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Volumn 426, Issue 8, 2014, Pages 1799-1811

Immunoglobulin G1 Fc domain motions: Implications for Fc engineering

Author keywords

glycoprotein; molecular dynamics; N glycan; x ray crystallography

Indexed keywords

CARBOHYDRATE; GLYCAN; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN HEAVY CHAIN; MONOMER; POLYPEPTIDE;

EID: 84897110175     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.01.011     Document Type: Article
Times cited : (69)

References (53)
  • 2
    • 84875410765 scopus 로고    scopus 로고
    • Intravenous immunoglobulin therapy: How does IgG modulate the immune system?
    • I. Schwab, and F. Nimmerjahn Intravenous immunoglobulin therapy: how does IgG modulate the immune system? Nat Rev Immunol 13 2013 176 189
    • (2013) Nat Rev Immunol , vol.13 , pp. 176-189
    • Schwab, I.1    Nimmerjahn, F.2
  • 3
    • 15244351004 scopus 로고    scopus 로고
    • Overview of monoclonal antibodies in cancer therapy: Present and promise
    • M. Stern, and R. Herrmann Overview of monoclonal antibodies in cancer therapy: present and promise Crit Rev Oncol Hematol 54 2005 11 29
    • (2005) Crit Rev Oncol Hematol , vol.54 , pp. 11-29
    • Stern, M.1    Herrmann, R.2
  • 4
    • 33847245397 scopus 로고    scopus 로고
    • Recombinant therapeutic antibodies
    • S. Dubel Recombinant therapeutic antibodies Appl Microbiol Biotechnol 74 2007 723 729
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 723-729
    • Dubel, S.1
  • 5
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-Å crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex
    • P. Sondermann, R. Huber, V. Oosthuizen, and U. Jacob The 3.2-Å crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex Nature 406 2000 267 273
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 6
    • 80054944116 scopus 로고    scopus 로고
    • Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans
    • T. Mizushima, H. Yagi, E. Takemoto, M. Shibata-Koyama, Y. Isoda, and S. Iida et al. Structural basis for improved efficacy of therapeutic antibodies on defucosylation of their Fc glycans Genes Cells 16 2011 1071 1080
    • (2011) Genes Cells , vol.16 , pp. 1071-1080
    • Mizushima, T.1    Yagi, H.2    Takemoto, E.3    Shibata-Koyama, M.4    Isoda, Y.5    Iida, S.6
  • 7
    • 0022414766 scopus 로고
    • Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
    • R.B. Parekh, R.A. Dwek, B.J. Sutton, D.L. Fernandes, A. Leung, and D. Stanworth et al. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG Nature 316 1985 452 457
    • (1985) Nature , vol.316 , pp. 452-457
    • Parekh, R.B.1    Dwek, R.A.2    Sutton, B.J.3    Fernandes, D.L.4    Leung, A.5    Stanworth, D.6
  • 8
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution
    • J. Deisenhofer Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution Biochemistry 20 1981 2361 2370
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 9
    • 40749147518 scopus 로고    scopus 로고
    • The N-linked sugar chains of human immunoglobulin G: Their unique pattern, and their functional roles
    • A. Kobata The N-linked sugar chains of human immunoglobulin G: their unique pattern, and their functional roles Biochim Biophys Acta 1780 2008 472 478
    • (2008) Biochim Biophys Acta , vol.1780 , pp. 472-478
    • Kobata, A.1
  • 10
    • 0035979377 scopus 로고    scopus 로고
    • Glycoengineering of therapeutic glycoproteins: In vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues
    • T.S. Raju, J.B. Briggs, S.M. Chamow, M.E. Winkler, and A.J. Jones Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues Biochemistry 40 2001 8868 8876
    • (2001) Biochemistry , vol.40 , pp. 8868-8876
    • Raju, T.S.1    Briggs, J.B.2    Chamow, S.M.3    Winkler, M.E.4    Jones, A.J.5
  • 11
    • 70350055478 scopus 로고    scopus 로고
    • Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I
    • A.W. Barb, E.K. Brady, and J.H. Prestegard Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I Biochemistry 48 2009 9705 9707
