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Volumn 106, Issue 4, 2017, Pages 1008-1017

An “Fc-Silenced” IgG1 Format With Extended Half-Life Designed for Improved Stability

Author keywords

benign blocker; biotechnology; CH2; calorimetry (DSC); developability; Fc silenced; IgG antibody; immunology; light scattering (dynamic); pharmacokinetics; protein aggregation; thermal analysis

Indexed keywords

FC RECEPTOR; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G1 TM; IMMUNOGLOBULIN G1 YTE; MACROGOL; UNCLASSIFIED DRUG; FC RECEPTOR IIA; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G;

EID: 85011044824     PISSN: 00223549     EISSN: 15206017     Source Type: Journal    
DOI: 10.1016/j.xphs.2016.12.023     Document Type: Article
Times cited : (38)

References (56)
  • 1
    • 4644245701 scopus 로고    scopus 로고
    • Enhancement of the antibody-dependent cellular cytotoxicity of low-fucose IgG1 is independent of FcgammaRIIIa functional polymorphism
    • 1 Niwa, R., Hatanaka, S., Shoji-Hosaka, E., et al. Enhancement of the antibody-dependent cellular cytotoxicity of low-fucose IgG1 is independent of FcgammaRIIIa functional polymorphism. Clin Cancer Res 10:18 (2004), 6248–6255.
    • (2004) Clin Cancer Res , vol.10 , Issue.18 , pp. 6248-6255
    • Niwa, R.1    Hatanaka, S.2    Shoji-Hosaka, E.3
  • 2
    • 70449727004 scopus 로고    scopus 로고
    • Optimization of Fc-mediated effector functions of monoclonal antibodies
    • 2 Strohl, W., Optimization of Fc-mediated effector functions of monoclonal antibodies. Curr Opin Biotechnol 20:6 (2009), 685–691.
    • (2009) Curr Opin Biotechnol , vol.20 , Issue.6 , pp. 685-691
    • Strohl, W.1
  • 3
    • 78651360674 scopus 로고    scopus 로고
    • Optimizing therapeutic antibody function progress with Fc domain engineering
    • 3 Kaneko, E., Niwa, R., Optimizing therapeutic antibody function progress with Fc domain engineering. Biodrugs 25:1 (2011), 1–11.
    • (2011) Biodrugs , vol.25 , Issue.1 , pp. 1-11
    • Kaneko, E.1    Niwa, R.2
  • 4
    • 49749147926 scopus 로고    scopus 로고
    • Intravenous immunoglobulins induce CD32-mediated platelet aggregation in vitro
    • 4 Pollreisz, A., Assinger, A., Hacker, S., et al. Intravenous immunoglobulins induce CD32-mediated platelet aggregation in vitro. Br J Dermatol 159:3 (2008), 578–584.
    • (2008) Br J Dermatol , vol.159 , Issue.3 , pp. 578-584
    • Pollreisz, A.1    Assinger, A.2    Hacker, S.3
  • 5
    • 84904031022 scopus 로고    scopus 로고
    • Therapeutic Antibody Engineering: Current and Future Advances Driving the Strongest Growth Area in the Pharma Industry
    • Woodhead Publishing Cambridge, UK
    • 5 Strohl, W.R., Strohl, L.M., Therapeutic Antibody Engineering: Current and Future Advances Driving the Strongest Growth Area in the Pharma Industry. 2012, Woodhead Publishing, Cambridge, UK.
    • (2012)
    • Strohl, W.R.1    Strohl, L.M.2
  • 6
    • 0027458717 scopus 로고
    • The generation of a humanized, non-mitogenic CD3 monoclonal antibody which retains in vitro immunosuppressive properties
    • 6 Bolt, S., Routledge, E., Lloyd, I., et al. The generation of a humanized, non-mitogenic CD3 monoclonal antibody which retains in vitro immunosuppressive properties. Eur J Immunol 23:2 (1993), 403–411.
    • (1993) Eur J Immunol , vol.23 , Issue.2 , pp. 403-411
    • Bolt, S.1    Routledge, E.2    Lloyd, I.3
  • 7
    • 60749099736 scopus 로고    scopus 로고
    • Functional characterization of N297A, a murine surrogate for low-Fc binding anti-human CD3 antibodies
    • 7 Chao, D.T., Ma, X., Li, O., Park, H., Law, D., Functional characterization of N297A, a murine surrogate for low-Fc binding anti-human CD3 antibodies. Immunol Invest 38:1 (2009), 76–92.
