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Volumn 5, Issue , 2015, Pages

Structural and Physical Basis for Anti-IgE Therapy

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-IGE ANTIBODIES; ANTIASTHMATIC AGENT; ANTIIDIOTYPIC ANTIBODY; IMMUNOGLOBULIN E; IMMUNOGLOBULIN E RECEPTOR; OMALIZUMAB; PROTEIN BINDING;

EID: 84933074093     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep11581     Document Type: Article
Times cited : (43)

References (54)
  • 1
    • 40049101678 scopus 로고    scopus 로고
    • IgE in allergy and asthma today
    • Gould, H. J. & Sutton, B. J. IgE in allergy and asthma today. Nat. Rev. Immunol. 8, 205-217 (2008).
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 205-217
    • Gould, H.J.1    Sutton, B.J.2
  • 2
    • 11944270019 scopus 로고
    • Monoclonal antibodies specific for human IgE-producing B cells: A potential therapeutic for IgE-mediated allergic diseases
    • Chang, T. W. et al. Monoclonal antibodies specific for human IgE-producing B cells: a potential therapeutic for IgE-mediated allergic diseases. Bio/technology 8, 122-126 (1990).
    • (1990) Bio/technology , vol.8 , pp. 122-126
    • Chang, T.W.1
  • 3
    • 77953195601 scopus 로고    scopus 로고
    • Antibodies specific for a segment of human membrane IgE deplete IgE-producing B cells in humanized mice
    • Brightbill, H. D. et al. Antibodies specific for a segment of human membrane IgE deplete IgE-producing B cells in humanized mice. J. Clin. Invest. 120, 2218-2229 (2010).
    • (2010) J. Clin. Invest. , vol.120 , pp. 2218-2229
    • Brightbill, H.D.1
  • 4
    • 80052299857 scopus 로고    scopus 로고
    • A randomized, placebo-controlled, dose-ranging study of single-dose omalizumab in patients with H1-antihistamine-refractory chronic idiopathic urticaria
    • Saini, S. et al. A randomized, placebo-controlled, dose-ranging study of single-dose omalizumab in patients with H1-antihistamine-refractory chronic idiopathic urticaria. J. Allergy Clin. Immunol. 128, 567-573 (2011).
    • (2011) J. Allergy Clin. Immunol. , vol.128 , pp. 567-573
    • Saini, S.1
  • 5
    • 84874732930 scopus 로고    scopus 로고
    • Omalizumab for the treatment of chronic idiopathic or spontaneous urticaria
    • Maurer, M. et al. Omalizumab for the treatment of chronic idiopathic or spontaneous urticaria. N. Engl. J. Med. 368, 924-935 (2013).
    • (2013) N. Engl. J. Med. , vol.368 , pp. 924-935
    • Maurer, M.1
  • 6
    • 84922343034 scopus 로고    scopus 로고
    • The potential pharmacologic mechanisms of omalizumab in patients with chronic spontaneous urticaria
    • Chang, T. W. et al. The potential pharmacologic mechanisms of omalizumab in patients with chronic spontaneous urticaria. J. Allergy Clin. Immunol. 135, 337-342 (2015).
    • (2015) J. Allergy Clin. Immunol. , vol.135 , pp. 337-342
    • Chang, T.W.1
  • 7
    • 0025089806 scopus 로고
    • Can antibodies to IgE act as anti-allergics?
    • Bialy H. Can antibodies to IgE act as anti-allergics? Nature Biotech. 8, 96 (1990)
    • (1990) Nature Biotech , vol.8 , pp. 96
    • Bialy, H.1
  • 8
    • 0031065108 scopus 로고    scopus 로고
    • Down-regulation of Fc? RI expression on human basophils during in vivo treatment of atopic patients with anti-IgE antibody
    • Saini, S. S. et al. Down-regulation of Fc? RI expression on human basophils during in vivo treatment of atopic patients with anti-IgE antibody. J. Immunol. 158, 1438-1445 (1997).
    • (1997) J. Immunol. , vol.158 , pp. 1438-1445
    • Saini, S.S.1
  • 10
    • 0347364816 scopus 로고    scopus 로고
    • Omalizumab treatment downregulates dendritic cell Fc? RI expression
    • Prussin, C. et al. Omalizumab treatment downregulates dendritic cell Fc? RI expression. J. Allergy Clin. Immunol. 112, 1147-1154, (2003).
    • (2003) J. Allergy Clin. Immunol. , vol.112 , pp. 1147-1154
    • Prussin, C.1
  • 11
    • 0027155071 scopus 로고
    • Can anti-IgE be used to treat allergy?
    • Davis, F. M. et al. Can anti-IgE be used to treat allergy? Springer Semin. Immunopathol. 15, 51-73 (1993).
    • (1993) Springer Semin. Immunopathol. , vol.15 , pp. 51-73
    • Davis, F.M.1
  • 12
    • 33947307347 scopus 로고    scopus 로고
    • Anti-IgE antibodies for the treatment of IgE-mediated allergic diseases
    • Chang, T. W., Wu, P. C., Hsu, C. L. & Hung, A. F. Anti-IgE antibodies for the treatment of IgE-mediated allergic diseases. Advances in Immunol. 93, 63-119 (2007).
    • (2007) Advances in Immunol. , vol.93 , pp. 63-119
    • Chang, T.W.1    Wu, P.C.2    Hsu, C.L.3    Hung, A.F.4
  • 13
    • 0031872148 scopus 로고    scopus 로고
    • Prediction of an anti-IgE binding site on IgE
    • Wright, J. D. & Lim, C. Prediction of an anti-IgE binding site on IgE. Prot. Eng. 11, 421-427 (1998).
    • (1998) Prot. Eng. , vol.11 , pp. 421-427
    • Wright, J.D.1    Lim, C.2
  • 15
    • 0034691520 scopus 로고    scopus 로고
    • Structure of the Fc fragment of human IgE bound to its high affinity receptor Fc? RI?
    • Garman, S. C., Wurzburg, B. A., Tarchevskaya, S. S., Kinet, J. P. & Jardetzky, T. S. Structure of the Fc fragment of human IgE bound to its high affinity receptor Fc? RI? . Nature 406, 259-266 (2000).
    • (2000) Nature , vol.406 , pp. 259-266
    • Garman, S.C.1    Wurzburg, B.A.2    Tarchevskaya, S.S.3    Kinet, J.P.4    Jardetzky, T.S.5
  • 16
    • 79955603056 scopus 로고    scopus 로고
    • Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor Fc? RI
    • Holdom, M. D. et al. Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor Fc? RI. Nat. Struct. Mol. Biol. 18, 571-576 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 571-576
    • Holdom, M.D.1
  • 17
    • 84864497135 scopus 로고    scopus 로고
    • Crystal structure of IgE bound to its B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor Fc? RI
    • Dhaliwal, B. et al. Crystal structure of IgE bound to its B-cell receptor CD23 reveals a mechanism of reciprocal allosteric inhibition with high affinity receptor Fc? RI. Proc. Natl. Acad. Sci. USA 109, 12686-12691 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 12686-12691
    • Dhaliwal, B.1
  • 18
    • 84881233799 scopus 로고    scopus 로고
    • Ca2+-dependent structural changes in the B-cell receptor CD23 increase its affinity for human immunoglobulin e
    • Yuan, D. et al. Ca2+-dependent structural changes in the B-cell receptor CD23 increase its affinity for human immunoglobulin E. J. Biol. Chem. 288, 21667-21677 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 21667-21677
    • Yuan, D.1
  • 19
    • 84899708754 scopus 로고    scopus 로고
    • A novel IgE-neutralizing antibody for the treatment of severe uncontrolled asthma
    • Cohen, E. S. et al. A novel IgE-neutralizing antibody for the treatment of severe uncontrolled asthma. mAbs 6, 755-763 (2014).
