메뉴 건너뛰기




Volumn 6, Issue 3, 2014, Pages 649-658

Influence of glycosylation pattern on the molecular properties of monoclonal antibodies

Author keywords

Differential scanning calorimetry; Fourier transform infrared spectroscopy; Glycosylation; Intrinsic fluorescence; Liquid chromatography mass spectroscopy; Monoclonal antibody; Size exclusion chromatography; Stability

Indexed keywords

IMMUNOGLOBULIN G1 ANTIBODY; MANNOSE; MONOCLONAL ANTIBODY; N ACETYLGLUCOSAMINE; PROTEINASE; PEPTIDE HYDROLASE;

EID: 84899769052     PISSN: 19420862     EISSN: 19420870     Source Type: Journal    
DOI: 10.4161/mabs.28588     Document Type: Article
Times cited : (52)

References (32)
  • 1
    • 28044433451 scopus 로고    scopus 로고
    • Protein posttranslational modifications: The chemistry of proteome diversifications
    • PMID:16267872
    • Walsh CT, Garneau-Tsodikova S, Gatto GJ Jr. Protein posttranslational modifications: the chemistry of proteome diversifications. Angew Chem Int Ed Engl 2005; 44:7342-72; http://dx.doi.org/10.1002/anie.200501023; PMID:16267872
    • (2005) Angew Chem Int Ed Engl , vol.44 , pp. 7342-7372
    • Walsh, C.T.1    Garneau-Tsodikova, S.2    Gatto Jr., G.J.3
  • 2
    • 33749860977 scopus 로고    scopus 로고
    • Post-translational modifications in the context of therapeutic proteins
    • PMID:17033665
    • Walsh G, Jefferis R. Post-translational modifications in the context of therapeutic proteins. Nat Biotechnol 2006; 24:1241-52; http://dx.doi.org/10. 1038/nbt1252; PMID:17033665
    • (2006) Nat Biotechnol , vol.24 , pp. 1241-1252
    • Walsh, G.1    Jefferis, R.2
  • 3
    • 79960946480 scopus 로고    scopus 로고
    • NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation
    • PMID:21750686
    • Van Damme P, Hole K, Pimenta-Marques A, Helsens K, Vandekerckhove J, Martinho RG, Gevaert K, Arnesen T. NatF contributes to an evolutionary shift in protein N-terminal acetylation and is important for normal chromosome segregation. PLoS Genet 2011; 7:e1002169; http://dx.doi.org/10.1371/journal. pgen.1002169; PMID:21750686
    • (2011) PLoS Genet , vol.7
    • Van Damme, P.1    Hole, K.2    Pimenta-Marques, A.3    Helsens, K.4    Vandekerckhove, J.5    Martinho, R.G.6    Gevaert, K.7    Arnesen, T.8
  • 4
    • 79960338300 scopus 로고    scopus 로고
    • Multiple post-translational modifications in hepatocyte nuclear factor 4α
    • PMID:21708125
    • Yokoyama A, Katsura S, Ito R, Hashiba W, Sekine H, Fujiki R, Kato S. Multiple post-translational modifications in hepatocyte nuclear factor 4α. Biochem Biophys Res Commun 2011; 410:749-53; http://dx.doi.org/10.1016/j.bbrc. 2011.06.033; PMID:21708125
    • (2011) Biochem Biophys Res Commun , vol.410 , pp. 749-753
    • Yokoyama, A.1    Katsura, S.2    Ito, R.3    Hashiba, W.4    Sekine, H.5    Fujiki, R.6    Kato, S.7
  • 5
    • 0030699146 scopus 로고    scopus 로고
    • Amidation of bioactive peptides: The structure of peptidylglycine alpha-hydroxylating monooxygenase
    • PMID:9360928
    • Prigge ST, Kolhekar AS, Eipper BA, Mains RE, Amzel LM. Amidation of bioactive peptides: the structure of peptidylglycine alpha-hydroxylating monooxygenase. Science 1997; 278:1300-5; http://dx.doi.org/10.1126/science.278. 5341.1300; PMID:9360928
    • (1997) Science , vol.278 , pp. 1300-1305
    • Prigge, S.T.1    Kolhekar, A.S.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 6
    • 0000821179 scopus 로고    scopus 로고
    • New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function
    • PMID:11028916
    • Prigge ST, Mains RE, Eipper BA, Amzel LM. New insights into copper monooxygenases and peptide amidation: structure, mechanism and function. Cell Mol Life Sci 2000; 57:1236-59; http://dx.doi.org/10.1007/PL00000763; PMID:11028916
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1236-1259
    • Prigge, S.T.1    Mains, R.E.2    Eipper, B.A.3    Amzel, L.M.4
  • 7
    • 78649919102 scopus 로고    scopus 로고
