메뉴 건너뛰기




Volumn 417, Issue , 2015, Pages 34-44

A method for high-throughput, sensitive analysis of IgG Fc and Fab glycosylation by capillary electrophoresis

Author keywords

Capillary electrophoresis; Fc separation; Glycan analysis; IgG N glycosylation

Indexed keywords

GLYCAN; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN FC FRAGMENT; GLYCOSYLATED IGG; IMMUNOGLOBULIN G; POLYSACCHARIDE;

EID: 84922990828     PISSN: 00221759     EISSN: 18727905     Source Type: Journal    
DOI: 10.1016/j.jim.2014.12.004     Document Type: Article
Times cited : (89)

References (42)
  • 1
    • 84877316930 scopus 로고    scopus 로고
    • Enhanced phagocytic activity of HIV-specific antibodies correlates with natural production of immunoglobulins with skewed affinity for FcγR2a and FcγR2b
    • Ackerman M., Dugast A.-S., McAndrew E.G., Tsoukas S., Licht A.F., Irvine D.J., Alter G. Enhanced phagocytic activity of HIV-specific antibodies correlates with natural production of immunoglobulins with skewed affinity for FcγR2a and FcγR2b. J. Virol. 2013, 87:5468. 10.1128/JVI. 03403-12.
    • (2013) J. Virol. , vol.87 , pp. 5468
    • Ackerman, M.1    Dugast, A.-S.2    McAndrew, E.G.3    Tsoukas, S.4    Licht, A.F.5    Irvine, D.J.6    Alter, G.7
  • 3
    • 0035955637 scopus 로고    scopus 로고
    • A second uniquely human mutation affecting sialic acid biology
    • Angata T., Varki N.M., Varki A. A second uniquely human mutation affecting sialic acid biology. J. Biol. Chem. 2001, 276:40282. 10.1074/jbc.M105926200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40282
    • Angata, T.1    Varki, N.M.2    Varki, A.3
  • 4
    • 77956185954 scopus 로고    scopus 로고
    • A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs
    • Anthony R.M., Ravetch J.V. A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs. J. Clin. Immunol. 2010, 30(Suppl. 1):S9. 10.1007/s10875-010-9405-6.
    • (2010) J. Clin. Immunol. , vol.30 , pp. S9
    • Anthony, R.M.1    Ravetch, J.V.2
  • 5
    • 84863570384 scopus 로고    scopus 로고
    • Quantitative glycan profiling of normal human plasma derived immunoglobulin and its fragments Fab and Fc
    • Anumula K.R. Quantitative glycan profiling of normal human plasma derived immunoglobulin and its fragments Fab and Fc. J. Immunol. Methods 2012, 382:167. 10.1016/j.jim.2012.05.022.
    • (2012) J. Immunol. Methods , vol.382 , pp. 167
    • Anumula, K.R.1
  • 6
    • 79956107362 scopus 로고    scopus 로고
    • Antibody-dependent cell-mediated viral inhibition emerges after simian immunodeficiency virus SIVmac251 infection of rhesus monkeys coincident with gp140-binding antibodies and is effective against neutralization-resistant viruses
    • Asmal M., Sun Y., Lane S., Yeh W., Schmidt S.D., Mascola J.R., Letvin N.L. Antibody-dependent cell-mediated viral inhibition emerges after simian immunodeficiency virus SIVmac251 infection of rhesus monkeys coincident with gp140-binding antibodies and is effective against neutralization-resistant viruses. J. Virol. 2011, 85:5465. 10.1128/JVI. 00313-11.
    • (2011) J. Virol. , vol.85 , pp. 5465
    • Asmal, M.1    Sun, Y.2    Lane, S.3    Yeh, W.4    Schmidt, S.D.5    Mascola, J.R.6    Letvin, N.L.7
  • 7
    • 84866104409 scopus 로고    scopus 로고
    • The role of sialic acid as a modulator of the anti-inflammatory activity of IgG
    • Böhm S., Schwab I., Lux A., Nimmerjahn F. The role of sialic acid as a modulator of the anti-inflammatory activity of IgG. Semin. Immunopathol. 2012, 34:443. 10.1007/s00281-012-0308-x.
