메뉴 건너뛰기




Volumn 7, Issue 21, 2016, Pages 31166-31176

Fractionation of Fab glycosylated immunoglobulin G with concanavalin A chromatography unveils new structural properties of the molecule

Author keywords

Asymmetry; ConA; Glycosylation; IgG; Symmetry

Indexed keywords

ASPARAGINE; ASPARAGINE LINKED OLIGOSACCHARIDE; CONCANAVALIN A; FC RECEPTOR; IMMUNOGLOBULIN F(AB) FRAGMENT; LECTIN; IMMUNOGLOBULIN G;

EID: 84971500848     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.9085     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol Prog. 2005; 21:11-16.
    • (2005) Biotechnol Prog , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 2
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J Mol Biol. 2003; 325:979-989.
    • (2003) J Mol Biol , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 3
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol. 2007; 25:21-50.
    • (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
  • 4
    • 33646093725 scopus 로고    scopus 로고
    • Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis
    • Holland M, Yagi H, Takahashi N, Kato K, Savage CO, Goodall DM, Jefferis R. Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA-associated systemic vasculitis. Biochim Biophys Acta. 2006; 1760:669-677.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 669-677
    • Holland, M.1    Yagi, H.2    Takahashi, N.3    Kato, K.4    Savage, C.O.5    Goodall, D.M.6    Jefferis, R.7
  • 5
    • 77956187222 scopus 로고    scopus 로고
    • Analytical and Functional Aspects of Antibody Sialylation
    • Stadlmann J, Pabst M, Altmann F. Analytical and Functional Aspects of Antibody Sialylation. J Clin Immunol. 2010; 30:S15-9.
    • (2010) J Clin Immunol , vol.30 , pp. S15-S19
    • Stadlmann, J.1    Pabst, M.2    Altmann, F.3
  • 6
    • 0014823629 scopus 로고
    • Attachment of carbohydrate to the variable region of myeloma immunoglobulin light chains
    • Sox HC, Jr, Hood L. Attachment of carbohydrate to the variable region of myeloma immunoglobulin light chains. Proc Natl Acad Sci U S A. 1970; 66:975-982.
    • (1970) Proc Natl Acad Sci U S A , vol.66 , pp. 975-982
    • Sox, H.C.1    Hood, L.2
  • 7
    • 0034328791 scopus 로고    scopus 로고
    • Antigen binding of an ovomucoid-specific antibody is affected by a carbohydrate chain located on the light chain variable region
    • Fujimura Y, Tachibana H, Eto N, Yamada K. Antigen binding of an ovomucoid-specific antibody is affected by a carbohydrate chain located on the light chain variable region. Biosci Biotechnol Biochem. 2000; 64:2298-2305.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 2298-2305
    • Fujimura, Y.1    Tachibana, H.2    Eto, N.3    Yamada, K.4
  • 8
    • 0025909201 scopus 로고
    • Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure
    • Wright A, Tao MH, Kabat EA, Morrison SL. Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure. EMBO J. 1991; 10:2717-2723.
    • (1991) EMBO J , vol.10 , pp. 2717-2723
    • Wright, A.1    Tao, M.H.2    Kabat, E.A.3    Morrison, S.L.4
  • 9
    • 0033558335 scopus 로고    scopus 로고
    • Position effects of variable region carbohydrate on the affinity and in vivo behavior of an anti-(1->6) dextran antibody
    • Coloma MJ, Trinh RK, Martinez AR, Morrison SL. Position effects of variable region carbohydrate on the affinity and in vivo behavior of an anti-(1->6) dextran antibody. J Immunol. 1999; 162:2162-2170.
    • (1999) J Immunol , vol.162 , pp. 2162-2170
    • Coloma, M.J.1    Trinh, R.K.2    Martinez, A.R.3    Morrison, S.L.4
  • 10
    • 0029962752 scopus 로고    scopus 로고
    • Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients
    • Youings A, Chang SC, Dwek RA, Scragg IG. Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients. Biochem J. 1996; 314:621-630.
    • (1996) Biochem J , vol.314 , pp. 621-630
    • Youings, A.1    Chang, S.C.2    Dwek, R.A.3    Scragg, I.G.4
  • 11
    • 34548409568 scopus 로고    scopus 로고
    • Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry
    • Mimura Y, Ashton PR, Takahashi N, Harvey DJ, Jefferis R. Contrasting glycosylation profiles between Fab and Fc of a human IgG protein studied by electrospray ionization mass spectrometry. J Immunol Methods. 2007; 326:116-126.
    • (2007) J Immunol Methods , vol.326 , pp. 116-126
    • Mimura, Y.1    Ashton, P.R.2    Takahashi, N.3    Harvey, D.J.4    Jefferis, R.5
  • 13
    • 0026522617 scopus 로고
    • Immobilized lectin columns: useful tools for the fractionation and structural analysis of oligosaccharides
    • Kobata A, Endo T. Immobilized lectin columns: useful tools for the fractionation and structural analysis of oligosaccharides. J Chromatogr. 1992; 597:111-122.
    • (1992) J Chromatogr , vol.597 , pp. 111-122
    • Kobata, A.1    Endo, T.2
  • 14
    • 0014944053 scopus 로고
    • Localization of the carbohydrate within the variable region of light and heavy chains of human gamma g myeloma proteins
    • Spiegelberg HL, Abel CA, Fishkin BG, Grey HM. Localization of the carbohydrate within the variable region of light and heavy chains of human gamma g myeloma proteins. Biochemistry. 1970; 9:4217-4223.
    • (1970) Biochemistry , vol.9 , pp. 4217-4223
    • Spiegelberg, H.L.1    Abel, C.A.2    Fishkin, B.G.3    Grey, H.M.4
  • 15
    • 65349144223 scopus 로고    scopus 로고
    • Immunoglobulin expression in nonlymphoid lineage and neoplastic cells
    • Chen Z, Qiu X, Gu J. Immunoglobulin expression in nonlymphoid lineage and neoplastic cells. Am J Pathol. 2009; 174:1139-1148.
    • (2009) Am J Pathol , vol.174 , pp. 1139-1148
    • Chen, Z.1    Qiu, X.2    Gu, J.3
  • 16
    • 0027198490 scopus 로고
    • Antibody variable region glycosylation: biochemical and clinical effects
    • Wright A, Morrison SL. Antibody variable region glycosylation: biochemical and clinical effects. Springer Semin Immunopathol. 1993; 15:259-273.
    • (1993) Springer Semin Immunopathol , vol.15 , pp. 259-273
    • Wright, A.1    Morrison, S.L.2
  • 17
    • 0023080492 scopus 로고
    • Fractionation and structural assessment of oligosaccharides and glycopeptides by use of immobilized lectins
    • Osawa T, Tsuji T. Fractionation and structural assessment of oligosaccharides and glycopeptides by use of immobilized lectins. Annu Rev Biochem. 1987; 56:21-42.
    • (1987) Annu Rev Biochem , vol.56 , pp. 21-42
    • Osawa, T.1    Tsuji, T.2
  • 19
    • 0024278423 scopus 로고
    • The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked alpha-2, 3 to penultimate galactose residues
    • Wang WC, Cummings RD. The immobilized leukoagglutinin from the seeds of Maackia amurensis binds with high affinity to complex-type Asn-linked oligosaccharides containing terminal sialic acid-linked alpha-2, 3 to penultimate galactose residues. J Biol Chem. 1988; 263:4576-4585.
    • (1988) J Biol Chem , vol.263 , pp. 4576-4585
    • Wang, W.C.1    Cummings, R.D.2
  • 20
    • 0024286486 scopus 로고
    • Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb
    • Shibuya N, Goldstein IJ, Van Damme EJ, Peumans WJ. Binding properties of a mannose-specific lectin from the snowdrop (Galanthus nivalis) bulb. J Biol Chem. 1988; 263:728-734.
    • (1988) J Biol Chem , vol.263 , pp. 728-734
    • Shibuya, N.1    Goldstein, I.J.2    Van Damme, E.J.3    Peumans, W.J.4
  • 21
  • 22
    • 0001697163 scopus 로고
    • Protein-Carbohydrate Interaction. Ii. Inhibition Studies on the Interaction of Concanavalin a with Polysaccharides
    • Goldstein IJ, Hollerman CE, Smith EE. Protein-Carbohydrate Interaction. Ii. Inhibition Studies on the Interaction of Concanavalin a with Polysaccharides. Biochemistry. 1965; 4:876-883.
    • (1965) Biochemistry , vol.4 , pp. 876-883
    • Goldstein, I.J.1    Hollerman, C.E.2    Smith, E.E.3
  • 23
    • 0016694206 scopus 로고
    • Three-dimensional structure, function and genetic control of immunoglobulins
    • Poljak RJ. Three-dimensional structure, function and genetic control of immunoglobulins. Nature. 1975; 256:373-376.
