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Volumn 44, Issue 7, 2007, Pages 1524-1534

Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality

Author keywords

Antibodies; Antibody dependent cellular cytotoxicity; Fc receptors; Glycosylation; Sialic acid

Indexed keywords

FC RECEPTOR; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G ANTIBODY; MEMBRANE ANTIGEN; MONOCLONAL ANTIBODY; SIALIC ACID;

EID: 33751253486     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2006.09.005     Document Type: Article
Times cited : (342)

References (36)
  • 1
    • 0029115046 scopus 로고
    • Rapid quantitative determination of sialic acids in glycoproteins by high-performance liquid chromatography with a sensitive fluorescence detection
    • Anumula K.R. Rapid quantitative determination of sialic acids in glycoproteins by high-performance liquid chromatography with a sensitive fluorescence detection. Anal. Biochem. 230 (1995) 24-30
    • (1995) Anal. Biochem. , vol.230 , pp. 24-30
    • Anumula, K.R.1
  • 2
    • 0030596512 scopus 로고    scopus 로고
    • Time-resolved fluorometric assay for natural killer activity using target cells labeled with a fluorescence enhancing ligand
    • Blomberg K., Hautala R., Lovgren J., Mukkala V.-M., Lindqvist C., and Akerman L. Time-resolved fluorometric assay for natural killer activity using target cells labeled with a fluorescence enhancing ligand. J. Immunol. Meth. 193 (1996) 199-206
    • (1996) J. Immunol. Meth. , vol.193 , pp. 199-206
    • Blomberg, K.1    Hautala, R.2    Lovgren, J.3    Mukkala, V.-M.4    Lindqvist, C.5    Akerman, L.6
  • 3
    • 0029558207 scopus 로고
    • The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H
    • Boyd P.N., Lines A.C., and Patel A.K. The effect of the removal of sialic acid, galactose and total carbohydrate on the functional activity of Campath-1H. Mol. Immunol. 32 (1995) 1311-1318
    • (1995) Mol. Immunol. , vol.32 , pp. 1311-1318
    • Boyd, P.N.1    Lines, A.C.2    Patel, A.K.3
  • 4
    • 0036464719 scopus 로고    scopus 로고
    • Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene
    • Cartron G., Dacheux L., Salles G., Solal-Celigny P., Bardos P., Colombat P., and Watier H. Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene. Blood 99 (2002) 754-758
    • (2002) Blood , vol.99 , pp. 754-758
    • Cartron, G.1    Dacheux, L.2    Salles, G.3    Solal-Celigny, P.4    Bardos, P.5    Colombat, P.6    Watier, H.7
  • 5
    • 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
    • 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-Å resolution. Biochemistry 20 (1981) 2361-2370
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 7
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcγRIIIa Asn-162: an element required for high affinity binding to non-fucosylated IgG glycoforms
    • Ferrara C., Stuart F., Sondermann P., Brünker P., and Umaña P. The carbohydrate at FcγRIIIa Asn-162: an element required for high affinity binding to non-fucosylated IgG glycoforms. J. Biol. Chem. 281 (2006) 5032-5036
    • (2006) J. Biol. Chem. , vol.281 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3    Brünker, P.4    Umaña, P.5
  • 9
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • Hodoniczky J., Zheng Y.Z., and James D.C. Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro. Biotechnol. Prog. 21 (2005) 1644-1652
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1644-1652
    • Hodoniczky, J.1    Zheng, Y.Z.2    James, D.C.3
  • 10
    • 0017152608 scopus 로고
    • Crystallographic structure studies of an IgG molecule and an Fc fragment
    • Huber R., Deisenhofer J., Colman P.M., Matsushima M., and Palm W. Crystallographic structure studies of an IgG molecule and an Fc fragment. Nature 264 (1976) 415-420
    • (1976) Nature , vol.264 , pp. 415-420
    • Huber, R.1    Deisenhofer, J.2    Colman, P.M.3    Matsushima, M.4    Palm, W.5
  • 12
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol. Prog. 21 (2005) 11-16
    • (2005) Biotechnol. Prog. , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 13
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y., Nimmerjahn F., and Ravetch J.V. 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
  • 15
    • 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., and Sondermann P. 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