    • (2012) Semin. Immunopathol. , vol.34 , pp. 443
    • Böhm, S.1    Schwab, I.2    Lux, A.3    Nimmerjahn, F.4
  • 9
    • 0034948464 scopus 로고    scopus 로고
    • Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment
    • Callewaert N., Geysens S., Molemans F., Contreras R. Ultrasensitive profiling and sequencing of N-linked oligosaccharides using standard DNA-sequencing equipment. Glycobiology 2001, 11:275.
    • (2001) Glycobiology , vol.11 , pp. 275
    • Callewaert, N.1    Geysens, S.2    Molemans, F.3    Contreras, R.4
  • 10
    • 84862826701 scopus 로고    scopus 로고
    • Human IgG Fc-glycosylation profiling reveals associations with age, sex, female sex hormones and thyroid cancer
    • Chen G., Wang Y., Qiu L., Qin X., Liu H., Wang X., Wang Y., Song G., Li F., Guo Y., Li F., Guo S., Li Z. Human IgG Fc-glycosylation profiling reveals associations with age, sex, female sex hormones and thyroid cancer. J. Proteome 2012, 75:2824. 10.1016/j.jprot.2012.02.001.
    • (2012) J. Proteome , vol.75 , pp. 2824
    • Chen, G.1    Wang, Y.2    Qiu, L.3    Qin, X.4    Liu, H.5    Wang, X.6    Wang, Y.7    Song, G.8    Li, F.9    Guo, Y.10    Li, F.11    Guo, S.12    Li, Z.13
  • 12
    • 84880708189 scopus 로고    scopus 로고
    • The carbohydrate switch between pathogenic and immunosuppressive antigen-specific antibodies
    • Collin M., Ehlers M. The carbohydrate switch between pathogenic and immunosuppressive antigen-specific antibodies. Exp. Dermatol. 2013, 22:511. 10.1111/exd.12171.
    • (2013) Exp. Dermatol. , vol.22 , pp. 511
    • Collin, M.1    Ehlers, M.2
  • 13
    • 0035921175 scopus 로고    scopus 로고
    • Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII
    • Davies J., Jiang L., Pan L.Z., LaBarre M.J., Anderson D., Reff M. Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII. Biotechnol. Bioeng. 2001, 74:288. 10.1002/bit.1119.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 288
    • Davies, J.1    Jiang, L.2    Pan, L.Z.3    LaBarre, M.J.4    Anderson, D.5    Reff, M.6
  • 14
    • 77955436442 scopus 로고    scopus 로고
    • Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins
    • Ghaderi D., Taylor R.E., Padler-Karavani V., Diaz S., Varki A. Implications of the presence of N-glycolylneuraminic acid in recombinant therapeutic glycoproteins. Nat. Biotechnol. 2010, 28:863. 10.1038/nbt.1651.
    • (2010) Nat. Biotechnol. , vol.28 , pp. 863
    • Ghaderi, D.1    Taylor, R.E.2    Padler-Karavani, V.3    Diaz, S.4    Varki, A.5
  • 15
    • 13544277161 scopus 로고    scopus 로고
    • Vaccine-elicited antibodies mediate antibody-dependent cellular cytotoxicity correlated with significantly reduced acute viremia in rhesus macaques challenged with SIVmac251
    • Gómez-Román V.R., Patterson L.J., Venzon D., Liewehr D., Aldrich K., Florese R., Robert-Guroff M. Vaccine-elicited antibodies mediate antibody-dependent cellular cytotoxicity correlated with significantly reduced acute viremia in rhesus macaques challenged with SIVmac251. J. Immunol. 2005, 174:2185.
    • (2005) J. Immunol. , vol.174 , pp. 2185
    • Gómez-Román, V.R.1    Patterson, L.J.2    Venzon, D.3    Liewehr, D.4    Aldrich, K.5    Florese, R.6    Robert-Guroff, M.7
  • 16
    • 68549091059 scopus 로고    scopus 로고
    • Proposal for a standard system for drawing structural diagrams of N- and O-linked carbohydrates and related compounds
    • Harvey D.J., Merry A.H., Royle L., Campbell M.P., Dwek R.A., Rudd P.M. Proposal for a standard system for drawing structural diagrams of N- and O-linked carbohydrates and related compounds. Proteomics 2009, 9:3796. 10.1002/pmic.200900096.