    • (2009) Immunol Invest , vol.38 , Issue.1 , pp. 76-92
    • Chao, D.T.1    Ma, X.2    Li, O.3    Park, H.4    Law, D.5
  • 8
    • 0034655265 scopus 로고    scopus 로고
    • Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc
    • 8 Idusogie, E.E., Presta, L.G., Gazzano-Santoro, H., et al. Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc. J Immunol 164:8 (2000), 4178–4184.
    • (2000) J Immunol , vol.164 , Issue.8 , pp. 4178-4184
    • Idusogie, E.E.1    Presta, L.G.2    Gazzano-Santoro, H.3
  • 9
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R
    • 9 Shields, R.L., Namenuk, A.K., Hong, K., et al. High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R. J Biol Chem 276:9 (2001), 6591–6604.
    • (2001) J Biol Chem , vol.276 , Issue.9 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3
  • 10
    • 0027216004 scopus 로고
    • A single amino-acid substitution abolishes the heterogeneity of chimeric mouse/human (igG4) antibody
    • 10 Angal, S., King, D.J., Bodmer, M.W., et al. A single amino-acid substitution abolishes the heterogeneity of chimeric mouse/human (igG4) antibody. Mol Immunol 30:1 (1993), 105–108.
    • (1993) Mol Immunol , vol.30 , Issue.1 , pp. 105-108
    • Angal, S.1    King, D.J.2    Bodmer, M.W.3
  • 11
    • 0030761203 scopus 로고    scopus 로고
    • Humanized porcine VCAM-specific monoclonal antibodies with chimeric IgG2/G4 constant regions block human leukocyte binding to porcine endothelial cells
    • 11 Mueller, J.P., Giannoni, M.A., Hartman, S.L., et al. Humanized porcine VCAM-specific monoclonal antibodies with chimeric IgG2/G4 constant regions block human leukocyte binding to porcine endothelial cells. Mol Immunol 34:6 (1997), 441–452.
    • (1997) Mol Immunol , vol.34 , Issue.6 , pp. 441-452
    • Mueller, J.P.1    Giannoni, M.A.2    Hartman, S.L.3
  • 12
    • 77953652926 scopus 로고    scopus 로고
    • IgG2m4, an engineered antibody isotype with reduced Fc function
    • 12 An, Z., Forrest, G., Moore, R., et al. IgG2m4, an engineered antibody isotype with reduced Fc function. mAbs 1:6 (2009), 572–579.
    • (2009) mAbs , vol.1 , Issue.6 , pp. 572-579
    • An, Z.1    Forrest, G.2    Moore, R.3
  • 13
    • 0034657794 scopus 로고    scopus 로고
    • The IgG Fc contains distinct Fc receptor (FcR) binding sites: the leukocyte receptors Fc gamma RI and Fc gamma RIIa bind to a region in the Fc distinct from that recognized by neonatal FcR and protein A
    • 13 Wines, B.D., Powell, M.S., Parren, P., Barnes, N., Hogarth, P.M., The IgG Fc contains distinct Fc receptor (FcR) binding sites: the leukocyte receptors Fc gamma RI and Fc gamma RIIa bind to a region in the Fc distinct from that recognized by neonatal FcR and protein A. J Immunol 164:10 (2000), 5313–5318.
    • (2000) J Immunol , vol.164 , Issue.10 , pp. 5313-5318
    • Wines, B.D.1    Powell, M.S.2    Parren, P.3    Barnes, N.4    Hogarth, P.M.5
  • 14
    • 84891631658 scopus 로고    scopus 로고
    • An engineered Fc variant of an IgG eliminates all immune effector functions via structural perturbations
    • 14 Vafa, O., Gilliland, G.L., Brezski, R.J., et al. An engineered Fc variant of an IgG eliminates all immune effector functions via structural perturbations. Methods 65:1 (2014), 114–126.
