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Volumn 7, Issue 3, 2015, Pages 562-570

The criticality of high-resolution N-linked carbohydrate assays and detailed characterization of antibody effector function in the context of biosimilar development

Author keywords

ADCC; Antibody; Biosimilar; CDC; Effector function; Fc domain; Glycosylation; mAb; N linked carbohydrates

Indexed keywords

ANTIBODY; CONCANAVALIN A; GLYCAN DERIVATIVE; IMMUNOGLOBULIN G1 ANTIBODY; SIALIDASE; BIOSIMILAR AGENT; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; MONOCLONAL ANTIBODY; POLYSACCHARIDE;

EID: 84944906901     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.1080/19420862.2015.1016692     Document Type: Article
Times cited : (20)

References (27)
  • 1
    • 79961116944 scopus 로고    scopus 로고
    • Developing the nation's biosimilars program
    • PMID: 21812668
    • Kozlowski S, Woodcock J, Midthun K, Sherman RB. Developing the nation's biosimilars program. N Engl J Med 2011; 365: 385-8; PMID: 21812668; http://dx. doi. org/10. 1056/NEJMp1107285.
    • (2011) N Engl J Med , vol.365 , pp. 385-388
    • Kozlowski, S.1    Woodcock, J.2    Midthun, K.3    Sherman, R.B.4
  • 2
    • 84865077796 scopus 로고    scopus 로고
    • Analytical aspects of biosimilarity issues of protein drugs
    • Kálmán-Szekeres Z, Olajos M, Ganzler K. Analytical aspects of biosimilarity issues of protein drugs. J Pharm Biomed Anal 2012; 69: 185-95; http://dx. doi. org/10. 1016/j. jpba. 2012. 04. 037.
    • (2012) J Pharm Biomed Anal , vol.69 , pp. 185-195
    • Kálmán-Szekeres, Z.1    Olajos, M.2    Ganzler, K.3
  • 7
    • 34347395733 scopus 로고    scopus 로고
    • Trastuzumab-mechamism of action and use in clinical practice
    • PMID: 17611206
    • Hudis C. Trastuzumab-mechamism of action and use in clinical practice. N Engl J Med 2007; 357: 39-51; PMID: 17611206; http://dx. doi. org/10. 1056/NEJMra043186.
    • (2007) N Engl J Med , vol.357 , pp. 39-51
    • Hudis, C.1
  • 9
    • 70349765751 scopus 로고    scopus 로고
    • 25 years of recombinant proteins from reactor-grown cells-Where do we go from here?
    • PMID: 19463938
    • Hacker DL, De Jesus M, Wurm FM. 25 years of recombinant proteins from reactor-grown cells-Where do we go from here? Biotechnol Adv 2009; 27: 1023-7; PMID: 19463938; http://dx. doi. org/10. 1016/j. biotechadv. 2009. 05. 008.
    • (2009) Biotechnol Adv , vol.27 , pp. 1023-1027
    • Hacker, D.L.1    De Jesus, M.2    Wurm, F.M.3
  • 10
    • 79955788202 scopus 로고    scopus 로고
    • Manufacturing recombinant proteins in kg-ton quantities using animal cells in bioreactors
    • PMID: 21256214
    • De Jesus M, Wurm FM. Manufacturing recombinant proteins in kg-ton quantities using animal cells in bioreactors. Eur J Pharm and Biopharm 2011; 78: 184-8; PMID: 21256214; http://dx. doi. org/10. 1016/j. ejpb. 2011. 01. 005.
    • (2011) Eur J Pharm and Biopharm , vol.78 , pp. 184-188
    • De Jesus, M.1    Wurm, F.M.2
  • 12
    • 77953659426 scopus 로고    scopus 로고
    • Engineered Fc variant antibodies with enhanced ability to recruite complement and mediate effector funtions
    • PMID: 20150767
    • Moore G, Chen H, Karki S, Lazar G. Engineered Fc variant antibodies with enhanced ability to recruite complement and mediate effector funtions. mAbs 2010; 2: 181-9; PMID: 20150767; http://dx. doi. org/10. 4161/mabs. 2. 2. 11158.
    • (2010) mAbs , vol.2 , pp. 181-189
    • Moore, G.1    Chen, H.2    Karki, S.3    Lazar, G.4
  • 14
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among nonfucosylated therapeutic IgG1antibodies with three different N-linked Fc oligosaccharides: The high-mannose, hybrid, and complex types