    • Biopharmaceuticals: Post-translational modification carboxylation and hydroxylation
    • Walsh G, ed. Weinheim: Wiley-VCH Verlag GmbH & Co.
    • Brown MA, Stenberg LM. Biopharmaceuticals: post-translational modification carboxylation and hydroxylation. In: Walsh G, ed. Post-translational modification of protein biopharmaceuticals. Weinheim: Wiley-VCH Verlag GmbH & Co., 2009:209-52.
    • (2009) Post-translational Modification of Protein Biopharmaceuticals , pp. 209-252
    • Brown, M.A.1    Stenberg, L.M.2
  • 8
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • PMID:17029568
    • Arnold JN, Wormald MR, Sim RB, Rudd PM, Dwek RA. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu Rev Immunol 2007; 25:21-50; http://dx.doi.org/10.1146/annurev.immunol.25. 022106.141702; PMID:17029568
    • (2007) Annu Rev Immunol , vol.25 , pp. 21-50
    • Arnold, J.N.1    Wormald, M.R.2    Sim, R.B.3    Rudd, P.M.4    Dwek, R.A.5
  • 9
    • 0026661583 scopus 로고
    • Signal integration at the level of protein kinases, protein phosphatases and their substrates
    • PMID:1333658
    • Cohen P. Signal integration at the level of protein kinases, protein phosphatases and their substrates. Trends Biochem Sci 1992; 17:408-13; http://dx.doi.org /10.1016/0968-0004(92)90010-7; PMID:1333658
    • (1992) Trends Biochem Sci , vol.17 , pp. 408-413
    • Cohen, P.1
  • 10
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • PMID:12007495
    • Mann M, Ong SE, Grønborg M, Steen H, Jensen ON, Pandey A. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol 2002; 20:261-8; http://dx.doi.org/10.1016/ S0167-7799(02)01944-3; PMID:12007495
    • (2002) Trends Biotechnol , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Grønborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6
  • 11
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: Nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • PMID:12042244
    • Spiro RG. Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 2002; 12:43R-56R; http://dx.doi.org/10.1093/glycob/12.4.43R; PMID:12042244
    • (2002) Glycobiology , vol.12
    • Spiro, R.G.1
  • 12
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • PMID:8490246
    • Varki A. Biological roles of oligosaccharides: all of the theories are correct. Glycobiology 1993; 3:97-130; http://dx.doi.org/10.1093/glycob/3.2.97; PMID:8490246
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 13
    • 0024270999 scopus 로고
    • Glycosylation at specific sites of erythropoietin is essential for biosynthesis, secretion, and biological function
    • PMID:3182860
    • Dubé S, Fisher JW, Powell JS. Glycosylation at specific sites of erythropoietin is essential for biosynthesis, secretion, and biological function. J Biol Chem 1988; 263:17516-21; PMID:3182860
    • (1988) J Biol Chem , vol.263 , pp. 17516-17521
    • Dubé, S.1    Fisher, J.W.2    Powell, J.S.3
  • 14
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibodydependent cellular toxicity
    • PMID:11986321
    • Shields RL, Lai J, Keck R, O'Connell LY, Hong K, Meng YG, Weikert SH, Presta LG. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibodydependent cellular toxicity. J Biol Chem 2002; 277:26733-40; http://dx.doi.org/10.1074/jbc.M202069200; PMID:11986321
    • (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
  • 15
    • 0032321747 scopus 로고    scopus 로고
    • Protein N-glycosylation: Molecular genetics and functional significance
    • PMID:9825220
    • Kukuruzinska MA, Lennon K. Protein N-glycosylation: molecular genetics and functional significance. Crit Rev Oral Biol Med 1998; 9:415-48; PMID:9825220; http://dx.doi.org/10.1177/10454411980090040301
    • (1998) Crit Rev Oral Biol Med , vol.9 , pp. 415-448
    • Kukuruzinska, M.A.1    Lennon, K.2
  • 16
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • PMID:12527303
    • Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J Mol Biol 2003; 325:979-89; http://dx.doi.org/10.1016/ S0022-2836(02)01250-0; PMID:12527303