    • (2014) Methods , vol.65 , Issue.1 , pp. 114-126
    • Vafa, O.1    Gilliland, G.L.2    Brezski, R.J.3
  • 15
  • 16
    • 84939254457 scopus 로고    scopus 로고
    • Targeting FcRn for the modulation of antibody dynamics
    • 16 Ward, E.S., Devanaboyina, S.C., Ober, R.J., Targeting FcRn for the modulation of antibody dynamics. Mol Immunol 67:2 (2015), 131–141.
    • (2015) Mol Immunol , vol.67 , Issue.2 , pp. 131-141
    • Ward, E.S.1    Devanaboyina, S.C.2    Ober, R.J.3
  • 17
    • 77950265888 scopus 로고    scopus 로고
    • Pharmacokinetics of humanized monoclonal anti-tumor necrosis factor-alpha antibody and its neonatal Fc receptor variants in mice and cynomolgus monkeys
    • 17 Deng, R., Loyet, K.M., Lien, S., et al. Pharmacokinetics of humanized monoclonal anti-tumor necrosis factor-alpha antibody and its neonatal Fc receptor variants in mice and cynomolgus monkeys. Drug Metab Dispos 38:4 (2010), 600–605.
    • (2010) Drug Metab Dispos , vol.38 , Issue.4 , pp. 600-605
    • Deng, R.1    Loyet, K.M.2    Lien, S.3
  • 18
    • 10744222698 scopus 로고    scopus 로고
    • Engineered human IgG antibodies with longer serum half-lives in primates
    • 18 Hinton, P.R., Johlfs, M.G., Xiong, J.M., et al. Engineered human IgG antibodies with longer serum half-lives in primates. J Biol Chem 279:8 (2004), 6213–6216.
    • (2004) J Biol Chem , vol.279 , Issue.8 , pp. 6213-6216
    • Hinton, P.R.1    Johlfs, M.G.2    Xiong, J.M.3
  • 19
    • 67649207267 scopus 로고    scopus 로고
    • Engineering human IgG1 affinity to human neonatal Fc receptor: impact of affinity improvement on pharmacokinetics in primates
    • 19 Yeung, Y.A., Leabman, M.K., Marvin, J.S., et al. Engineering human IgG1 affinity to human neonatal Fc receptor: impact of affinity improvement on pharmacokinetics in primates. J Immunol 182:12 (2009), 7663–7671.
    • (2009) J Immunol , vol.182 , Issue.12 , pp. 7663-7671
    • Yeung, Y.A.1    Leabman, M.K.2    Marvin, J.S.3
  • 20
    • 76349123565 scopus 로고    scopus 로고
    • Enhanced antibody half-life improves in vivo activity
    • 20 Zalevsky, J., Chamberlain, A.K., Horton, H.M., et al. Enhanced antibody half-life improves in vivo activity. Nat Biotechnol 28:2 (2010), 157–159.
    • (2010) Nat Biotechnol , vol.28 , Issue.2 , pp. 157-159
    • Zalevsky, J.1    Chamberlain, A.K.2    Horton, H.M.3
  • 21
    • 84922780197 scopus 로고    scopus 로고
    • pH-dependent binding engineering reveals an FcRn affinity threshold that governs IgG recycling
    • 21 Borrok, M.J., Wu, Y.L., Beyaz, N., et al. pH-dependent binding engineering reveals an FcRn affinity threshold that governs IgG recycling. J Biol Chem 290:7 (2015), 4282–4290.
    • (2015) J Biol Chem , vol.290 , Issue.7 , pp. 4282-4290
    • Borrok, M.J.1    Wu, Y.L.2    Beyaz, N.3
  • 22
    • 48549105161 scopus 로고    scopus 로고
    • Molecular engineering and design of therapeutic antibodies
    • 22 Presta, L.G., Molecular engineering and design of therapeutic antibodies. Curr Opin Immunol 20:4 (2008), 460–470.
    • (2008) Curr Opin Immunol , vol.20 , Issue.4 , pp. 460-470
    • Presta, L.G.1
  • 23
    • 33747631571 scopus 로고    scopus 로고
    • Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn)
    • 23 Dall'Acqua, W.F., Kiener, P.A., Wu, H.R., Properties of human IgG1s engineered for enhanced binding to the neonatal Fc receptor (FcRn). J Biol Chem 281:33 (2006), 23514–23524.