    • PMID: 17012310
    • Kanda Y, Yamada T, Mori K, Okazaki A, Inoue M, Kitajima-Miyama K, Kuni-Kamochi R, Nakano R, Yano K, Kakita S, et al. Comparison of biological activity among nonfucosylated therapeutic IgG1antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types. Glycobiology 2006; 17: 104-18; PMID: 17012310; http://dx. doi. org/10. 1093/glycob/cwl057.
    • (2006) 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    Kuni-Kamochi, R.7    Nakano, R.8    Yano, K.9    Kakita, S.10
  • 15
    • 28444495153 scopus 로고    scopus 로고
    • IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides
    • Niwa R, Natsume A, Uehara A, Wakitani M, Iida S, Uchida K, Satoh M, Shitara K. IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides. J Immunol Methods 2006; 306: 151-60; http://dx. doi. org/10. 1016/j. jim. 2005. 08. 009.
    • (2006) 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
  • 16
    • 84863440630 scopus 로고    scopus 로고
    • Production, characterization and pharmacokinetic properties of antibodies with N-linked Mannose-5 glycans
    • PMID: 22699308
    • Yu M, Brown D, Reed C, Chung S, Lutman J, Stefanich E, Wong A, Stefan J-P, Bayer R. Production, characterization and pharmacokinetic properties of antibodies with N-linked Mannose-5 glycans. mAbs 2012; 4: 475-87; PMID: 22699308; http://dx. doi. org/10. 4161/mabs. 20737.
    • (2012) mAbs , vol.4 , pp. 475-487
    • Yu, M.1    Brown, D.2    Reed, C.3    Chung, S.4    Lutman, J.5    Stefanich, E.6    Wong, A.7    Stefan, J.-P.8    Bayer, R.9
  • 17
    • 0028670916 scopus 로고
    • Galactosylation of human IgG monoclonal anti-D produced by EBV-transformed B-lymphoblastoid cell lines is depedent on culture media and affects Fc receptor-mediated functional activity
    • PMID: 7756579
    • Kumpel B, Rademacher T, Rook G, Williams P, Wilson I. Galactosylation of human IgG monoclonal anti-D produced by EBV-transformed B-lymphoblastoid cell lines is depedent on culture media and affects Fc receptor-mediated functional activity. Hum Antibodies Hybridomas 1994; 5: 143-51; PMID: 7756579.
    • (1994) Hum Antibodies Hybridomas , vol.5 , pp. 143-151
    • Kumpel, B.1    Rademacher, T.2    Rook, G.3    Williams, P.4    Wilson, I.5
  • 18
    • 28844463354 scopus 로고    scopus 로고
    • Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro
    • PMID: 16321047
    • Hodoniczky J, Zheng YZ, James D. Control of recombinant monoclonal antibody effector functions by Fc N-glycan remodeling in vitro. Biotechnol Prog 2005; 21: 1644-52; PMID: 16321047; http://dx. doi. org/10. 1021/bp050228w.
    • (2005) Biotechnol Prog , vol.21 , pp. 1644-1652
    • Hodoniczky, J.1    Zheng, Y.Z.2    James, D.3
  • 19
    • 0028169439 scopus 로고
    • Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1
    • PMID: 8064227
    • Wright A, Morrison S. Effect of altered CH2-associated carbohydrate structure on the functional properties and in vivo fate of chimeric mouse-human immunoglobulin G1. J Exp Med 1994; 180: 1087-96; PMID: 8064227; http://dx. doi. org/10. 1084/jem. 180. 3. 1087.
    • (1994) J Exp Med , vol.180 , pp. 1087-1096
    • Wright, A.1    Morrison, S.2
  • 20
    • 42349085035 scopus 로고    scopus 로고
    • A recombinant IgG Fc that recapitulates teh anti-inflammitory activity of IVIG
    • PMID: 18420934
    • Anthony R, Nimmerjahn F, Ashline D, Renhold V, Paulson J, Ravetch J. A recombinant IgG Fc that recapitulates teh anti-inflammitory activity of IVIG. Science 2008; 320: 373-6; PMID: 18420934; http://dx. doi. org/10. 1126/science. 1154315.
    • (2008) Science , vol.320 , pp. 373-376