    • (2003) J Mol Biol , vol.325 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 17
    • 61649087668 scopus 로고    scopus 로고
    • Glycosylation as a strategy to improve antibody-based therapeutics
    • PMID:19247305
    • Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug Discov 2009; 8:226-34; PMID:19247305; http://dx.doi.org/10.1038/nrd2804
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 226-234
    • Jefferis, R.1
  • 18
    • 33845590523 scopus 로고    scopus 로고
    • Comparison of biological activity among nonfucosylated therapeutic IgG1 antibodies 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 IgG1 antibodies with three different N-linked Fc oligosaccharides: the high-mannose, hybrid, and complex types. Glycobiology 2007; 17:104-18; http://dx.doi.org/10.1093/glycob/cwl057; PMID:17012310
    • (2007) 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
  • 19
    • 38449115463 scopus 로고    scopus 로고
    • Development of a simple and rapid method for producing non-fucosylated oligomannose containing antibodies with increased effector function
    • PMID:17680659
    • Zhou Q, Shankara S, Roy A, Qiu H, Estes S, McVie-Wylie A, Culm-Merdek K, Park A, Pan C, Edmunds T. Development of a simple and rapid method for producing non-fucosylated oligomannose containing antibodies with increased effector function. Biotechnol Bioeng 2008; 99:652-65; http://dx.doi.org/10.1002/bit. 21598; PMID:17680659
    • (2008) Biotechnol Bioeng , vol.99 , pp. 652-665
    • Zhou, Q.1    Shankara, S.2    Roy, A.3    Qiu, H.4    Estes, S.5    McVie-Wylie, A.6    Culm-Merdek, K.7    Park, A.8    Pan, C.9    Edmunds, T.10
  • 20
    • 63449138097 scopus 로고    scopus 로고
    • Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions
    • PMID:19236877
    • Crispin M, Bowden TA, Coles CH, Harlos K, Aricescu AR, Harvey DJ, Stuart DI, Jones EY. Carbohydrate and domain architecture of an immature antibody glycoform exhibiting enhanced effector functions. J Mol Biol 2009; 387:1061-6; http://dx.doi.org/10.1016/j.jmb.2009.02.033; PMID:19236877
    • (2009) J Mol Biol , vol.387 , pp. 1061-1066
    • Crispin, M.1    Bowden, T.A.2    Coles, C.H.3    Harlos, K.4    Aricescu, A.R.5    Harvey, D.J.6    Stuart, D.I.7    Jones, E.Y.8
  • 21
    • 81255197729 scopus 로고    scopus 로고
    • The impact of glycosylation on monoclonal antibody conformation and stability
    • PMID:22123061
    • Zheng K, Bantog C, Bayer R. The impact of glycosylation on monoclonal antibody conformation and stability. MAbs 2011; 3:568-76; PMID:22123061; http://dx.doi.org/10.4161/mabs.3.6.17922
    • (2011) MAbs , vol.3 , pp. 568-576
    • Zheng, K.1    Bantog, C.2    Bayer, R.3
  • 22
    • 3343000049 scopus 로고    scopus 로고
    • Methods to study protein folding by stopped-flow FT-IR
    • PMID:15283913
    • Fabian H, Naumann D. Methods to study protein folding by stopped-flow FT-IR. Methods 2004; 34:28-40; PMID:15283913; http://dx.doi.org/10.1016/j.ymeth. 2004.03.004
    • (2004) Methods , vol.34 , pp. 28-40
    • Fabian, H.1    Naumann, D.2
  • 23
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolutionenhanced infrared spectra
    • PMID:3276352
    • Surewicz WK, Mantsch HH. New insight into protein secondary structure from resolutionenhanced infrared spectra. Biochim Biophys Acta 1988; 952:115-30; PMID:3276352; http://dx.doi.org/10.1016/0167-4838(88)90107-0
    • (1988) Biochim Biophys Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 24
    • 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
    • PMID:11275255
    • Mimura Y, Church S, Ghirlando R, Ashton PR, Dong S, Goodall M, Lund J, 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 2000; 37:697-706; http://dx.doi.org/10.1016/S0161- 5890(00)00105-X; PMID:11275255
    • (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
  • 25
    • 43249105327 scopus 로고    scopus 로고
    • Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies
    • PMID:17721938
    • Ionescu RM, Vlasak J, Price C, Kirchmeier M. Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies. J Pharm Sci 2008; 97:1414-26; PMID:17721938; http://dx.doi.org/10.1002/jps.21104
    • (2008) J Pharm Sci , vol.97 , pp. 1414-1426
    • Ionescu, R.M.1    Vlasak, J.2    Price, C.3    Kirchmeier, M.4
  • 26
    • 39149138479 scopus 로고    scopus 로고
    • Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid
    • PMID:18157932
    • Ryan MH, Petrone D, Nemeth JF, Barnathan E, Björck L, Jordan RE. Proteolysis of purified IgGs by human and bacterial enzymes in vitro and the detection of specific proteolytic fragments of endogenous IgG in rheumatoid synovial fluid. Mol Immunol 2008; 45:1837-46; http://dx.doi.org/10.1016/j. molimm.2007.10.043; PMID:18157932
    • (2008) Mol Immunol , vol.45 , pp. 1837-1846
    • Ryan, M.H.1    Petrone, D.2    Nemeth, J.F.3    Barnathan, E.4    Björck, L.5    Jordan, R.E.6
  • 27
    • 34547909649 scopus 로고    scopus 로고
    • Fc glycans terminated with N-acetylglucosamine residues increase antibody resistance to papain
    • PMID:17571902
    • Raju TS, Scallon B. Fc glycans terminated with N-acetylglucosamine residues increase antibody resistance to papain. Biotechnol Prog 2007; 23:964-71; http://dx.doi.org/10.1002/bp070118k; PMID:17571902
    • (2007) Biotechnol Prog , vol.23 , pp. 964-971
    • Raju, T.S.1    Scallon, B.2
  • 28
    • 46749112184 scopus 로고    scopus 로고
    • Fragmentation of a recombinant monoclonal antibody at various pH
    • PMID:18473123
    • Gaza-Bulseco G, Liu H. Fragmentation of a recombinant monoclonal antibody at various pH. Pharm Res 2008; 25:1881-90; http://dx.doi.org/10.1007/s11095- 008-9606-3; PMID:18473123
    • (2008) Pharm Res , vol.25 , pp. 1881-1890
    • Gaza-Bulseco, G.1    Liu, H.2
  • 29
    • 7044247460 scopus 로고    scopus 로고
    • Folding mechanism of the CH2 antibody domain
    • PMID:15504405
    • Feige MJ, Walter S, Buchner J. Folding mechanism of the CH2 antibody domain. J Mol Biol 2004; 344:107-18; PMID:15504405; http://dx.doi.org/10.1016/j. jmb.2004.09.033
    • (2004) J Mol Biol , vol.344 , pp. 107-118
    • Feige, M.J.1    Walter, S.2    Buchner, J.3
  • 30
    • 31744447070 scopus 로고    scopus 로고
    • Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain
    • PMID:16442075
    • Raju TS, Scallon BJ. Glycosylation in the Fc domain of IgG increases resistance to proteolytic cleavage by papain. Biochem Biophys Res Commun 2006; 341:797-803; http://dx.doi.org/10.1016/j.bbrc.2006.01.030; PMID:16442075
    • (2006) Biochem Biophys Res Commun , vol.341 , pp. 797-803
    • Raju, T.S.1    Scallon, B.J.2
  • 31
    • 0027957966 scopus 로고
    • Glycoforms modify the dynamic stability and functional activity of an enzyme
    • PMID:8286336
    • Rudd PM, Joao HC, Coghill E, Fiten P, Saunders MR, Opdenakker G, Dwek RA. Glycoforms modify the dynamic stability and functional activity of an enzyme. Biochemistry 1994; 33:17-22; PMID:8286336; http://dx.doi.org/10.1021/bi00167a003
    • (1994) Biochemistry , vol.33 , pp. 17-22
    • Rudd, P.M.1    Joao, H.C.2    Coghill, E.3    Fiten, P.4    Saunders, M.R.5    Opdenakker, G.6    Dwek, R.A.7
  • 32
    • 80052930496 scopus 로고    scopus 로고
    • Detection and identification of a serine to arginine sequence variant in a therapeutic monoclonal antibody
    • PMID:21900054
    • Ren D, Zhang J, Pritchett R, Liu H, Kyauk J, Luo J, Amanullah A. Detection and identification of a serine to arginine sequence variant in a therapeutic monoclonal antibody. J Chromatogr B Analyt Technol Biomed Life Sci 2011; 879:2877-84; PMID:21900054; http://dx.doi.org/10.1016/j.jchromb.2011.08. 015
    • (2011) J Chromatogr B Analyt Technol Biomed Life Sci , vol.879 , pp. 2877-2884
    • Ren, D.1    Zhang, J.2    Pritchett, R.3    Liu, H.4    Kyauk, J.5    Luo, J.6    Amanullah, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.