    • (2014) MAbs , vol.6 , pp. 755-763
    • Cohen, E.S.1
  • 20
    • 84897989805 scopus 로고    scopus 로고
    • Human immunoglobulin e flexes between acutely bent and extended conformations
    • Drinkwater, N. et al. Human immunoglobulin E flexes between acutely bent and extended conformations. Nat. Struct. Mol. Biol. 21, 397-404 (2014).
    • (2014) Nat. Struct. Mol. Biol. , vol.21 , pp. 397-404
    • Drinkwater, N.1
  • 21
    • 84867765150 scopus 로고    scopus 로고
    • An engineered disulfide bond reversibly traps the IgE-Fc 3-4 in a closed, nonreceptor binding conformation
    • Wurzburg, B. A. et al. An engineered disulfide bond reversibly traps the IgE-Fc 3-4 in a closed, nonreceptor binding conformation. J. Biol. Chem. 287, 36251-36257 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 36251-36257
    • Wurzburg, B.A.1
  • 22
    • 84861212045 scopus 로고    scopus 로고
    • A fluorescent biosensor reveals conformational changes in human immunoglobulin e Fc: Implications for mechanisms of receptor binding, inhibition, and allergen recognition
    • Hunt, J. et al. A fluorescent biosensor reveals conformational changes in human immunoglobulin E Fc: implications for mechanisms of receptor binding, inhibition, and allergen recognition. J. Biol. Chem. 287, 17459-17470 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 17459-17470
    • Hunt, J.1
  • 23
    • 84884171998 scopus 로고    scopus 로고
    • Protein-protein docking using EMAP in CHARMM and support vector machine: Application to Ab/Ag complexes J
    • Wright, J. D., Sargsyan, K., Wu, X., Brooks, B. R. & Lim, C. Protein-protein docking using EMAP in CHARMM and support vector machine: Application to Ab/Ag complexes J. Chem. Theory & Comput. 9, 4186-4194 (2013).
    • (2013) Chem. Theory & Comput. , vol.9 , pp. 4186-4194
    • Wright, J.D.1    Sargsyan, K.2    Wu, X.3    Brooks, B.R.4    Lim, C.5
  • 24
    • 0014828908 scopus 로고
    • An analysis of the sequences of the variable regions of Bence-Jones proteins and myeloma light chains and their implications for antibody complementarity
    • Wu, Y. Y. & Kabat, E. A. An analysis of the sequences of the variable regions of Bence-Jones proteins and myeloma light chains and their implications for antibody complementarity. J. Exp. Med 132, 211-249 (1970).
    • (1970) J. Exp. Med , vol.132 , pp. 211-249
    • Wu, Y.Y.1    Kabat, E.A.2
  • 25
  • 26
    • 0027244256 scopus 로고
    • Humanization of an antibody directed against IgE
    • Presta, L. G. et al. Humanization of an antibody directed against IgE. J. Immunol. 151, 2623-2632 (1993).
    • (1993) J. Immunol. , vol.151 , pp. 2623-2632
    • Presta, L.G.1
  • 27
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word, J. M., Lovell, S. C., Richardson, J. S. & Rchardson, D. C. Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation. J. Mol. Biol. 285, 1735-1747 (1999).
    • (1999) J. Mol. Biol. , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Rchardson, D.C.4
  • 28
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • Vriend, G. WHAT IF: A molecular modeling and drug design program. J. Mol. Graph. 8, 52-56 (1990).
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 29
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A. & Baker, N. A. PDB2PQR: an automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-667 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. W665-667
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4
  • 30
    • 79951476387 scopus 로고    scopus 로고
    • PROPKA3: Consistent treatment of internal and surface residues in empirical pKa predictions
    • Olsson, M. H. M., Søndergard, C. R., Rostkowski, M. R. & Jensen, J. H. PROPKA3: Consistent treatment of internal and surface residues in empirical pKa predictions. J. Chem. Theory & Comput. 7, 526-537 (2011).