    • (2009) Biochemistry , vol.48 , pp. 9705-9707
    • Barb, A.W.1    Brady, E.K.2    Prestegard, J.H.3
  • 12
    • 79951838374 scopus 로고    scopus 로고
    • NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic
    • A.W. Barb, and J.H. Prestegard NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic Nat Chem Biol 7 2011 147 153
    • (2011) Nat Chem Biol , vol.7 , pp. 147-153
    • Barb, A.W.1    Prestegard, J.H.2
  • 13
    • 84861883015 scopus 로고    scopus 로고
    • NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation
    • A.W. Barb, L. Meng, Z. Gao, R.W. Johnson, K.W. Moremen, and J.H. Prestegard NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation Biochemistry 51 2012 4618 4626
    • (2012) Biochemistry , vol.51 , pp. 4618-4626
    • Barb, A.W.1    Meng, L.2    Gao, Z.3    Johnson, R.W.4    Moremen, K.W.5    Prestegard, J.H.6
  • 14
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • J.N. Arnold, M.R. Wormald, R.B. Sim, P.M. Rudd, and R.A. Dwek The impact of glycosylation on the biological function and structure of human immunoglobulins Annu Rev Immunol 25 2007 21 50
    • (2007) Annu Rev Immunol , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 15
    • 84873495247 scopus 로고    scopus 로고
    • Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers
    • G. Lauc, J.E. Huffman, M. Pucic, L. Zgaga, B. Adamczyk, and A. Muzinic et al. Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers PLoS Genet 9 2013 e1003225
    • (2013) PLoS Genet , vol.9 , pp. 1003225
    • Lauc, G.1    Huffman, J.E.2    Pucic, M.3    Zgaga, L.4    Adamczyk, B.5    Muzinic, A.6
  • 16
    • 0028169439 scopus 로고
    • Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1
    • A. Wright, and S.L. Morrison Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1 J Exp Med 180 1994 1087 1096
    • (1994) J Exp Med , vol.180 , pp. 1087-1096
    • Wright, A.1    Morrison, S.L.2
  • 17
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: The high-mannose, hybrid, and complex types
    • Y. Kanda, T. Yamada, K. Mori, A. Okazaki, M. Inoue, and K. Kitajima-Miyama et al. Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types Glycobiology 17 2007 104 118
    • (2007) Glycobiology , vol.17 , pp. 104-118
    • Kanda, Y.1    Yamada, T.2    Mori, K.3    Okazaki, A.4    Inoue, M.5    Kitajima-Miyama, K.6
  • 18
    • 79961233787 scopus 로고    scopus 로고
    • Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose
    • C. Ferrara, S. Grau, C. Jager, P. Sondermann, P. Brunker, and I. Waldhauer et al. Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose Proc Natl Acad Sci U S A 108 2011 12669 12674
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12669-12674
    • Ferrara, C.1    Grau, S.2    Jager, C.3    Sondermann, P.4    Brunker, P.5    Waldhauer, I.6
  • 19
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • S. Krapp, Y. Mimura, R. Jefferis, R. Huber, and P. Sondermann Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity J Mol Biol 325 2003 979 989
    • (2003) J Mol Biol , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 20
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Y. Kaneko, F. Nimmerjahn, and J.V. Ravetch Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation Science 313 2006 670 673
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 21
    • 33847079676 scopus 로고    scopus 로고
    • Evaluating protein structures determined by structural genomics consortia
    • A. Bhattacharya, R. Tejero, and G.T. Montelione Evaluating protein structures determined by structural genomics consortia Proteins 66 2007 778 795
    • (2007) Proteins , vol.66 , pp. 778-795
    • Bhattacharya, A.1    Tejero, R.2    Montelione, G.T.3
  • 22
    • 0030767485 scopus 로고    scopus 로고
    • VERIFY3D: Assessment of protein models with three-dimensional profiles
    • D. Eisenberg, R. Luthy, and J.U. Bowie VERIFY3D: assessment of protein models with three-dimensional profiles Macromolecular Crystallography, Pt B 277 1997 396 404