    • (2006) J Biol Chem , vol.281 , Issue.33 , pp. 23514-23524
    • Dall'Acqua, W.F.1    Kiener, P.A.2    Wu, H.R.3
  • 24
    • 0036839457 scopus 로고    scopus 로고
    • Increasing the affinity of a human IgG1, for the neonatal Fc receptor: biological consequences
    • 24 Dall'Acqua, W.F., Woods, R.M., Ward, E.S., et al. Increasing the affinity of a human IgG1, for the neonatal Fc receptor: biological consequences. J Immunol 169:9 (2002), 5171–5180.
    • (2002) J Immunol , vol.169 , Issue.9 , pp. 5171-5180
    • Dall'Acqua, W.F.1    Woods, R.M.2    Ward, E.S.3
  • 25
    • 84887418713 scopus 로고    scopus 로고
    • A novel investigational Fc-modified humanized monoclonal antibody, motavizumab-YTE, has an extended half-life in healthy adults
    • 25 Robbie, G.J., Criste, R., Dall'Acqua, W.F., et al. A novel investigational Fc-modified humanized monoclonal antibody, motavizumab-YTE, has an extended half-life in healthy adults. Antimicrobial Agents Chemother 57:12 (2013), 6147–6153.
    • (2013) Antimicrobial Agents Chemother , vol.57 , Issue.12 , pp. 6147-6153
    • Robbie, G.J.1    Criste, R.2    Dall'Acqua, W.F.3
  • 26
    • 84896718811 scopus 로고    scopus 로고
    • Asymmetrical Fc engineering greatly enhances antibody-dependent cellular cytotoxicity (ADCC) effector function and stability of the modified antibodies
    • 26 Liu, Z., Gunasekaran, K., Wang, W., et al. Asymmetrical Fc engineering greatly enhances antibody-dependent cellular cytotoxicity (ADCC) effector function and stability of the modified antibodies. J Biol Chem 289:6 (2014), 3571–3590.
    • (2014) J Biol Chem , vol.289 , Issue.6 , pp. 3571-3590
    • Liu, Z.1    Gunasekaran, K.2    Wang, W.3
  • 27
    • 84921340583 scopus 로고    scopus 로고
    • Correlations between changes in conformational dynamics and physical stability in a mutant IgG1 mAb engineered for extended serum half-life
    • 27 Majumdar, R., Esfandiary, R., Bishop, S.M., et al. Correlations between changes in conformational dynamics and physical stability in a mutant IgG1 mAb engineered for extended serum half-life. mAbs 7:1 (2015), 84–95.
    • (2015) mAbs , vol.7 , Issue.1 , pp. 84-95
    • Majumdar, R.1    Esfandiary, R.2    Bishop, S.M.3
  • 28
    • 0033519426 scopus 로고    scopus 로고
    • Glycosylation of human IgG-Fc: influences on structure revealed by differential scanning micro-calorimetry
    • 28 Ghirlando, R., Lund, J., Goodall, M., Jefferis, R., Glycosylation of human IgG-Fc: influences on structure revealed by differential scanning micro-calorimetry. Immunol Lett 68:1 (1999), 47–52.
    • (1999) Immunol Lett , vol.68 , Issue.1 , pp. 47-52
    • Ghirlando, R.1    Lund, J.2    Goodall, M.3    Jefferis, R.4
  • 29
    • 84872496673 scopus 로고    scopus 로고
    • Generation and comparative characterization of glycosylated and aglycosylated human IgG1 antibodies
    • 29 Hristodorov, D., Fischer, R., Joerissen, H., Mueller-Tiemann, B., Apeler, H., Linden, L., Generation and comparative characterization of glycosylated and aglycosylated human IgG1 antibodies. Mol Biotechnol 53:3 (2013), 326–335.
    • (2013) Mol Biotechnol , vol.53 , Issue.3 , pp. 326-335
    • Hristodorov, D.1    Fischer, R.2    Joerissen, H.3    Mueller-Tiemann, B.4    Apeler, H.5    Linden, L.6
  • 30
    • 84895924014 scopus 로고    scopus 로고
    • Understanding the relationship between biotherapeutic protein stability and solid–liquid interfacial shear in constant region mutants of IgG1 and IgG4
    • 30 Tavakoli-Keshe, R., Phillips, J.J., Turner, R., Bracewell, D.G., Understanding the relationship between biotherapeutic protein stability and solid–liquid interfacial shear in constant region mutants of IgG1 and IgG4. J Pharm Sci 103:2 (2013), 437–444.
