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Volumn 8, Issue 6, 2016, Pages 1098-1106

Increased in vivo effector function of human IgG4 isotype antibodies through afucosylation

Author keywords

ADCC; B cell depletion; CD20; IgG subclass

Indexed keywords

CD20 ANTIBODY; GLYCAN; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G4; CD20 ANTIGEN; FUCOSE; IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY;

EID: 84976299327     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.1080/19420862.2016.1189049     Document Type: Article
Times cited : (19)

References (35)
  • 1
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: the neonatal Fc receptor comes of age
    • 17703228
    • D.C.Roopenian, S.Akilesh. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol 2007; 7:715-25; PMID:17703228; doi 10.1038/nri2155
    • (2007) Nat Rev Immunol , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 2
    • 84865677743 scopus 로고    scopus 로고
    • Isotype and glycoform selection for antibody therapeutics
    • 22465822
    • R.Jefferis. Isotype and glycoform selection for antibody therapeutics. Arch Biochem Biophys 2012; 526:159-66; PMID:22465822; doi 10.1016/j.abb.2012.03.021
    • (2012) Arch Biochem Biophys , vol.526 , pp. 159-166
    • Jefferis, R.1
  • 3
    • 1142298744 scopus 로고    scopus 로고
    • Human antibody-Fc receptor interactions illuminated by crystal structures
    • 15040582
    • J.M.Woof, D.R.Burton. Human antibody-Fc receptor interactions illuminated by crystal structures. Nat Rev Immunol 2004; 4:89-99; PMID:15040582; doi 10.1038/nri1266
    • (2004) Nat Rev Immunol , vol.4 , pp. 89-99
    • Woof, J.M.1    Burton, D.R.2
  • 5
    • 0036464719 scopus 로고    scopus 로고
    • Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene
    • 11806974
    • G.Cartron, L.Dacheux, G.Salles, P.Solal-Celigny, P.Bardos, P.Colombat, H.Watier. Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene. Blood 2002; 99:754-8; PMID:11806974; doi 10.1182/blood.V99.3.754
    • (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
  • 6
    • 77951561987 scopus 로고    scopus 로고
    • Increasing the efficacy of CD20 antibody therapy through the engineering of a new type II anti-CD20 antibody with enhanced direct and immune effector cell-mediated B-cell cytotoxicity
    • 20194898
    • E.Mossner, P.Brunker, S.Moser, U.Puntener, C.Schmidt, S.Herter, R.Grau, C.Gerdes, A.Nopora, E.van Puijenbroek, et al. Increasing the efficacy of CD20 antibody therapy through the engineering of a new type II anti-CD20 antibody with enhanced direct and immune effector cell-mediated B-cell cytotoxicity. Blood 2010; 115:4393-402; PMID:20194898; doi 10.1182/blood-2009-06-225979
    • (2010) Blood , vol.115 , pp. 4393-4402
    • Mossner, E.1    Brunker, P.2    Moser, S.3    Puntener, U.4    Schmidt, C.5    Herter, S.6    Grau, R.7    Gerdes, C.8    Nopora, A.9    van Puijenbroek, E.10
  • 7
    • 84889853699 scopus 로고    scopus 로고
    • Effects of altered FcgammaR binding on antibody pharmacokinetics in cynomolgus monkeys
    • 24492343
    • M.K.Leabman, Y.G.Meng, R.F.Kelley, L.E.DeForge, K.J.Cowan, S.Iyer. Effects of altered FcgammaR binding on antibody pharmacokinetics in cynomolgus monkeys. mAbs 2013; 5:896-903; PMID:24492343; doi 10.4161/mabs.26436
    • (2013) mAbs , vol.5 , pp. 896-903
    • Leabman, M.K.1    Meng, Y.G.2    Kelley, R.F.3    DeForge, L.E.4    Cowan, K.J.5    Iyer, S.6
  • 8
    • 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
    • 11986321
    • R.L.Shields, J.Lai, R.Keck, L.Y.O'Connell, K.Hong, Y.G.Meng, S.H.Weikert, L.G.Presta. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J Biol Chem 2002; 277:26733-40; PMID:11986321; doi 10.1074/jbc.M202069200
    • (2002) 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.7    Presta, L.G.8
  • 9
    • 28444495153 scopus 로고    scopus 로고
    • IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides
    • 16219319