    • (2009) Proteomics , vol.9 , pp. 3796
    • Harvey, D.J.1    Merry, A.H.2    Royle, L.3    Campbell, M.P.4    Dwek, R.A.5    Rudd, P.M.6
  • 18
    • 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 C.O.S., Goodall D.M., 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. 10.1016/j.bbagen.2005.11.021.
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 669
    • Holland, M.1    Yagi, H.2    Takahashi, N.3    Kato, K.4    Savage, C.O.S.5    Goodall, D.M.6    Jefferis, R.7
  • 20
    • 84858976069 scopus 로고    scopus 로고
    • Alignment of laser-induced fluorescence and mass spectrometric detection traces using electrophoretic mobility scaling in CE-LIF-MS of labeled N-glycans
    • Huhn C., Ruhaak L.R., Mannhardt J., Wuhrer M., Neusüß C., Deelder A.M., Meyer H. Alignment of laser-induced fluorescence and mass spectrometric detection traces using electrophoretic mobility scaling in CE-LIF-MS of labeled N-glycans. ELECTROPHORESIS 2012, 33:563. 10.1002/elps.201100367.
    • (2012) ELECTROPHORESIS , vol.33 , pp. 563
    • Huhn, C.1    Ruhaak, L.R.2    Mannhardt, J.3    Wuhrer, M.4    Neusüß, C.5    Deelder, A.M.6    Meyer, H.7
  • 21
    • 84902550854 scopus 로고    scopus 로고
    • IgG-effector functions: "The Good, The Bad and The Ugly."
    • Kapur R., Einarsdottir H.K., Vidarsson G. IgG-effector functions: "The Good, The Bad and The Ugly.". Immunol. Lett. 2014, 1-6. 10.1016/j.imlet.2014.01.015.
    • (2014) Immunol. Lett.
    • Kapur, R.1    Einarsdottir, H.K.2    Vidarsson, G.3
  • 22
    • 84866017430 scopus 로고    scopus 로고
    • The immunoglobulin, IgG Fc receptor and complement triangle in autoimmune diseases
    • Karsten C.M., Köhl J. The immunoglobulin, IgG Fc receptor and complement triangle in autoimmune diseases. Immunobiology 2012, 217:1067. 10.1016/j.imbio.2012.07.015.
    • (2012) Immunobiology , vol.217 , pp. 1067
    • Karsten, C.M.1    Köhl, J.2
  • 23
    • 0030606920 scopus 로고    scopus 로고
    • Analysis of different glycosylation states in IgG subclasses
    • Keusch J., Levy Y., Shoenfeld Y., Youinou P. Analysis of different glycosylation states in IgG subclasses. Clin. Chim. Acta 1996, 252:147.
    • (1996) Clin. Chim. Acta , vol.252 , pp. 147
    • Keusch, J.1    Levy, Y.2    Shoenfeld, Y.3    Youinou, P.4
  • 24
    • 34247616380 scopus 로고    scopus 로고
    • Glycome mapping on DNA sequencing equipment
    • Laroy W., Contreras R., Callewaert N. Glycome mapping on DNA sequencing equipment. Nat. Protoc. 2006, 1:397. 10.1038/nprot.2006.60.
    • (2006) Nat. Protoc. , vol.1 , pp. 397
    • Laroy, W.1    Contreras, R.2    Callewaert, N.3
  • 25
    • 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 P.R., Takahashi N., Harvey D.J., 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. 10.1016/j.jim.2007.07.014.
    • (2007) J. Immunol. Methods , vol.326 , pp. 116
    • Mimura, Y.1    Ashton, P.R.2    Takahashi, N.3    Harvey, D.J.4    Jefferis, R.5
  • 26
    • 77953760056 scopus 로고    scopus 로고
    • Antibody-mediated modulation of immune responses
    • Nimmerjahn F., Ravetch J.V. Antibody-mediated modulation of immune responses. Immunol. Rev. 2010, 236:265. 10.1111/j.1600-065X.2010.00910.x.