    • (2013) J Pharm Sci , vol.103 , Issue.2 , pp. 437-444
    • Tavakoli-Keshe, R.1    Phillips, J.J.2    Turner, R.3    Bracewell, D.G.4
  • 31
    • 84949568378 scopus 로고    scopus 로고
    • Structural changes and aggregation mechanisms for anti-streptavidin IgG1 at elevated concentration
    • 31 Barnett, G.V., Qi, W., Amin, S., et al. Structural changes and aggregation mechanisms for anti-streptavidin IgG1 at elevated concentration. J Phys Chem B 119:49 (2015), 15150–15163.
    • (2015) J Phys Chem B , vol.119 , Issue.49 , pp. 15150-15163
    • Barnett, G.V.1    Qi, W.2    Amin, S.3
  • 32
    • 84892936418 scopus 로고    scopus 로고
    • Understanding the relevance of local conformational stability and dynamics to the aggregation propensity of an IgG1 and IgG2 monoclonal antibodies
    • 32 Thakkar, S.V., Sahni, N., Joshi, S.B., et al. Understanding the relevance of local conformational stability and dynamics to the aggregation propensity of an IgG1 and IgG2 monoclonal antibodies. Protein Sci 22:10 (2013), 1295–1305.
    • (2013) Protein Sci , vol.22 , Issue.10 , pp. 1295-1305
    • Thakkar, S.V.1    Sahni, N.2    Joshi, S.B.3
  • 33
    • 84897869100 scopus 로고    scopus 로고
    • Immunogenicity of therapeutic proteins: influence of aggregation
    • 33 Ratanji, K.D., Derrick, J.P., Dearman, R.J., Kimber, I., Immunogenicity of therapeutic proteins: influence of aggregation. J Immunotoxicol 11:2 (2014), 99–109.
    • (2014) J Immunotoxicol , vol.11 , Issue.2 , pp. 99-109
    • Ratanji, K.D.1    Derrick, J.P.2    Dearman, R.J.3    Kimber, I.4
  • 34
    • 33646546740 scopus 로고    scopus 로고
    • Antibody response to aggregated human interferon alpha2b in wild-type and transgenic immune tolerant mice depends on type and level of aggregation
    • 34 Hermeling, S., Schellekens, H., Maas, C., Gebbink, M., Crommelin, D.I.A., Jiskoot, W., Antibody response to aggregated human interferon alpha2b in wild-type and transgenic immune tolerant mice depends on type and level of aggregation. J Pharm Sci 95:5 (2006), 1084–1096.
    • (2006) J Pharm Sci , vol.95 , Issue.5 , pp. 1084-1096
    • Hermeling, S.1    Schellekens, H.2    Maas, C.3    Gebbink, M.4    Crommelin, D.I.A.5    Jiskoot, W.6
  • 35
    • 2642550862 scopus 로고    scopus 로고
    • Challenges in the development of high protein concentration formulations
    • 35 Shire, S.J., Shahrokh, Z., Liu, J., Challenges in the development of high protein concentration formulations. J Pharm Sci 93:6 (2004), 1390–1402.
    • (2004) J Pharm Sci , vol.93 , Issue.6 , pp. 1390-1402
    • Shire, S.J.1    Shahrokh, Z.2    Liu, J.3
  • 36
    • 84955192386 scopus 로고    scopus 로고
    • Global and local conformation of human IgG antibody variants rationalizes loss of thermodynamic stability
    • 36 Edgeworth, M.J., Phillips, J.J., Lowe, D.C., Kippen, A.D., Higazi, D.R., Scrivens, J.H., Global and local conformation of human IgG antibody variants rationalizes loss of thermodynamic stability. Angew Chem Int Ed Engl 54:50 (2015), 15156–15159.
    • (2015) Angew Chem Int Ed Engl , vol.54 , Issue.50 , pp. 15156-15159
    • Edgeworth, M.J.1    Phillips, J.J.2    Lowe, D.C.3    Kippen, A.D.4    Higazi, D.R.5    Scrivens, J.H.6
  • 37
    • 0004032583 scopus 로고
    • Sequences of Proteins of Immunological Interest
    • 5th ed. NIH Bethesda, MD Publ. No91–3442
    • 37 Kabat, E.A., Wu, T.T., Perry, H.M., Gottesman, K.S., Foeller, C., Sequences of Proteins of Immunological Interest. 5th ed., 1991, NIH, Bethesda, MD Publ. No91–3442.
    • (1991)
    • Kabat, E.A.1    Wu, T.T.2    Perry, H.M.3    Gottesman, K.S.4    Foeller, C.5
  • 38
    • 79951895571 scopus 로고    scopus 로고
    • Formulation development of therapeutic monoclonal antibodies using high-throughput fluorescence and static light scattering techniques: role of conformational and colloidal stability
    • 38 Goldberg, D.S., Bishop, S.M., Shah, A.U., Sathish, H.A., Formulation development of therapeutic monoclonal antibodies using high-throughput fluorescence and static light scattering techniques: role of conformational and colloidal stability. J Pharm Sci 100:4 (2011), 1306–1315.
    • (2011) J Pharm Sci , vol.100 , Issue.4 , pp. 1306-1315
    • Goldberg, D.S.1    Bishop, S.M.2    Shah, A.U.3    Sathish, H.A.4
  • 39
    • 84961198252 scopus 로고    scopus 로고
    • Inhibition of CD73 AMP hydrolysis by a therapeutic antibody with a dual, non-competitive mechanism of action
    • 39 Geoghegan, J.C., Diedrich, G., Lu, X., et al. Inhibition of CD73 AMP hydrolysis by a therapeutic antibody with a dual, non-competitive mechanism of action. mAbs 8:3 (2016), 454–467.
    • (2016) mAbs , vol.8 , Issue.3 , pp. 454-467
    • Geoghegan, J.C.1    Diedrich, G.2    Lu, X.3
  • 40
    • 84903270626 scopus 로고    scopus 로고
    • Plasmonic measurements of monoclonal antibody self-association using self-interaction nanoparticle spectroscopy
    • 40 Jayaraman, J., Wu, J., Brunelle, M.C., et al. Plasmonic measurements of monoclonal antibody self-association using self-interaction nanoparticle spectroscopy. Biotechnol Bioeng 111:8 (2014), 1513–1520.
    • (2014) Biotechnol Bioeng , vol.111 , Issue.8 , pp. 1513-1520
    • Jayaraman, J.1    Wu, J.2    Brunelle, M.C.3
  • 41
    • 79251581274 scopus 로고    scopus 로고
    • Application of a high-throughput screening procedure with PEG-induced precipitation to compare relative protein solubility during formulation development with IgG1 monoclonal antibodies
    • 41 Gibson, T.J., McCarty, K., McFadyen, I.J., et al. Application of a high-throughput screening procedure with PEG-induced precipitation to compare relative protein solubility during formulation development with IgG1 monoclonal antibodies. J Pharm Sci 100:3 (2011), 1009–1021.
    • (2011) J Pharm Sci , vol.100 , Issue.3 , pp. 1009-1021
    • Gibson, T.J.1    McCarty, K.2    McFadyen, I.J.3
  • 42
    • 0037379288 scopus 로고    scopus 로고
    • The MHC class I-like IgG receptor controls perinatal IgG transport, IgG homeostasis, and fate of IgG-Fc-coupled drugs
    • 42 Roopenian, D.C., Christianson, G.J., Sproule, T.J., et al. The MHC class I-like IgG receptor controls perinatal IgG transport, IgG homeostasis, and fate of IgG-Fc-coupled drugs. J Immunol 170:7 (2003), 3528–3533.
    • (2003) J Immunol , vol.170 , Issue.7 , pp. 3528-3533
    • Roopenian, D.C.1    Christianson, G.J.2    Sproule, T.J.3
  • 43
    • 84922777287 scopus 로고    scopus 로고
    • CD-20 Specific Antibodies and Methods of Employing Same
    • United States Patent Application Publication US2009/0136516 A1
    • 43 Tedder, T.F., Uchida, J., Hamaguchi, Y., Poe, J.C., CD-20 Specific Antibodies and Methods of Employing Same. 2009 United States Patent Application Publication US2009/0136516 A1.