    • R.Niwa, A.Natsume, A.Uehara, M.Wakitani, S.Iida, K.Uchida, M.Satoh, K.Shitara. IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides. J Immunol Methods 2005; 306:151-60; PMID:16219319; doi 10.1016/j.jim.2005.08.009
    • (2005) J Immunol Methods , vol.306 , pp. 151-160
    • Niwa, R.1    Natsume, A.2    Uehara, A.3    Wakitani, M.4    Iida, S.5    Uchida, K.6    Satoh, M.7    Shitara, K.8
  • 10
    • 84867836578 scopus 로고    scopus 로고
    • Revisiting the role of glycosylation in the structure of human IgG Fc
    • 22747430
    • M.J.Borrok, S.T.Jung, T.H.Kang, A.F.Monzingo, G.Georgiou. Revisiting the role of glycosylation in the structure of human IgG Fc. ACS Chem Biol 2012; 7:1596-602; PMID:22747430; doi 10.1021/cb300130k
    • (2012) ACS Chem Biol , vol.7 , pp. 1596-1602
    • Borrok, M.J.1    Jung, S.T.2    Kang, T.H.3    Monzingo, A.F.4    Georgiou, G.5
  • 11
    • 84863249248 scopus 로고    scopus 로고
    • Aglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system
    • 22377750
    • G.Yin, E.D.Garces, J.Yang, J.Zhang, C.Tran, A.R.Steiner, C.Roos, S.Bajad, S.Hudak, K.Penta, et al. Aglycosylated antibodies and antibody fragments produced in a scalable in vitro transcription-translation system. mAbs 2012; 4:217-25; PMID:22377750; doi 10.4161/mabs.4.2.19202
    • (2012) mAbs , vol.4 , pp. 217-225
    • Yin, G.1    Garces, E.D.2    Yang, J.3    Zhang, J.4    Tran, C.5    Steiner, A.R.6    Roos, C.7    Bajad, S.8    Hudak, S.9    Penta, K.10
  • 13
    • 0029852737 scopus 로고    scopus 로고
    • A therapeutic human IgG4 monoclonal antibody that depletes target cells in humans
    • 8973608
    • J.D.Isaacs, M.G.Wing, J.D.Greenwood, B.L.Hazleman, G.Hale, H.Waldmann. A therapeutic human IgG4 monoclonal antibody that depletes target cells in humans. Clin Exp Immunol 1996; 106:427-33; PMID:8973608; doi 10.1046/j.1365-2249.1996.d01-876.x
    • (1996) Clin Exp Immunol , vol.106 , pp. 427-433
    • Isaacs, J.D.1    Wing, M.G.2    Greenwood, J.D.3    Hazleman, B.L.4    Hale, G.5    Waldmann, H.6
  • 14
    • 84908062862 scopus 로고    scopus 로고
    • Evaluating the impact of cell culture process parameters on monoclonal antibody N-glycosylation
    • M.Ivarsson, T.K.Villiger, M.Morbidelli, M.Soos. Evaluating the impact of cell culture process parameters on monoclonal antibody N-glycosylation. J Biotechnol 2014; 188C:88-96; PMID:25173615; doi 10.1016/j.jbiotec.2014.08.026
    • (2014) J Biotechnol , vol.188C , pp. 88-96
    • Ivarsson, M.1    Villiger, T.K.2    Morbidelli, M.3    Soos, M.4
  • 15
    • 84864117650 scopus 로고    scopus 로고
    • Methods to engineer and identify IgG1 variants with improved FcRn binding or effector function
    • 22723108
    • R.F.Kelley, Y.G.Meng. Methods to engineer and identify IgG1 variants with improved FcRn binding or effector function. Methods Mol Biol 2012; 901:277-93; PMID:22723108; doi 10.1007/978-1-61779-931-0_18
    • (2012) Methods Mol Biol , vol.901 , pp. 277-293
    • Kelley, R.F.1    Meng, Y.G.2
  • 16
    • 84860911340 scopus 로고    scopus 로고
    • Quantitative evaluation of fucose reducing effects in a humanized antibody on Fcgamma receptor binding and antibody-dependent cell-mediated cytotoxicity activities
    • 22531441
    • S.Chung, V.Quarmby, X.Gao, Y.Ying, L.Lin, C.Reed, C.Fong, W.Lau, Z.J.Qiu, A.Shen, et al. Quantitative evaluation of fucose reducing effects in a humanized antibody on Fcgamma receptor binding and antibody-dependent cell-mediated cytotoxicity activities. mAbs 2012; 4:326-40; PMID:22531441; doi 10.4161/mabs.19941
    • (2012) mAbs , vol.4 , pp. 326-340
    • Chung, S.1    Quarmby, V.2    Gao, X.3    Ying, Y.4    Lin, L.5    Reed, C.6    Fong, C.7    Lau, W.8    Qiu, Z.J.9    Shen, A.10
  • 18
    • 19944427673 scopus 로고    scopus 로고
    • Importance of cellular microenvironment and circulatory dynamics in B cell immunotherapy
    • 15634903
    • Q.Gong, Q.Ou, S.Ye, W.P.Lee, J.Cornelius, L.Diehl, W.Y.Lin, Z.Hu, Y.Lu, Y.Chen, et al. Importance of cellular microenvironment and circulatory dynamics in B cell immunotherapy. J Immunol 2005; 174:817-26; PMID:15634903; doi 10.4049/jimmunol.174.2.817
