NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic (original) (raw)

• Roitt, I.M., Brostoff, J. & Male, D.K. Immunology 6th edn. (Mosby, 2001).
• Goronzy, J.J. & Weyand, C.M. Developments in the scientific understanding of rheumatoid arthritis. Arthritis Res. Ther. 11, 249 (2009).
  Article Google Scholar
• Arnold, J.N. et al. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 25, 21–50 (2007).
  Article CAS Google Scholar
• Alavi, A. & Axford, J.S. Sweet and sour: the impact of sugars on disease. Rheumatology 47, 760–770 (2008).
  Article CAS Google Scholar
• Parekh, R.B. et al. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 316, 452–457 (1985).
  Article CAS Google Scholar
• Kaneko, Y., Nimmerjahn, F., Madaio, M.P. & Ravetch, J.V. Pathology and protection in nephrotoxic nephritis is determined by selective engagement of specific Fc receptors. J. Exp. Med. 203, 789–797 (2006).
  Article CAS Google Scholar
• Anthony, R.M. et al. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science 320, 373–376 (2008).
  Article CAS Google Scholar
• Malhotra, R. et al. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nat. Med. 1, 237–243 (1995).
  Article CAS Google Scholar
• Yamaguchi, Y. et al. Glycoform-dependent conformational alteration of the Fc region of human immunoglobulin G1 as revealed by NMR spectroscopy. Biochim. Biophys. Acta 1760, 693–700 (2006).
  Article CAS Google Scholar
• Mimura, Y. et al. Role of oligosaccharide residues of IgG1-Fc in Fc γ RIIb binding. J. Biol. Chem. 276, 45539–45547 (2001).
  Article CAS Google Scholar
• Scallon, B.J. et al. Higher levels of sialylated Fc glycans in immunoglobulin G molecules can adversely impact functionality. Mol. Immunol. 44, 1524–1534 (2007).
  Article CAS Google Scholar
• Anthony, R.M., Wermeling, F., Karlsson, M.C. & Ravetch, J.V. Identification of a receptor required for the anti-inflammatory activity of IVIG. Proc. Natl. Acad. Sci. USA 105, 19571–19578 (2008).
  Article CAS Google Scholar
• Burmeister, W.P., Huber, A.H. & Bjorkman, P.J. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 372, 379–383 (1994).
  Article CAS Google Scholar
• Sondermann, P., Huber, R., Oosthuizen, V. & Jacob, U. The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc γRIII complex. Nature 406, 267–273 (2000).
  Article CAS Google Scholar
• Radaev, S. et al. The structure of a human type III Fcγ receptor in complex with Fc. J. Biol. Chem. 276, 16469–16477 (2001).
  Article CAS Google Scholar
• Idusogie, E.E. et al. Mapping of the C1q binding site on rituxan, a chimeric antibody with a human IgG1 Fc. J. Immunol. 164, 4178–4184 (2000).
  Article CAS Google Scholar
• Deisenhofer, J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution. Biochemistry 20, 2361–2370 (1981).
  Article CAS Google Scholar
• Yamaguchi, Y. et al. Dynamics of the carbohydrate chains attached to the Fc portion of immunoglobulin G as studied by NMR spectroscopy assisted by selective C-13 labeling of the glycans. J. Biomol. NMR 12, 385–394 (1998).
  Article CAS Google Scholar
• Wormald, M.R. et al. Variations in oligosaccharide-protein interactions in immunoglobulin G determine the site-specific glycosylation profiles and modulate the dynamic motion of the Fc oligosaccharides. Biochemistry 36, 1370–1380 (1997).
  Article CAS Google Scholar
• Kobata, A. The N-linked sugar chains of human immunoglobulin G: their unique pattern, and their functional roles. Biochim. Biophys. Acta 1780, 472–478 (2008).
  Article CAS Google Scholar
• Barb, A.W., Brady, E.K. & Prestegard, J.H. Branch-specific sialylation of IgG-Fc glycans by ST6Gal-I. Biochemistry 48, 9705–9707 (2009).
  Article CAS Google Scholar
• Mittermaier, A. & Kay, L.E. New tools provide new insights in NMR studies of protein dynamics. Science 312, 224–228 (2006).
  Article CAS Google Scholar
• Chang, V.T. et al. Glycoprotein structural genomics: solving the glycosylation problem. Structure 15, 267–273 (2007).
  Article CAS Google Scholar
• Barb, A.W. et al. Intramolecular glycan-protein interactions in glycoproteins. Methods Enzymol. 477, 365–388 (2010).
  Article Google Scholar
• Cavanagh, J. Protein NMR Spectroscopy: Principles and Practice 2nd edn. (Academic Press, 2007).
• