2003) J. Biol. Chem , vol.278 , pp. 5410-5418
    • Yokota, A.1    Tsumoto, K.2    Shiroishi, M.3    Kondo, H.4    Kumagai, I.5
  • 27
    • 0028289925 scopus 로고
    • Solvent rearrangement in an antigen-antibody interface introduced by site-directed mutagenesis of the antibody combining site
    • Ysern, X., Fields, B. A., Bhat, T. N., Goldbaum, F. A., Dall'Acqua, W., Schwarz, F. P., Poljak, R. J., and Mariuzza, R. A. (1994) Solvent rearrangement in an antigen-antibody interface introduced by site-directed mutagenesis of the antibody combining site. J. Mol. Biol. 238, 496-500.
    • (1994) J. Mol. Biol , vol.238 , pp. 496-500
    • Ysern, X.1    Fields, B.A.2    Bhat, T.N.3    Goldbaum, F.A.4    Dall'Acqua, W.5    Schwarz, F.P.6    Poljak, R.J.7    Mariuzza, R.A.8
  • 28
    • 0036923836 scopus 로고    scopus 로고
    • Differences in electrostatic properties at antibody-antigen binding sites: Implications for specificity and cross-reactivity
    • Sinha, N., Mohan, S., Lipschultz, C. A., and Smith-Gill, S. J. (2002) Differences in electrostatic properties at antibody-antigen binding sites: implications for specificity and cross-reactivity. Biophys. J. 83, 2946-2968.
    • (2002) Biophys. J , vol.83 , pp. 2946-2968
    • Sinha, N.1    Mohan, S.2    Lipschultz, C.A.3    Smith-Gill, S.J.4
  • 29
    • 0242385341 scopus 로고    scopus 로고
    • Modeling the binding sites of anti-hen egg white lysozyme antibodies HyHEL-8 and HyHEL-26: An insight into the molecular basis of antibody cross-reactivity and specificity
    • Mohan, S., Sinha, N., and Smith-Gill, S. J. (2003) Modeling the binding sites of anti-hen egg white lysozyme antibodies HyHEL-8 and HyHEL-26: an insight into the molecular basis of antibody cross-reactivity and specificity. Biophys. J. 85, 3221-3236.
    • (2003) Biophys. J , vol.85 , pp. 3221-3236
    • Mohan, S.1    Sinha, N.2    Smith-Gill, S.J.3
  • 31
    • 0033181015 scopus 로고    scopus 로고
    • The effect of inhibitor binding on the structural stability and cooperativity of the HIV-1 protease
    • Todd, M. J., and Freire, E. (1999) The effect of inhibitor binding on the structural stability and cooperativity of the HIV-1 protease. Proteins 36, 147-156.
    • (1999) Proteins , vol.36 , pp. 147-156
    • Todd, M.J.1    Freire, E.2
  • 32
    • 0021383150 scopus 로고
    • VL-VH expression by monoclonal antibodies recognizing avian lysozyme
    • Smith-Gill, S. J., Mainhart, C. R., Lavoie, T. B., Rudikoff, S., and Potter, M. (1984) VL-VH expression by monoclonal antibodies recognizing avian lysozyme. J. Immunol. 132, 963-967.
    • (1984) J. Immunol , vol.132 , pp. 963-967
    • Smith-Gill, S.J.1    Mainhart, C.R.2    Lavoie, T.B.3    Rudikoff, S.4    Potter, M.5
  • 36
    • 0032958585 scopus 로고    scopus 로고
    • Energetic analysis of an antigen/antibody interface: Alanine scanning mutagenesis and double mutant cycles on the HyHEL-10/lysozyme interaction
    • Pons, J., Rajpal, A., and Kirsch, J. F. (1999) Energetic analysis of an antigen/antibody interface: alanine scanning mutagenesis and double mutant cycles on the HyHEL-10/lysozyme interaction. Protein Sci. 8, 958-968.