    • (2005) J Immunol , vol.174 , pp. 817-826
    • Gong, Q.1    Ou, Q.2    Ye, S.3    Lee, W.P.4    Cornelius, J.5    Diehl, L.6    Lin, W.Y.7    Hu, Z.8    Lu, Y.9    Chen, Y.10
  • 19
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms
    • 16330541
    • C.Ferrara, F.Stuart, P.Sondermann, P.Brunker, P.Umana. The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms. J Biol Chem 2006; 281:5032-6; PMID:16330541; doi 10.1074/jbc.M510171200
    • (2006) J Biol Chem , vol.281 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3    Brunker, P.4    Umana, P.5
  • 20
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex
    • 10917521
    • P.Sondermann, R.Huber, V.Oosthuizen, U.Jacob. The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature 2000; 406:267-73; PMID:10917521; doi 10.1038/35018508
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 21
    • 79961233787 scopus 로고    scopus 로고
    • Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose
    • 21768335
    • C.Ferrara, S.Grau, C.Jager, P.Sondermann, P.Brunker, I.Waldhauer, M.Hennig, A.Ruf, A.C.Rufer, M.Stihle, 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 2011; 108:12669-74; PMID:21768335; doi 10.1073/pnas.1108455108
    • (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    Hennig, M.7    Ruf, A.8    Rufer, A.C.9    Stihle, M.10
  • 22
    • 34247378189 scopus 로고    scopus 로고
    • Quantitative in vivo comparisons of the Fc gamma receptor-dependent agonist activities of different fucosylation variants of an immunoglobulin G antibody
    • 17466910
    • B.Scallon, S.McCarthy, J.Radewonuk, A.Cai, M.Naso, T.S.Raju, R.Capocasale. Quantitative in vivo comparisons of the Fc gamma receptor-dependent agonist activities of different fucosylation variants of an immunoglobulin G antibody. Int Immunopharmacol 2007; 7:761-72; PMID:17466910; doi 10.1016/j.intimp.2007.01.014
    • (2007) Int Immunopharmacol , vol.7 , pp. 761-772
    • Scallon, B.1    McCarthy, S.2    Radewonuk, J.3    Cai, A.4    Naso, M.5    Raju, T.S.6    Capocasale, R.7
  • 23
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses
    • 19018092
    • P.Bruhns, B.Iannascoli, P.England, D.A.Mancardi, N.Fernandez, S.Jorieux, M.Daëron. Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses. Blood 2009; 113:3716-25; PMID:19018092; doi 10.1182/blood-2008-09-179754
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1    Iannascoli, B.2    England, P.3    Mancardi, D.A.4    Fernandez, N.5    Jorieux, S.6    Daëron, M.7
  • 25
    • 84889850198 scopus 로고    scopus 로고
    • Knobs-into-holes antibody production in mammalian cell lines reveals that asymmetric afucosylation is sufficient for full antibody-dependent cellular cytotoxicity
    • 23995614
    • W.Shatz, S.Chung, B.Li, B.Marshall, M.Tejada, W.Phung, W.Sandoval, R.F.Kelley, J.M.Scheer. Knobs-into-holes antibody production in mammalian cell lines reveals that asymmetric afucosylation is sufficient for full antibody-dependent cellular cytotoxicity. mAbs 2013; 5:872-81; PMID:23995614; doi 10.4161/mabs.26307
    • (2013) mAbs , vol.5 , pp. 872-881
    • Shatz, W.1    Chung, S.2    Li, B.3    Marshall, B.4    Tejada, M.5    Phung, W.6    Sandoval, W.7    Kelley, R.F.8    Scheer, J.M.9
  • 26
    • 84862495640 scopus 로고    scopus 로고
    • Properties of mouse and human IgG receptors and their contribution to disease models
    • 22535666
    • P.Bruhns. Properties of mouse and human IgG receptors and their contribution to disease models. Blood 2012; 119:5640-9; PMID:22535666; doi 10.1182/blood-2012-01-380121
    • (2012) Blood , vol.119 , pp. 5640-5649
    • Bruhns, P.1
  • 27
    • 84859991126 scopus 로고    scopus 로고
    • Mouse model recapitulating human Fcgamma receptor structural and functional diversity
    • 22474370