    • (1997) Macromolecular Crystallography, Pt B , vol.277 , pp. 396-404
    • Eisenberg, D.1    Luthy, R.2    Bowie, J.U.3
  • 23
    • 0027490731 scopus 로고
    • Recognition of errors in 3-dimensional structures of proteins
    • M.J. Sippl Recognition of errors in 3-dimensional structures of proteins Proteins-Struct Funct Genet 17 1993 355 362
    • (1993) Proteins-Struct Funct Genet , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 24
    • 0000243829 scopus 로고
    • Procheck - A program to check the stereochemical quality of protein structures
    • R.A. Laskowski, M.W. Macarthur, D.S. Moss, and J.M. Thornton Procheck - a program to check the stereochemical quality of protein structures J Appl Crystallogr 26 1993 283 291
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • W.L. DeLano, M.H. Ultsch, A.M. de Vos, and J.A. Wells Convergent solutions to binding at a protein-protein interface Science 287 2000 1279 1283
    • (2000) Science , vol.287 , pp. 1279-1283
    • Delano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 28
    • 39149106011 scopus 로고    scopus 로고
    • Structural characterization of a mutated, ADCC-enhanced human Fc fragment
    • V. Oganesyan, M.M. Damschroder, W. Leach, H. Wu, and W.F. Dall'Acqua Structural characterization of a mutated, ADCC-enhanced human Fc fragment Mol Immunol 45 2008 1872 1882
    • (2008) Mol Immunol , vol.45 , pp. 1872-1882
    • Oganesyan, V.1    Damschroder, M.M.2    Leach, W.3    Wu, H.4    Dall'Acqua, W.F.5
  • 29
    • 33646105366 scopus 로고    scopus 로고
    • Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy
    • Y. Yamaguchi, M. Nishimura, M. Nagano, H. Yagi, H. Sasakawa, and K. Uchida et al. Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy Biochim Biophys Acta Gen Subj 1760 2006 693 700
    • (2006) Biochim Biophys Acta Gen Subj , vol.1760 , pp. 693-700
    • Yamaguchi, Y.1    Nishimura, M.2    Nagano, M.3    Yagi, H.4    Sasakawa, H.5    Uchida, K.6
  • 30
    • 84879775496 scopus 로고    scopus 로고
    • Engineering hydrophobic protein-carbohydrate interactions to fine-tune monoclonal antibodies
    • X. Yu, K. Baruah, D.J. Harvey, S. Vasiljevic, D.S. Alonzi, and B.D. Song et al. Engineering hydrophobic protein-carbohydrate interactions to fine-tune monoclonal antibodies J Am Chem Soc 135 2013 9723 9732
    • (2013) J Am Chem Soc , vol.135 , pp. 9723-9732
    • Yu, X.1    Baruah, K.2    Harvey, D.J.3    Vasiljevic, S.4    Alonzi, D.S.5    Song, B.D.6
  • 31
    • 84884309807 scopus 로고    scopus 로고
    • Crystal structure of sialylated IgG Fc: Implications for the mechanism of intravenous immunoglobulin therapy
    • M. Crispin, X. Yu, and T.A. Bowden Crystal structure of sialylated IgG Fc: implications for the mechanism of intravenous immunoglobulin therapy Proc Natl Acad Sci U S A 110 38 2013 E3544 E3546
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.38
    • Crispin, M.1    Yu, X.2    Bowden, T.A.3
  • 32
    • 84867806174 scopus 로고    scopus 로고
    • Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis
    • T.A. Bowden, K. Baruah, C.H. Coles, D.J. Harvey, X. Yu, and B.D. Song et al. Chemical and structural analysis of an antibody folding intermediate trapped during glycan biosynthesis J Am Chem Soc 134 2012 17554 17563
    • (2012) J Am Chem Soc , vol.134 , pp. 17554-17563
    • Bowden, T.A.1    Baruah, K.2    Coles, C.H.3    Harvey, D.J.4    Yu, X.5    Song, B.D.6
  • 33
    • 63449138097 scopus 로고    scopus 로고
    • Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions
    • M. Crispin, T.A. Bowden, C.H. Coles, K. Harlos, A.R. Aricescu, and D.J. Harvey et al. Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions J Mol Biol 387 2009 1061 1066
    • (2009) J Mol Biol , vol.387 , pp. 1061-1066
    • Crispin, M.1    Bowden, T.A.2    Coles, C.H.3    Harlos, K.4    Aricescu, A.R.5    Harvey, D.J.6
  • 34
    • 84864365553 scopus 로고    scopus 로고
    • Function and 3D structure of the N-glycans on glycoproteins
