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Short Communication

Glycosylation of random IgG distinguishes seropositive and seronegative rheumatoid arthritis

, , ORCID Icon, , , , , , , , , & ORCID Icon show all
Pages 111-117 | Received 01 Feb 2018, Accepted 20 Apr 2018, Published online: 07 May 2018

References

  • Nimmerjahn F, Anthony RM, Ravetch JV. Agalactosylated IgG antibodies depend on cellular Fc receptors for in vivo activity. Proc Natl Acad Sci USA. 2007;104:8433–8437.
  • Scanlan CN, Burton DR, Dwek RA. Making autoantibodies safe. Proc Natl Acad Sci USA. 2008;105:4081–4082.
  • Kaneko Y, Nimmerjahn F, Ravetch JV. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science. 2006;313:670–673.
  • Meier S, Duus J. Carbohydrate dynamics: antibody glycans wiggle and jiggle. Nat Chem Biol. 2011;7:131–132.
  • Seeling M, Brückner C, Nimmerjahn F. Differential antibody glycosylation in autoimmunity: sweet biomarker or modulator of disease activity? Nat Rev Rheumatol. 2017;13:621–630.
  • Ludwig RJ, Vanhoorelbeke K, Leypoldt F, et al. Mechanisms of autoantibody-induced pathology. Front Immunol. 2017;8:603.
  • DiLillo DJ, Ravetch JV. Fc-receptor interactions regulate both cytotoxic and immunomodulatory therapeutic antibody effector functions. Cancer Immunol Res. 2015;3:704–713.
  • Trbojević-Akmačić I, Vilaj M, Lauc G. High-throughput analysis of immunoglobulin G glycosylation. Expert Rev Proteomics. 2016;13:523–534.
  • Shinkawa T, Nakamura K, Yamane N, et al. The absence of Fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J Biol Chem. 2003;278:3466–3473.
  • Ferrara C, Brünker P, Suter T, et al. Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous β1, 4-N-acetylglucosaminyltransferase III and Golgi α-mannosidase II. Biotechnol Bioeng. 2006;93:851–861.
  • Shields RL, Lai J, Keck R, et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity. J Biol Chem. 2002;277:26733–26740.
  • Matsumiya S, Yamaguchi Y, Saito J, et al. Structural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1. J Mol Biol. 2007;368:767–779.
  • Le NPL, Bowden TA, Struwe WB, et al. Immune recruitment or suppression by glycan engineering of endogenous and therapeutic antibodies. Biochim Biophys Acta - Gen Subj. 2016;1860:1655–1668.
  • Li T, DiLillo DJ, Bournazos S, et al. Modulating IgG effector function by Fc glycan engineering. Proc Natl Acad Sci USA. 2017;114:3485–3490.
  • Washburn N, Schwab I, Ortiz D, et al. Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity. Proc Natl Acad Sci USA. 2015;112:E1297–E1306.
  • Almeida A, Kolarich D. The promise of protein glycosylation for personalised medicine. Biochim Biophys Acta Gen Subj. 2016;1860:1583–1595. [Internet].
  • Kao D, Lux A, Schaffert A, et al. IgG subclass and vaccination stimulus determine changes in antigen specific antibody glycosylation in mice. Eur J Immunol. 2017;47:2070–2079.
  • Biermann MHC, Griffante G, Podolska MJ, et al. Sweet but dangerous – the role of immunoglobulin G glycosylation in autoimmunity and inflammation. Lupus. 2016;25:934–942.
  • Sjöwall C, Zapf J, von Löhneysen S, et al. Altered glycosylation of complexed native IgG molecules is associated with disease activity of systemic lupus erythematosus. Lupus. 2015;24:569–581.
  • Fickentscher C, Magorivska I, Janko C, et al. The pathogenicity of anti-β2GP1-IgG autoantibodies depends on Fc glycosylation. J Immunol Res. 2015;2015:1–12.
  • Stümer J, Biermann MHCHC, Knopf J, et al. Altered glycan accessibility on native immunoglobulin G complexes in early rheumatoid arthritis and its changes during therapy. Clin Exp Immunol. 2017;189:372–382.
  • Magorivska I, Muñoz LE, Janko C, et al. Sialylation of anti-histone immunoglobulin G autoantibodies determines their capabilities to participate in the clearance of late apoptotic cells. Clin Exp Immunol. 2016;184:110–117.
  • Hajba L, Csanky E, Guttman A. Liquid phase separation methods for N-glycosylation analysis of glycoproteins of biomedical and biopharmaceutical interest: a critical review. Anal Chim Acta. 2016;943:8–16.
  • Chen S, Lu C, Gu H, et al. Aleuria Aurantia lectin (AAL)-reactive immunoglobulin G rapidly appears in sera of animals following antigen exposure. PLoS One. 2012;7:e44422.
  • Jefferis R. Glycosylation as a strategy to improve antibody-based therapeutics. Nat Rev Drug Discov. 2009;8:226–234.
  • Chui D, Sellakumar G, Green RS, et al. Genetic remodeling of protein glycosylation in vivo induces autoimmune disease. Proc Natl Acad Sci. 2001;98:1142–1147.
  • Visser A, Hamza N, Kroese FGM, et al. Acquiring new N-glycosylation sites in variable regions of immunoglobulin genes by somatic hypermutation is a common feature of autoimmune diseases. Ann Rheum Dis 2017. DOI:10.1136/annrheumdis-2017-212568
  • Hafkenscheid L, Bondt A, Scherer HU, et al. Structural analysis of variable domain glycosylation of anti-citrullinated protein antibodies in rheumatoid arthritis reveals the presence of highly sialylated glycans. Mol Cell Proteomics. 2017;16:278–287.

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