    • P.Smith, D.J.DiLillo, S.Bournazos, F.Li, J.V.Ravetch. Mouse model recapitulating human Fcgamma receptor structural and functional diversity. Proc Natl Acad Sci U S A 2012; 109:6181-6; PMID:22474370; doi 10.1073/pnas.1203954109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 6181-6186
    • Smith, P.1    DiLillo, D.J.2    Bournazos, S.3    Li, F.4    Ravetch, J.V.5
  • 30
    • 77955375562 scopus 로고    scopus 로고
    • Enhancement of DNA uptake in FUT8-deleted CHO cells for transient production of afucosylated antibodies
    • 20564613
    • A.W.Wong, T.K.Baginski, D.E.Reilly. Enhancement of DNA uptake in FUT8-deleted CHO cells for transient production of afucosylated antibodies. Biotechnol Bioeng 2010; 106:751-63; PMID:20564613; doi 10.1002/bit.22749
    • (2010) Biotechnol Bioeng , vol.106 , pp. 751-763
    • Wong, A.W.1    Baginski, T.K.2    Reilly, D.E.3
  • 31
    • 84979150310 scopus 로고    scopus 로고
    • The mAb-glyco-chip kit - a workflow solution for rapid and fully automated characterization of N-linked glycans from monoclonal antibodies
    • L.Trojer, K.Gromadski, T.van de Groor, S.Buckenmaier. The mAb-glyco-chip kit - a workflow solution for rapid and fully automated characterization of N-linked glycans from monoclonal antibodies. Chromatography Today 2011; 2011:5
    • (2011) Chromatography Today , vol.2011 , pp. 5
    • Trojer, L.1    Gromadski, K.2    van de Groor, T.3    Buckenmaier, S.4
  • 32
    • 79551593709 scopus 로고    scopus 로고
    • Identification of IgG(1) variants with increased affinity to FcgammaRIIIa and unaltered affinity to FcgammaRI and FcRn: comparison of soluble receptor-based and cell-based binding assays
    • 21185301
    • Y.Lu, J.M.Vernes, N.Chiang, Q.Ou, J.Ding, C.Adams, K.Hong, B.T.Truong, D.Ng, A.Shen, et al. Identification of IgG(1) variants with increased affinity to FcgammaRIIIa and unaltered affinity to FcgammaRI and FcRn: comparison of soluble receptor-based and cell-based binding assays. J Immunol Methods 2011; 365:132-41; PMID:21185301; doi 10.1016/j.jim.2010.12.014
    • (2011) J Immunol Methods , vol.365 , pp. 132-141
    • Lu, Y.1    Vernes, J.M.2    Chiang, N.3    Ou, Q.4    Ding, J.5    Adams, C.6    Hong, K.7    Truong, B.T.8    Ng, D.9    Shen, A.10
  • 33
    • 10344237546 scopus 로고    scopus 로고
    • Simple quantitative live cell and anti-idiotypic antibody based ELISA for humanized antibody directed to cell surface protein CD20
    • 15604027
    • K.Hong, L.G.Presta, Y.Lu, A.Penn, C.Adams, A.Chuntharapai, J.Yang, W.L.Wong, Y.G.Meng. Simple quantitative live cell and anti-idiotypic antibody based ELISA for humanized antibody directed to cell surface protein CD20. J Immunol Methods 2004; 294:189-97; PMID:15604027; doi 10.1016/j.jim.2004.09.003
    • (2004) J Immunol Methods , vol.294 , pp. 189-197
    • Hong, K.1    Presta, L.G.2    Lu, Y.3    Penn, A.4    Adams, C.5    Chuntharapai, A.6    Yang, J.7    Wong, W.L.8    Meng, Y.G.9
  • 34
    • 84896274654 scopus 로고    scopus 로고
    • Methods for measuring antibody-dependent cell-mediated cytotoxicity in vitro
    • 24497354
    • A.S.Miller, M.L.Tejada, H.Gazzano-Santoro. Methods for measuring antibody-dependent cell-mediated cytotoxicity in vitro. Methods Mol Biol 2014; 1134:59-65; PMID:24497354; doi 10.1007/978-1-4939-0326-9_5
    • (2014) Methods Mol Biol , vol.1134 , pp. 59-65
    • Miller, A.S.1    Tejada, M.L.2    Gazzano-Santoro, H.3
  • 35
    • 84921395878 scopus 로고    scopus 로고
    • Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles–part 1: separation-based methods
    • 25524468
    • D.Reusch, M.Haberger, B.Maier, M.Maier, R.Kloseck, B.Zimmermann, M.Hook, Z.Szabo, S.Tep, J.Wegstein, et al. Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles–part 1: separation-based methods. mAbs 2015; 7:167-79; PMID:25524468; doi 10.4161/19420862.2014.986000
    • (2015) mAbs , vol.7 , pp. 167-179
    • Reusch, D.1    Haberger, M.2    Maier, B.3    Maier, M.4    Kloseck, R.5    Zimmermann, B.6    Hook, M.7    Szabo, Z.8    Tep, S.9    Wegstein, J.10


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