    • (1975) Nature , vol.256 , pp. 373-376
    • Poljak, R.J.1
  • 24
    • 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-A resolution
    • Deisenhofer J. 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-A resolution. Biochemistry. 1981; 20:2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 26
    • 33751253486 scopus 로고    scopus 로고
    • Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality
    • Scallon BJ, Tam SH, McCarthy SG, Cai AN, Raju TS. Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol Immunol. 2007; 44:1524-1534.
    • (2007) Mol Immunol , vol.44 , pp. 1524-1534
    • Scallon, B.J.1    Tam, S.H.2    McCarthy, S.G.3    Cai, A.N.4    Raju, T.S.5
  • 28
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science. 2006; 313:670-673.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 29
    • 28444437100 scopus 로고    scopus 로고
    • Fucose removal from complex-type oligosaccharide enhances the antibody-dependent cellular cytotoxicity of single-geneencoded antibody comprising a single-chain antibody linked the antibody constant region
    • Natsume A, Wakitani M, Yamane-Ohnuki N, Shoji-Hosaka E, Niwa R, Uchida K, Satoh M, Shitara K. Fucose removal from complex-type oligosaccharide enhances the antibody-dependent cellular cytotoxicity of single-geneencoded antibody comprising a single-chain antibody linked the antibody constant region. J Immunol Methods. 2005; 306:93-103.
    • (2005) J Immunol Methods , vol.306 , pp. 93-103
    • Natsume, A.1    Wakitani, M.2    Yamane-Ohnuki, N.3    Shoji-Hosaka, E.4    Niwa, R.5    Uchida, K.6    Satoh, M.7    Shitara, K.8
  • 30
    • 0037474276 scopus 로고    scopus 로고
    • The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity
    • Shinkawa T, Nakamura K, Yamane N, Shoji-Hosaka E, Kanda Y, Sakurada M, Uchida K, Anazawa H, Satoh M, Yamasaki M, Hanai N, Shitara K. The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J Biol Chem. 2003; 278:3466-3473.
    • (2003) J Biol Chem , vol.278 , pp. 3466-3473
    • Shinkawa, T.1    Nakamura, K.2    Yamane, N.3    Shoji-Hosaka, E.4    Kanda, Y.5    Sakurada, M.6    Uchida, K.7    Anazawa, H.8    Satoh, M.9    Yamasaki, M.10    Hanai, N.11    Shitara, K.12
  • 31
    • 68249103612 scopus 로고    scopus 로고
    • Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins
    • Takahashi M, Kuroki Y, Ohtsubo K, Taniguchi N. Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins. Carbohydr Res. 2009; 344:1387-1390.
    • (2009) Carbohydr Res , vol.344 , pp. 1387-1390
    • Takahashi, M.1    Kuroki, Y.2    Ohtsubo, K.3    Taniguchi, N.4
  • 32
    • 34247215987 scopus 로고    scopus 로고
    • Enhanced binding affinity for FcgammaRIIIa of fucose-negative antibody is sufficient to induce maximal antibody-dependent cellular cytotoxicity
    • Masuda K, Kubota T, Kaneko E, Iida S, Wakitani M, Kobayashi-Natsume Y, Kubota A, Shitara K, Nakamura K. Enhanced binding affinity for FcgammaRIIIa of fucose-negative antibody is sufficient to induce maximal antibody-dependent cellular cytotoxicity. Mol Immunol. 2007; 44:3122-3131.
    • (2007) Mol Immunol , vol.44 , pp. 3122-3131
    • Masuda, K.1    Kubota, T.2    Kaneko, E.3    Iida, S.4    Wakitani, M.5    Kobayashi-Natsume, Y.6    Kubota, A.7    Shitara, K.8    Nakamura, K.9
  • 33
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • Malhotra R, Wormald MR, Rudd PM, Fischer PB, Dwek RA, Sim RB. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nat Med. 1995; 1:237-243.
    • (1995) Nat Med , vol.1 , pp. 237-243
    • Malhotra, R.1    Wormald, M.R.2    Rudd, P.M.3    Fischer, P.B.4    Dwek, R.A.5    Sim, R.B.6
  • 36
    • 84885204309 scopus 로고    scopus 로고
    • Association between galactosylation of immunoglobulin G and improvement of rheumatoid arthritis during pregnancy is independent of sialylation