    • M. Nagae, and Y. Yamaguchi Function and 3D structure of the N-glycans on glycoproteins Int J Mol Sci 13 2012 8398 8429
    • (2012) Int J Mol Sci , vol.13 , pp. 8398-8429
    • Nagae, M.1    Yamaguchi, Y.2
  • 35
  • 36
    • 84879088841 scopus 로고    scopus 로고
    • IgG2 Fc structure and the dynamic features of the IgG CH2-CH3 interface
    • A. Teplyakov, Y. Zhao, T.J. Malia, G. Obmolova, and G.L. Gilliland IgG2 Fc structure and the dynamic features of the IgG CH2-CH3 interface Mol Immunol 56 2013 131 139
    • (2013) Mol Immunol , vol.56 , pp. 131-139
    • Teplyakov, A.1    Zhao, Y.2    Malia, T.J.3    Obmolova, G.4    Gilliland, G.L.5
  • 38
    • 65449120739 scopus 로고    scopus 로고
    • Ramachandran-type plots for glycosidic linkages: Examples from molecular dynamic simulations using the Glycam06 force field
    • A.M. Salisburg, A.L. Deline, K.W. Lexa, G.C. Shields, and K.N. Kirschner Ramachandran-type plots for glycosidic linkages: examples from molecular dynamic simulations using the Glycam06 force field J Comput Chem 30 2009 910 921
    • (2009) J Comput Chem , vol.30 , pp. 910-921
    • Salisburg, A.M.1    Deline, A.L.2    Lexa, K.W.3    Shields, G.C.4    Kirschner, K.N.5
  • 39
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Macromol Crystallogr, Pt. A 276 1997 307 326
    • (1997) Macromol Crystallogr, Pt. A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 41
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • A.T. Brunger Version 1.2 of the Crystallography and NMR system Nat Protoc 2 2007 2728 2733
    • (2007) Nat Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 45
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • V. Hornak, R. Abel, A. Okur, B. Strockbine, A. Roitberg, and C. Simmerling Comparison of multiple Amber force fields and development of improved protein backbone parameters Proteins 65 2006 712 725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 47
    • 84860767348 scopus 로고    scopus 로고
    • Routine microsecond molecular dynamics simulations with AMBER on GPUs. 1. Generalized Born
    • A.W. Gotz, M.J. Williamson, D. Xu, D. Poole, S. Le Grand, and R.C. Walker Routine microsecond molecular dynamics simulations with AMBER on GPUs. 1. Generalized Born J Chem Theory Comput 8 2012 1542 1555
    • (2012) J Chem Theory Comput , vol.8 , pp. 1542-1555
    • Gotz, A.W.1    Williamson, M.J.2    Xu, D.3    Poole, D.4    Le Grand, S.5    Walker, R.C.6
  • 48
    • 84868214675 scopus 로고    scopus 로고
    • SPFP: Speed without compromise - A mixed precision model for GPU accelerated molecular dynamics simulations
    • S. Le Grand, A.W. Götz, and R.C. Walker SPFP: speed without compromise - a mixed precision model for GPU accelerated molecular dynamics simulations Comput Phys Commun 184 2013 374 380
    • (2013) Comput Phys Commun , vol.184 , pp. 374-380
    • Le Grand, S.1    Götz, A.W.2    Walker, R.C.3
  • 50
    • 48749148224 scopus 로고
    • Rattle: A 'velocity' version of the shake algorithm for molecular dynamics calculations
    • H.C. Andersen Rattle: a 'velocity' version of the shake algorithm for molecular dynamics calculations J Comput Phys 52 1983
    • (1983) J Comput Phys , vol.52
    • Andersen, H.C.1
  • 51
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N log (N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald: an N log (N) method for Ewald sums in large systems J Chem Phys 98 1993 10089 10092
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 53
    • 13444283836 scopus 로고    scopus 로고
    • Carbohydrate Structure Suite (CSS): Analysis of carbohydrate 3D structures derived from the PDB
    • T. Lutteke, M. Frank, and C.W. von der Lieth Carbohydrate Structure Suite (CSS): analysis of carbohydrate 3D structures derived from the PDB Nucleic Acids Res 33 2005 D242 D246
    • (2005) Nucleic Acids Res , vol.33
    • Lutteke, T.1    Frank, M.2    Von Der Lieth, C.W.3


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