    • Anthony, R.1    Nimmerjahn, F.2    Ashline, D.3    Renhold, V.4    Paulson, J.5    Ravetch, J.6
  • 21
    • 77955412238 scopus 로고    scopus 로고
    • Post-translational modifications differentially effect IgG1 conformation and receptor binding
    • PMID: 20103567
    • Houde D, Peng Y, Berkowitz S, Engen J. Post-translational modifications differentially effect IgG1 conformation and receptor binding. Mol Cell Proteomics 2010; 9: 1716-28; PMID: 20103567; http://dx. doi. org/10. 1074/mcp. M900540-MCP200.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1716-1728
    • Houde, D.1    Peng, Y.2    Berkowitz, S.3    Engen, J.4
  • 22
    • 0023181865 scopus 로고
    • Increased concanavalin A-binding capacity of immunoglobulin G purified from sera of patients with rheumatoid arthritis
    • Malaise M, Franchimont P, Bouillene C, Houssier C, Mahieu P. Increased concanavalin A-binding capacity of immunoglobulin G purified from sera of patients with rheumatoid arthritis. Clin Exp Immunol 1987; 68: 543-51.
    • (1987) Clin Exp Immunol , vol.68 , pp. 543-551
    • Malaise, M.1    Franchimont, P.2    Bouillene, C.3    Houssier, C.4    Mahieu, P.5
  • 23
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • PMID: 16888140
    • Kaneko Y, Nimmerjahn F, Ravetch J. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006; 313: 670-3; PMID: 16888140; http://dx. doi. org/10. 1126/science. 1129594.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.3
  • 24
    • 84883879484 scopus 로고    scopus 로고
    • Physicochemical and functional comparability between the proposed biosimilar rituximab GP2013 and originator rituximab
    • PMID: 23649935
    • Visser J, Feuerstein I, Stangler T, Schmiederer T, Fritsch C. Physicochemical and functional comparability between the proposed biosimilar rituximab GP2013 and originator rituximab. BioDrugs 2013; 27: 495-507; PMID: 23649935; http://dx. doi. org/10. 1007/s40259-013-0036-3.
    • (2013) BioDrugs , vol.27 , pp. 495-507
    • Visser, J.1    Feuerstein, I.2    Stangler, T.3    Schmiederer, T.4    Fritsch, C.5
  • 25
    • 60149106150 scopus 로고    scopus 로고
    • Quality by design for biopharmaceuticals
    • PMID: 19131992
    • Rathore A, Winkle H. Quality by design for biopharmaceuticals. Nat Biotechnol 2009; 27: 26-34; PMID: 19131992; http://dx. doi. org/10. 1038/nbt0109-26.
    • (2009) Nat Biotechnol , vol.27 , pp. 26-34
    • Rathore, A.1    Winkle, H.2
  • 26
    • 79958837668 scopus 로고    scopus 로고
    • High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans
    • PMID: 21421994
    • Goetze A, Liu Y, Zhang Z, Shah B, Lee E, Bondarenko P, Flynn G. High-mannose glycans on the Fc region of therapeutic IgG antibodies increase serum clearance in humans. Glycobiology 2011; 21: 949-69; PMID: 21421994; http://dx. doi. org/10. 1093/glycob/cwr027.
    • (2011) Glycobiology , vol.21 , pp. 949-969
    • Goetze, A.1    Liu, Y.2    Zhang, Z.3    Shah, B.4    Lee, E.5    Bondarenko, P.6    Flynn, G.7
  • 27
    • 84860911340 scopus 로고    scopus 로고
    • Quantitative evaluation of fucose reducing effects in a humanized antibody on FcGamma receptor biniding and antibody-dependent cell-mediated cytotoxicity activities
    • PMID: 22531441
    • Chung S, Quarmby V, Gao X, Ying Y, Lin L, Reed C, Fong C, Lau W, Qui Z, Shen A, et al. Quantitative evaluation of fucose reducing effects in a humanized antibody on FcGamma receptor biniding and antibody-dependent cell-mediated cytotoxicity activities. mAbs 2012; 4: 326-40; PMID: 22531441; http://dx. doi. org/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    Qui, Z.9    Shen, A.10


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