    • (2009)
    • Tedder, T.F.1    Uchida, J.2    Hamaguchi, Y.3    Poe, J.C.4
  • 44
    • 0035194285 scopus 로고    scopus 로고
    • Effector function activities of a panel of mutants of a broadly neutralizing antibody against human immunodeficiency virus type 1
    • 44 Hezareh, M., Hessell, A.J., Jensen, R.C., van de Winkel, J.G.J., Parren, P., Effector function activities of a panel of mutants of a broadly neutralizing antibody against human immunodeficiency virus type 1. J Virol 75:24 (2001), 12161–12168.
    • (2001) J Virol , vol.75 , Issue.24 , pp. 12161-12168
    • Hezareh, M.1    Hessell, A.J.2    Jensen, R.C.3    van de Winkel, J.G.J.4    Parren, P.5
  • 45
    • 84876556946 scopus 로고    scopus 로고
    • Novel asymmetrically engineered antibody Fc variant with superior Fc gamma R binding affinity and specificity compared with afucosylated Fc variant
    • 45 Mimoto, F., Igawa, T., Kuramochi, T., et al. Novel asymmetrically engineered antibody Fc variant with superior Fc gamma R binding affinity and specificity compared with afucosylated Fc variant. mAbs 5:2 (2013), 229–236.
    • (2013) mAbs , vol.5 , Issue.2 , pp. 229-236
    • Mimoto, F.1    Igawa, T.2    Kuramochi, T.3
  • 46
    • 78049344329 scopus 로고    scopus 로고
    • Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation
    • 46 Saluja, A., Fesinmeyer, R.M., Hogan, S., Brems, D.N., Gokarn, Y.R., Diffusion and sedimentation interaction parameters for measuring the second virial coefficient and their utility as predictors of protein aggregation. Biophys J 99:8 (2010), 2657–2665.
    • (2010) Biophys J , vol.99 , Issue.8 , pp. 2657-2665
    • Saluja, A.1    Fesinmeyer, R.M.2    Hogan, S.3    Brems, D.N.4    Gokarn, Y.R.5
  • 47
    • 84860877016 scopus 로고    scopus 로고
    • Behavior of monoclonal antibodies: relation between the second virial coefficient (B-2) at low concentrations and aggregation propensity and viscosity at high concentrations
    • 47 Saito, S., Hasegawa, J., Kobayashi, N., Kishi, N., Uchiyama, S., Fukui, K., Behavior of monoclonal antibodies: relation between the second virial coefficient (B-2) at low concentrations and aggregation propensity and viscosity at high concentrations. Pharm Res 29:2 (2012), 397–410.
    • (2012) Pharm Res , vol.29 , Issue.2 , pp. 397-410
    • Saito, S.1    Hasegawa, J.2    Kobayashi, N.3    Kishi, N.4    Uchiyama, S.5    Fukui, K.6
  • 48
    • 84863491050 scopus 로고    scopus 로고
    • Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter
    • 48 Connolly, B.D., Petry, C., Yadav, S., et al. Weak interactions govern the viscosity of concentrated antibody solutions: high-throughput analysis using the diffusion interaction parameter. Biophys J 103:1 (2012), 69–78.
    • (2012) Biophys J , vol.103 , Issue.1 , pp. 69-78
    • Connolly, B.D.1    Petry, C.2    Yadav, S.3
  • 49
    • 84921328059 scopus 로고    scopus 로고
    • Rational design of viscosity reducing mutants of a monoclonal antibody: hydrophobic versus electrostatic inter-molecular interactions
    • 49 Nichols, P., Li, L., Kumar, S., et al. Rational design of viscosity reducing mutants of a monoclonal antibody: hydrophobic versus electrostatic inter-molecular interactions. mAbs 7:1 (2015), 212–230.
    • (2015) mAbs , vol.7 , Issue.1 , pp. 212-230
    • Nichols, P.1    Li, L.2    Kumar, S.3
  • 50
    • 84881309816 scopus 로고    scopus 로고
    • Application of a PEG precipitation method for solubility screening: a tool for developing high protein concentration formulations
    • 50 Li, L., Kantor, A., Warne, N., Application of a PEG precipitation method for solubility screening: a tool for developing high protein concentration formulations. Protein Sci 22:8 (2013), 1118–1123.