    • (2010) Immunol. Rev. , vol.236 , pp. 265
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 27
    • 4644245701 scopus 로고    scopus 로고
    • Enhancement of the antibody-dependent cellular cytotoxicity of low-fucose IgG1 Is independent of FcgammaRIIIa functional polymorphism
    • Niwa R., Hatanaka S., Shoji-Hosaka E., Sakurada M., Kobayashi Y., Uehara A., Yokoi H., Nakamura K., Shitara K. Enhancement of the antibody-dependent cellular cytotoxicity of low-fucose IgG1 Is independent of FcgammaRIIIa functional polymorphism. Clin. Cancer Res. 2004, 10:6248. 10.1158/1078-0432.CCR-04-0850.
    • (2004) Clin. Cancer Res. , vol.10 , pp. 6248
    • Niwa, R.1    Hatanaka, S.2    Shoji-Hosaka, E.3    Sakurada, M.4    Kobayashi, Y.5    Uehara, A.6    Yokoi, H.7    Nakamura, K.8    Shitara, K.9
  • 28
    • 1242317024 scopus 로고    scopus 로고
    • Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcgammaRIIIa
    • Okazaki A., Shoji-Hosaka E., Nakamura K., Wakitani M., Uchida K., Kakita S., Tsumoto K., Kumagai I., Shitara K. Fucose depletion from human IgG1 oligosaccharide enhances binding enthalpy and association rate between IgG1 and FcgammaRIIIa. J. Mol. Biol. 2004, 336:1239. 10.1016/j.jmb.2004.01.007.
    • (2004) J. Mol. Biol. , vol.336 , pp. 1239
    • Okazaki, A.1    Shoji-Hosaka, E.2    Nakamura, K.3    Wakitani, M.4    Uchida, K.5    Kakita, S.6    Tsumoto, K.7    Kumagai, I.8    Shitara, K.9
  • 30
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • Raju T.S. Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr. Opin. Immunol. 2008, 20:471. 10.1016/j.coi.2008.06.007.
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 471
    • Raju, T.S.1
  • 31
    • 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., 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 2000, 10:477.
    • (2000) Glycobiology , vol.10 , pp. 477
    • Raju, T.S.1    Briggs, J.B.2    Borge, S.M.3    Jones, A.J.4
  • 32
    • 84892577275 scopus 로고    scopus 로고
    • High-throughput glycosylation analysis of therapeutic immunoglobulin G by capillary gel electrophoresis using a DNA analyzer
    • Reusch D., Haberger M., Kailich T., Heidenreich A.-K., Kampe M., Bulau P., Wuhrer M. High-throughput glycosylation analysis of therapeutic immunoglobulin G by capillary gel electrophoresis using a DNA analyzer. MAbs 2014, 6:185. 10.4161/mabs.26712.
    • (2014) MAbs , vol.6 , pp. 185
    • Reusch, D.1    Haberger, M.2    Kailich, T.3    Heidenreich, A.-K.4    Kampe, M.5    Bulau, P.6    Wuhrer, M.7
  • 33
    • 84886998928 scopus 로고    scopus 로고
    • Comparison of the glycosylation of in vitro generated polyclonal human IgG and therapeutic immunoglobulins
    • Ritamo I., Cloutier M., Valmu L., Néron S., Räbinä J. Comparison of the glycosylation of in vitro generated polyclonal human IgG and therapeutic immunoglobulins. Mol. Immunol. 2014, 57:255. 10.1016/j.molimm.2013.10.005.
    • (2014) Mol. Immunol. , vol.57 , pp. 255
    • Ritamo, I.1    Cloutier, M.2    Valmu, L.3    Néron, S.4    Räbinä, J.5
  • 34
    • 76749113309 scopus 로고    scopus 로고
    • Structure and function of immunoglobulins
    • Schroeder H.W., Cavacini L. Structure and function of immunoglobulins. J. Allergy Clin. Immunol. 2010, 125:S41. 10.1016/j.jaci.2009.09.046.