    • (2011) J. Chem. Theory & Comput. , vol.7 , pp. 526-537
    • Olsson, M.H.M.1    Søndergard, C.R.2    Rostkowski, M.R.3    Jensen, J.H.4
  • 31
    • 69249137563 scopus 로고    scopus 로고
    • HAAD: A quick algorithm for accurate prediction of hydrogen atoms in protein structures
    • Li, Y., Roy, A. & Zhang, Y. HAAD: A quick algorithm for accurate prediction of hydrogen atoms in protein structures. PLoS One 4, e6701 (2009).
    • (2009) PLoS One , vol.4 , pp. e6701
    • Li, Y.1    Roy, A.2    Zhang, Y.3
  • 32
    • 51449106743 scopus 로고    scopus 로고
    • Fine epitope mapping of humanized anti-IgE monoclonal antibody omalizumab
    • Zheng, L. et al. Fine epitope mapping of humanized anti-IgE monoclonal antibody omalizumab. Biochem. Biophys. Res. Commun. 375, 619-622 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.375 , pp. 619-622
    • Zheng, L.1
  • 33
    • 0029117815 scopus 로고
    • Characterization of complex formation by humanized anti-IgE monoclonal antibody and monoclonal human IgE
    • Liu, J., Lester, P., Builder, S. & Shire, S. J. Characterization of complex formation by humanized anti-IgE monoclonal antibody and monoclonal human IgE. Biochemistry 34, 10474-10482 (1995).
    • (1995) Biochemistry , vol.34 , pp. 10474-10482
    • Liu, J.1    Lester, P.2    Builder, S.3    Shire, S.J.4
  • 35
    • 18744372751 scopus 로고    scopus 로고
    • Calculation of absolute protein-ligand binding free energy from computer simulations
    • Woo, H.-J. & Roux, B. Calculation of absolute protein-ligand binding free energy from computer simulations. Proc. Natl. Acad. Sci. U.S.A 102, 6825-6830 (2005).
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 6825-6830
    • Woo, H.-J.1    Roux, B.2
  • 36
    • 0025939199 scopus 로고
    • Conformations of IgE bound to its receptor FceRI and in solution
    • Zheng, Y., Shopes, B., Holowka, D. & Baird, B. Conformations of IgE bound to its receptor FceRI and in solution. Biochemistry 30, 9125-9132 (1991).
    • (1991) Biochemistry , vol.30 , pp. 9125-9132
    • Zheng, Y.1    Shopes, B.2    Holowka, D.3    Baird, B.4
  • 37
    • 0028828789 scopus 로고
    • Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure
    • Beavil, A. J., Young, R. J., Sutton, B. J. & Perkins, S. J. Bent domain structure of recombinant human IgE-Fc in solution by X-ray and neutron scattering in conjunction with an automated curve fitting procedure. Biochemistry 34, 14449-14461 (1995).
    • (1995) Biochemistry , vol.34 , pp. 14449-14461
    • Beavil, A.J.1    Young, R.J.2    Sutton, B.J.3    Perkins, S.J.4
  • 38
    • 0036308980 scopus 로고    scopus 로고
    • The crystal structure of IgE Fc reveals an asymmetrically bent conformation
    • Wan, T. et al. The crystal structure of IgE Fc reveals an asymmetrically bent conformation. Nat. Immunol. 3, 681-686 (2002).
    • (2002) Nat. Immunol. , vol.3 , pp. 681-686
    • Wan, T.1
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Method Enzymol. 276, 307-326 (1997).
    • (1997) Method Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 40
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 41
    • 40349084125 scopus 로고    scopus 로고
    • The crystal structure of the pathogenic collagen type II-specific mouse monoclonal antibody CIIC1 Fab: Structure to function analysis
    • Uysal, H. et al. The crystal structure of the pathogenic collagen type II-specific mouse monoclonal antibody CIIC1 Fab: structure to function analysis. Mol. Immunol. 45, 2196-2204 (2008).
    • (2008) Mol. Immunol. , vol.45 , pp. 2196-2204
    • Uysal, H.1
  • 42
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Cryst. D66, 213-221 (2010)
    • (2010) Acta Cryst. , vol.D66 , pp. 213-221
    • Adams, P.D.1
  • 44
    • 84986512474 scopus 로고
    • CHARMm: A program for macromolecular energy, minimization, and dynamics calculations
    • Brooks, B. R. et al. CHARMm: A program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4, 187-217 (1983).