  • 16
    • 0028670916 scopus 로고
    • Galactosylation of human IgG monoclonal anti-D produced by EBV-transformed B-lymphoblastoid cell lines is dependent on culture method and affects Fc receptor-mediated functional activity
    • Kumpel B.M., Rademacher T.W., Rook G.A.W., Williams P.J., and Wilson I.B.H. Galactosylation of human IgG monoclonal anti-D produced by EBV-transformed B-lymphoblastoid cell lines is dependent on culture method and affects Fc receptor-mediated functional activity. Hum. Antibod. Hybrid. 5 (1994) 143-151
    • (1994) Hum. Antibod. Hybrid. , vol.5 , pp. 143-151
    • Kumpel, B.M.1    Rademacher, T.W.2    Rook, G.A.W.3    Williams, P.J.4    Wilson, I.B.H.5
  • 17
    • 0021866261 scopus 로고
    • Effector functions of monoclonal aglycosylated mouse IgG2a: binding and activation of complement component C1 and interaction with human Fc receptor
    • Leatherbarrow R.J., Rademacher T.W., Dwek R.A., Woof J.M., Clark A., Burton D.R., Richardson R., and Feinstein A. Effector functions of monoclonal aglycosylated mouse IgG2a: binding and activation of complement component C1 and interaction with human Fc receptor. Mol. Immunol. 22 (1985) 407-415
    • (1985) Mol. Immunol. , vol.22 , pp. 407-415
    • Leatherbarrow, R.J.1    Rademacher, T.W.2    Dwek, R.A.3    Woof, J.M.4    Clark, A.5    Burton, D.R.6    Richardson, R.7    Feinstein, A.8
  • 18
    • 0030470557 scopus 로고    scopus 로고
    • Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fcγ receptor I and influence the synthesis of its oligosaccharide chains
    • Lund J., Takahashi N., Pound J.D., Goodall M., and Jefferis R. Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fcγ receptor I and influence the synthesis of its oligosaccharide chains. J. Immunol. 157 (1996) 4963-4969
    • (1996) J. Immunol. , vol.157 , pp. 4963-4969
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Jefferis, R.5
  • 19
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms
    • Mimura Y., Church S., Ghirlando R., Ashton P.R., Dong S., Goodall M., Lund J., and Jefferis R. The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms. Mol. Immunol. 37 (2000) 697-706
    • (2000) Mol. Immunol. , vol.37 , pp. 697-706
    • Mimura, Y.1    Church, S.2    Ghirlando, R.3    Ashton, P.R.4    Dong, S.5    Goodall, M.6    Lund, J.7    Jefferis, R.8
  • 20
    • 0021041854 scopus 로고
    • Biological significance of carbohydrate chains on monoclonal antibodies
    • Nose M., and Wigzell H. Biological significance of carbohydrate chains on monoclonal antibodies. Proc. Natl. Acad. Sci. U.S.A. 80 (1983) 6632-6636
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 6632-6636
    • Nose, M.1    Wigzell, H.2
  • 21
    • 0030587060 scopus 로고    scopus 로고
    • Analysis of acidic oligosaccharides and glycopeptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Papac D.I., Wong A., and Jones A.J. Analysis of acidic oligosaccharides and glycopeptides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal. Chem. 68 (1996) 3215-3223
    • (1996) Anal. Chem. , vol.68 , pp. 3215-3223
    • Papac, D.I.1    Wong, A.2    Jones, A.J.3
  • 22
    • 0031799347 scopus 로고    scopus 로고
    • A high-throughput microscale method to release N-linked oligosaccharides from glycoproteins for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis
    • Papac D.I., Briggs J.B., Chin E.T., and Jones A.J. A high-throughput microscale method to release N-linked oligosaccharides from glycoproteins for matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis. Glycobiology 8 (1998) 445-454
    • (1998) Glycobiology , vol.8 , pp. 445-454
    • Papac, D.I.1    Briggs, J.B.2    Chin, E.T.3    Jones, A.J.4
  • 23
    • 25644449032 scopus 로고    scopus 로고
    • Glycosylation variations with expression systems
    • Raju T.S. Glycosylation variations with expression systems. BioProcess Int. 1 (2003) 44-53
    • (2003) BioProcess Int. , vol.1 , pp. 44-53
    • Raju, T.S.1
  • 24
    • 0035979377 scopus 로고    scopus 로고
    • Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal N-acetylglucosamine and galactose residues
    • Raju T.S., Briggs J.B., Chamow S.M., Winkler M.E., and Jones A.J.S. 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.S.5
  • 25
    • 0034050074 scopus 로고    scopus 로고
    • Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics
    • Raju T.S., Briggs J.B., Borge S.M., and Jones A.J. Species-specific variation in glycosylation of IgG: evidence for the species-specific sialylation and branch-specific galactosylation and importance for engineering recombinant glycoprotein therapeutics. Glycobiology 10 (2000) 477-486
    • (2000) Glycobiology , vol.10 , pp. 477-486
    • Raju, T.S.1    Briggs, J.B.2    Borge, S.M.3    Jones, A.J.4
  • 26
    • 0027992647 scopus 로고
    • Role of sialic acid on the viscosity of canine tracheal mucin glycoprotein
    • Raju T.S., and Davidson E.A. Role of sialic acid on the viscosity of canine tracheal mucin glycoprotein. Biochem. Biophys. Res. Commun. 205 (1994) 402-409
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 402-409
    • Raju, T.S.1    Davidson, E.A.2
  • 27
    • 31744447070 scopus 로고    scopus 로고
    • Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain
    • Raju T.S., and Scallon B.J. Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain. Biochem. Biophys. Res. Commun. 341 (2006) 797-803
    • (2006) Biochem. Biophys. Res. Commun. , vol.341 , pp. 797-803
    • Raju, T.S.1    Scallon, B.J.2
  • 28
    • 0003936557 scopus 로고    scopus 로고
    • Robinson J.P., Darzynkiewiez A., Dean P.H., et al. (Eds), John Wiley & Sons, New York p. 5.1.3
    • In: Robinson J.P., Darzynkiewiez A., Dean P.H., et al. (Eds). Current Protocols in Cytometry vol. 1 (2001), John Wiley & Sons, New York p. 5.1.3
    • (2001) Current Protocols in Cytometry , vol.1
  • 29
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity
    • Shields R.L., Lai J., Keck R., O'Connell L.Y., Hong K., Meng Y.G., Weikert S.H.A., and Presta L.G. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277 (2003) 26733-26740
    • (2003) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Meng, Y.G.6    Weikert, S.H.A.7    Presta, L.G.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., and 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. 278 (2003) 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
    • 0035827222 scopus 로고    scopus 로고
    • Molecular basis of immune complex recognition: a comparison of Fc-receptor structures
    • Sondermann P., Kaiser J., and Jacob U. Molecular basis of immune complex recognition: a comparison of Fc-receptor structures. J. Mol. Biol. 309 (2001) 737-749
    • (2001) J. Mol. Biol. , vol.309 , pp. 737-749
    • Sondermann, P.1    Kaiser, J.2    Jacob, U.3
  • 32
    • 0024438061 scopus 로고
    • Studies of aglycosylated chimeric mouse-human IgG: role of carbohydrate in the structure and effector functions mediated by the human IgG constant region
    • Tao M.-H., and Morrison S.L. Studies of aglycosylated chimeric mouse-human IgG: role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. J. Immunol. 143 (1989) 2595-2601
    • (1989) J. Immunol. , vol.143 , pp. 2595-2601
    • Tao, M.-H.1    Morrison, S.L.2
  • 33
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Umaña P., Jean-Mairet J., Moudry R., Amstutz H., and Bailey J. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat. Biotech. 17 (1999) 176-180
    • (1999) Nat. Biotech. , vol.17 , pp. 176-180
    • Umaña, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.5
  • 34
    • 0021364466 scopus 로고
    • The release and purification of sialic acids from glycoconjugates: methods to minimize the loss and migration of O-acetyl groups
    • Varki A., and Diaz S. The release and purification of sialic acids from glycoconjugates: methods to minimize the loss and migration of O-acetyl groups. Anal. Biochem. 137 (1984) 236-247
    • (1984) Anal. Biochem. , vol.137 , pp. 236-247
    • Varki, A.1    Diaz, S.2
  • 35
    • 0032055988 scopus 로고    scopus 로고
    • Effect of C2-associated carbohydrate structure on Ig effector function: studies with chimeric mouse-human IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells
    • Wright A., and Morrison S.L. Effect of C2-associated carbohydrate structure on Ig effector function: studies with chimeric mouse-human IgG1 antibodies in glycosylation mutants of Chinese hamster ovary cells. J. Immunol. 160 (1998) 3393-3402
    • (1998) J. Immunol. , vol.160 , pp. 3393-3402
    • Wright, A.1    Morrison, S.L.2


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