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. S41
    • Schroeder, H.W.1    Cavacini, L.2
  • 35
    • 84860257686 scopus 로고    scopus 로고
    • IVIg-mediated amelioration of ITP in mice is dependent on sialic acid and SIGNR1
    • Schwab I., Biburger M., Krönke G., Schett G., Nimmerjahn F. IVIg-mediated amelioration of ITP in mice is dependent on sialic acid and SIGNR1. Eur. J. Immunol. 2012, 42:826. 10.1002/eji.201142260.
    • (2012) Eur. J. Immunol. , vol.42 , pp. 826
    • Schwab, I.1    Biburger, M.2    Krönke, G.3    Schett, G.4    Nimmerjahn, F.5
  • 37
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII 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., Presta L.G. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 2002, 277:26733. 10.1074/jbc.M202069200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733
    • 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
  • 38
    • 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. 10.1074/jbc.M210665200.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466
    • 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
  • 39
    • 34250682223 scopus 로고    scopus 로고
    • Enhanced Fc-dependent cellular cytotoxicity of Fc fusion proteins derived from TNF receptor II and LFA-3 by fucose removal from Asn-linked oligosaccharides
    • Shoji-Hosaka E., Kobayashi Y., Wakitani M., Uchida K., Niwa R., Nakamura K., Shitara K. Enhanced Fc-dependent cellular cytotoxicity of Fc fusion proteins derived from TNF receptor II and LFA-3 by fucose removal from Asn-linked oligosaccharides. J. Biochem. 2006, 140:777. 10.1093/jb/mvj207.
    • (2006) J. Biochem. , vol.140 , pp. 777
    • Shoji-Hosaka, E.1    Kobayashi, Y.2    Wakitani, M.3    Uchida, K.4    Niwa, R.5    Nakamura, K.6    Shitara, K.7
  • 40
    • 77952487132 scopus 로고    scopus 로고
    • Immunoglobulin G galactosylation and sialylation are associated with pregnancy-induced improvement of rheumatoid arthritis and the postpartum flare: results from a large prospective cohort study
    • Van De Geijn F.E., Wuhrer M., Selman M.H., Willemsen S.P., De Man Y.A., Deelder A.M., Hazes J.M., Dolhain R.J. Immunoglobulin G galactosylation and sialylation are associated with pregnancy-induced improvement of rheumatoid arthritis and the postpartum flare: results from a large prospective cohort study. Arthritis Res. Ther. 2009, 11:R193. 10.1186/ar2892.
    • (2009) Arthritis Res. Ther. , vol.11 , pp. R193
    • Van De Geijn, F.E.1    Wuhrer, M.2    Selman, M.H.3    Willemsen, S.P.4    De Man, Y.A.5    Deelder, A.M.6    Hazes, J.M.7    Dolhain, R.J.8
  • 41
    • 84885866223 scopus 로고    scopus 로고
    • IgG-Fc N-glycosylation at Asn297 and IgA O-glycosylation in the hinge region in health and disease
    • Xue J., Zhu L.-P., Wei Q. IgG-Fc N-glycosylation at Asn297 and IgA O-glycosylation in the hinge region in health and disease. Glycoconj. J. 2013, 30:735. 10.1007/s10719-013-9481-y.
    • (2013) Glycoconj. J. , vol.30 , pp. 735
    • Xue, J.1    Zhu, L.-P.2    Wei, Q.3
  • 42
    • 84888205517 scopus 로고    scopus 로고
    • Galactosylation of IgG1 modulates FcγRIIB-mediated inhibition of murine autoimmune hemolytic anemia
    • Yamada K., Ito K., Furukawa J.-I., Nakata J., Alvarez M., Verbeek J.S., Shinohara Y., Izui S. Galactosylation of IgG1 modulates FcγRIIB-mediated inhibition of murine autoimmune hemolytic anemia. J. Autoimmun. 2013, 47:104. 10.1016/j.jaut.2013.09.001.
    • (2013) J. Autoimmun. , vol.47 , pp. 104
    • Yamada, K.1    Ito, K.2    Furukawa, J.-I.3    Nakata, J.4    Alvarez, M.5    Verbeek, J.S.6    Shinohara, Y.7    Izui, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.