    • (1983) J. Comput. Chem. , vol.4 , pp. 187-217
    • Brooks, B.R.1
  • 46
    • 0037285752 scopus 로고    scopus 로고
    • A core-weighted fitting method for docking atomic structures into low resolution maps: Application to cyroelectron microsopy
    • Wu, X.-W. et al. A core-weighted fitting method for docking atomic structures into low resolution maps: Application to cyroelectron microsopy. J. Struct. Biol. 141, 63-69 (2003).
    • (2003) J. Struct. Biol. , vol.141 , pp. 63-69
    • Wu, X.-W.1
  • 47
    • 21644469377 scopus 로고    scopus 로고
    • Assessment of CAPRI predictions in rounds 3-5 shows progress in docking procedures
    • Mendez, R., Leplae, R., Lensink, M. F. & Wodak, S. J. Assessment of CAPRI predictions in rounds 3-5 shows progress in docking procedures. Proteins 60, 150-169 (2005).
    • (2005) Proteins , vol.60 , pp. 150-169
    • Mendez, R.1    Leplae, R.2    Lensink, M.F.3    Wodak, S.J.4
  • 48
    • 76249087938 scopus 로고    scopus 로고
    • CHARMM general force field (CGenFF): A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields
    • Vanommeslaeghe, K. et al. CHARMM general force field (CGenFF): A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields. J. Comp. Chem. 31, 671-690 (2010).
    • (2010) J. Comp. Chem. , vol.31 , pp. 671-690
    • Vanommeslaeghe, K.1
  • 50
    • 33846823909 scopus 로고
    • Particle mesh ewald: An N.log(N) method for Ewald sums in large systems
    • Darden, T., York, D. & Pedersen, L. Particle mesh Ewald: An N.log(N) method for Ewald sums in large systems. J. Chem. Phys. 98, 10089-10092 (1993).
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 51
    • 0032560959 scopus 로고    scopus 로고
    • Continuum solvent studies of the stability of DNA, RNA and phosphoramidate-DNA Helices
    • Srinivasan, J., III, T. E. C., Cieplak, P., Kolman, P. A. & Case, D. A. Continuum solvent studies of the stability of DNA, RNA and phosphoramidate-DNA Helices. J. Am. Chem. Soc. 120, 9401-9409 (1998).
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9401-9409
    • Srinivasan, J.1    Cieplak, P.2    Kolman, P.A.3    Case, D.A.4
  • 52
    • 67849092756 scopus 로고    scopus 로고
    • A combined experimental and theoretical study of long-range interactions modulating dimerization and activity of yeast geranylgeranyl diphosphate synthase
    • Lo, C.-H. et al. A combined experimental and theoretical study of long-range interactions modulating dimerization and activity of yeast geranylgeranyl diphosphate synthase. J. Am. Chem. Soc. 131, 4051-4062 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 4051-4062
    • Lo, C.-H.1
  • 53
    • 72249088170 scopus 로고    scopus 로고
    • Redesign of a non-specific endonuclease to yield better DNA-binding activity and altered DNA sequence preference in cleavage
    • Wang, Y. T. et al. Redesign of a non-specific endonuclease to yield better DNA-binding activity and altered DNA sequence preference in cleavage. J. Am. Chem. Soc. 131, 17345-17353 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17345-17353
    • Wang, Y.T.1
  • 54
    • 0032096837 scopus 로고    scopus 로고
    • Continuum solvation model: Computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation
    • Im, W., Beglov, D. Continuum solvation model: Computation of electrostatic forces from numerical solutions to the Poisson-Boltzmann equation. Comput. Phys. Commun. 111, 59-75 (1998).
    • (1998) Comput. Phys. Commun. , vol.111 , pp. 59-75
    • Im, W.1    Beglov, D.2


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