3,970
Views
45
CrossRef citations to date
0
Altmetric
Report

Influence of glycosylation pattern on the molecular properties of monoclonal antibodies

, , , &
Pages 649-658 | Received 14 Feb 2014, Accepted 18 Mar 2014, Published online: 24 Mar 2014

References

  • 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
  • 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
  • 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
  • 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
  • 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
  • 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
  • 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.
  • 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
  • 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
  • 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
  • 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
  • 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
  • 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
  • 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 antibody-dependent cellular toxicity. J Biol Chem 2002; 277:26733 - 40; http://dx.doi.org/10.1074/jbc.M202069200; PMID: 11986321
  • Kukuruzinska MA, Lennon K. Protein N-glycosylation: molecular genetics and functional significance. Crit Rev Oral Biol Med 1998; 9:415 - 48; http://dx.doi.org/10.1177/10454411980090040301; PMID: 9825220
  • 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
  • Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug Discov 2009; 8:226 - 34; http://dx.doi.org/10.1038/nrd2804; PMID: 19247305
  • 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
  • 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
  • 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
  • Zheng K, Bantog C, Bayer R. The impact of glycosylation on monoclonal antibody conformation and stability. MAbs 2011; 3:568 - 76; http://dx.doi.org/10.4161/mabs.3.6.17922; PMID: 22123061
  • Fabian H, Naumann D. Methods to study protein folding by stopped-flow FT-IR. Methods 2004; 34:28 - 40; http://dx.doi.org/10.1016/j.ymeth.2004.03.004; PMID: 15283913
  • Surewicz WK, Mantsch HH. New insight into protein secondary structure from resolution-enhanced infrared spectra. Biochim Biophys Acta 1988; 952:115 - 30; http://dx.doi.org/10.1016/0167-4838(88)90107-0; PMID: 3276352
  • 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
  • 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; http://dx.doi.org/10.1002/jps.21104; PMID: 17721938
  • 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
  • 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
  • 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
  • Feige MJ, Walter S, Buchner J. Folding mechanism of the CH2 antibody domain. J Mol Biol 2004; 344:107 - 18; http://dx.doi.org/10.1016/j.jmb.2004.09.033; PMID: 15504405
  • 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
  • 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; http://dx.doi.org/10.1021/bi00167a003; PMID: 8286336
  • 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; http://dx.doi.org/10.1016/j.jchromb.2011.08.015; PMID: 21900054

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.