    • Bondt A, Selman MH, Deelder AM, Hazes JM, Willemsen SP, Wuhrer M, Dolhain RJ. Association between galactosylation of immunoglobulin G and improvement of rheumatoid arthritis during pregnancy is independent of sialylation. J Proteome Res. 2013; 12:4522-4531.
    • (2013) J Proteome Res , vol.12 , pp. 4522-4531
    • Bondt, A.1    Selman, M.H.2    Deelder, A.M.3    Hazes, J.M.4    Willemsen, S.P.5    Wuhrer, M.6    Dolhain, R.J.7
  • 37
    • 0023912648 scopus 로고
    • Agerelated galactosylation of the N-linked oligosaccharides of human serum IgG
    • Parekh R, Roitt I, Isenberg D, Dwek R, Rademacher T. Agerelated galactosylation of the N-linked oligosaccharides of human serum IgG. J Exp Med. 1988; 167:1731-1736.
    • (1988) J Exp Med , vol.167 , pp. 1731-1736
    • Parekh, R.1    Roitt, I.2    Isenberg, D.3    Dwek, R.4    Rademacher, T.5
  • 39
    • 0030996004 scopus 로고    scopus 로고
    • Structural changes of immunoglobulin G oligosaccharides with age in healthy human serum
    • Yamada E, Tsukamoto Y, Sasaki R, Yagyu K, Takahashi N. Structural changes of immunoglobulin G oligosaccharides with age in healthy human serum. Glycoconj J. 1997; 14:401-405.
    • (1997) Glycoconj J , vol.14 , pp. 401-405
    • Yamada, E.1    Tsukamoto, Y.2    Sasaki, R.3    Yagyu, K.4    Takahashi, N.5
  • 40
    • 84872754818 scopus 로고    scopus 로고
    • Analysis and functional consequences of increased Fab-sialylation of intravenous immunoglobulin (IVIG) after lectin fractionation
    • Kasermann F, Boerema DJ, Ruegsegger M, Hofmann A, Wymann S, Zuercher AW, Miescher S. Analysis and functional consequences of increased Fab-sialylation of intravenous immunoglobulin (IVIG) after lectin fractionation. PLoS One. 2012; 7:e37243.
    • (2012) PLoS One , vol.7
    • Kasermann, F.1    Boerema, D.J.2    Ruegsegger, M.3    Hofmann, A.4    Wymann, S.5    Zuercher, A.W.6    Miescher, S.7
  • 42
    • 0024214849 scopus 로고
    • The primary structure of the variable region of an immunoglobin IV light-chain amyloid-fibril protein (AL GIL)
    • Fykse EM, Sletten K, Husby G, Cornwell GG, 3rd. The primary structure of the variable region of an immunoglobin IV light-chain amyloid-fibril protein (AL GIL). The Biochem J. 1988; 256:973-980.
    • (1988) The Biochem J , vol.256 , pp. 973-980
    • Fykse, E.M.1    Sletten, K.2    Husby, G.3    Cornwell, G.G.4
  • 43
    • 0022826741 scopus 로고
    • Structural studies of a carbohydrate-containing immunoglobulin-lambda-lightchain amyloid-fibril protein (AL) of variable subgroup III
    • Holm E, Sletten K, Husby G. Structural studies of a carbohydrate-containing immunoglobulin-lambda-lightchain amyloid-fibril protein (AL) of variable subgroup III. Biochem J. 1986; 239:545-551.
    • (1986) Biochem J , vol.239 , pp. 545-551
    • Holm, E.1    Sletten, K.2    Husby, G.3
  • 44
    • 0022400442 scopus 로고
    • The amino acid sequence of a carbohydrate-containing immunoglobulinlight-chain-type amyloid-fibril protein
    • Tveteraas T, Sletten K, Westermark P. The amino acid sequence of a carbohydrate-containing immunoglobulinlight-chain-type amyloid-fibril protein. Biochem J. 1985; 232:183-190.
    • (1985) Biochem J , vol.232 , pp. 183-190
    • Tveteraas, T.1    Sletten, K.2    Westermark, P.3
  • 45
    • 2142813035 scopus 로고    scopus 로고
    • V region carbohydrate and antibody expression
    • Gala FA, Morrison SL. V region carbohydrate and antibody expression. J Immunol. 2004; 172:5489-5494.
    • (2004) J Immunol , vol.172 , pp. 5489-5494
    • Gala, F.A.1    Morrison, S.L.2
  • 46
    • 84910647104 scopus 로고    scopus 로고
    • Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes
    • Bondt A, Rombouts Y, Selman MH, Hensbergen PJ, Reiding KR, Hazes JM, Dolhain RJ, Wuhrer M. Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes. Mol Cell Proteomics. 2014; 13:3029-3039.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 3029-3039
    • Bondt, A.1    Rombouts, Y.2    Selman, M.H.3    Hensbergen, P.J.4    Reiding, K.R.5    Hazes, J.M.6    Dolhain, R.J.7    Wuhrer, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.