    • (1999) Protein Sci , vol.8 , pp. 958-968
    • Pons, J.1    Rajpal, A.2    Kirsch, J.F.3
  • 37
    • 0031665047 scopus 로고    scopus 로고
    • Quantitative evaluation of the chicken lysozyme epitope in the HyHEL-10 Fab complex: Free energies and kinetics
    • Rajpal, A., Taylor, M. G., and Kirsch, J. F. (1998) Quantitative evaluation of the chicken lysozyme epitope in the HyHEL-10 Fab complex: free energies and kinetics. Protein Sci. 7 1868-1874.
    • (1998) Protein Sci , vol.7 , pp. 1868-1874
    • Rajpal, A.1    Taylor, M.G.2    Kirsch, J.F.3
  • 38
    • 0031694146 scopus 로고    scopus 로고
    • Kinetic epitope mapping of the chicken lysozyme·HyHEL-10 Fab complex: Delineation of docking trajectories
    • Taylor, M. G., Rajpal, A., and Kirsch, J. F. (1998) Kinetic epitope mapping of the chicken lysozyme·HyHEL-10 Fab complex: delineation of docking trajectories. Protein Sci. 7, 1857-1867.
    • (1998) Protein Sci , vol.7 , pp. 1857-1867
    • Taylor, M.G.1    Rajpal, A.2    Kirsch, J.F.3
  • 41
    • 0042090280 scopus 로고    scopus 로고
    • Structural consequences of target epitope-directed functional alteration of an antibody. The case of anti-hen lysozyme antibody, HyHEL-10
    • Kumagai, I., Nishimiya, Y., Kondo, H., and Tsumoto, K. (2003) Structural consequences of target epitope-directed functional alteration of an antibody. The case of anti-hen lysozyme antibody, HyHEL-10. J. Biol. Chem. 278, 24929-24936.
    • (2003) J. Biol. Chem , vol.278 , pp. 24929-24936
    • Kumagai, I.1    Nishimiya, Y.2    Kondo, H.3    Tsumoto, K.4
  • 42
    • 0034724710 scopus 로고    scopus 로고
    • Thermodynamic consequences of grafting enhanced affinity toward the mutated antigen onto an antibody. The case of anti-lysozyme antibody, HyHEL-10
    • Nishimiya, Y., Tsumoto, K., Shiroishi, M., Yutani, K., and Kumagai, I. (2000) Thermodynamic consequences of grafting enhanced affinity toward the mutated antigen onto an antibody. The case of anti-lysozyme antibody, HyHEL-10. J. Biol. Chem. 275, 12813-12820.
    • (2000) J. Biol. Chem , vol.275 , pp. 12813-12820
    • Nishimiya, Y.1    Tsumoto, K.2    Shiroishi, M.3    Yutani, K.4    Kumagai, I.5
  • 43
    • 0028809265 scopus 로고
    • Configurational effects in antibody-antigen interactions studied by microcalorimetry
    • Murphy, K. P., Freire, E., and Paterson, Y. (1995) Configurational effects in antibody-antigen interactions studied by microcalorimetry. Proteins 21, 83-90.
    • (1995) Proteins , vol.21 , pp. 83-90
    • Murphy, K.P.1    Freire, E.2    Paterson, Y.3
  • 44
    • 23244468302 scopus 로고    scopus 로고
    • Molecular dynamics simulation of a high-affinity antibody-protein complex: The binding site is a mosaic of locally flexible and preorganized rigid regions
    • Sinha, N., and Smith-Gill, S. J. (2005) Molecular dynamics simulation of a high-affinity antibody-protein complex: the binding site is a mosaic of locally flexible and preorganized rigid regions. Cell Biochem. Biophys. 43, 253-273.
    • (2005) Cell Biochem. Biophys , vol.43 , pp. 253-273
    • Sinha, N.1    Smith-Gill, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.