    • (2013) Protein Sci , vol.22 , Issue.8 , pp. 1118-1123
    • Li, L.1    Kantor, A.2    Warne, N.3
  • 51
    • 77957244161 scopus 로고    scopus 로고
    • B-cell depletion in vitro and in vivo with an afucosylated anti-CD19 antibody
    • 51 Herbst, R., Wang, Y., Gallagher, S., et al. B-cell depletion in vitro and in vivo with an afucosylated anti-CD19 antibody. J Pharmacol Exp Ther 335:1 (2010), 213–222.
    • (2010) J Pharmacol Exp Ther , vol.335 , Issue.1 , pp. 213-222
    • Herbst, R.1    Wang, Y.2    Gallagher, S.3
  • 52
    • 84877898507 scopus 로고    scopus 로고
    • Correlations between pharmacokinetics of IgG antibodies in primates vs. FcRn-transgenic mice reveal a rodent model with predictive capabilities
    • 52 Tam, S.H., McCarthy, S.G., Brosnan, K., Goldberg, K.M., Scallon, B.J., Correlations between pharmacokinetics of IgG antibodies in primates vs. FcRn-transgenic mice reveal a rodent model with predictive capabilities. mAbs 5:3 (2013), 397–405.
    • (2013) mAbs , vol.5 , Issue.3 , pp. 397-405
    • Tam, S.H.1    McCarthy, S.G.2    Brosnan, K.3    Goldberg, K.M.4    Scallon, B.J.5
  • 53
    • 39149106011 scopus 로고    scopus 로고
    • Structural characterization of a mutated, ADCC-enhanced human Fc fragment
    • 53 Oganesyan, V., Damschroder, M.M., Leach, W., Wu, H., Dall'Acqua, W.F., Structural characterization of a mutated, ADCC-enhanced human Fc fragment. Mol Immunol 45:7 (2008), 1872–1882.
    • (2008) Mol Immunol , vol.45 , Issue.7 , pp. 1872-1882
    • Oganesyan, V.1    Damschroder, M.M.2    Leach, W.3    Wu, H.4    Dall'Acqua, W.F.5
  • 54
    • 84926671056 scopus 로고    scopus 로고
    • Examination of thermal unfolding and aggregation profiles of a series of developable therapeutic monoclonal antibodies
    • 54 Brader, M.L., Estey, T., Bai, S., et al. Examination of thermal unfolding and aggregation profiles of a series of developable therapeutic monoclonal antibodies. Mol Pharm 12:4 (2015), 1005–1017.
    • (2015) Mol Pharm , vol.12 , Issue.4 , pp. 1005-1017
    • Brader, M.L.1    Estey, T.2    Bai, S.3
  • 55
    • 84864319122 scopus 로고    scopus 로고
    • Comparison of high-throughput biophysical methods to identify stabilizing excipients for a model IgG2 monoclonal antibody: conformational stability and kinetic aggregation measurements
    • 55 Cheng, W.Q., Joshi, S.B., He, F., et al. Comparison of high-throughput biophysical methods to identify stabilizing excipients for a model IgG2 monoclonal antibody: conformational stability and kinetic aggregation measurements. J Pharm Sci 101:5 (2012), 1701–1720.
    • (2012) J Pharm Sci , vol.101 , Issue.5 , pp. 1701-1720
    • Cheng, W.Q.1    Joshi, S.B.2    He, F.3
  • 56
    • 84858176295 scopus 로고    scopus 로고
    • Avidity confers Fc gamma R binding and immune effector function to aglycosylated immunoglobulin G1
    • 56 Nesspor, T.C., Raju, T.S., Chin, C.N., Vafa, O., Brezski, R.J., Avidity confers Fc gamma R binding and immune effector function to aglycosylated immunoglobulin G1. J Mol Recognit 25:3 (2012), 147–154.
    • (2012) J Mol Recognit , vol.25 , Issue.3 , pp. 147-154
    • Nesspor, T.C.1    Raju, T.S.2    Chin, C.N.3    Vafa, O.4    Brezski, R.J.5


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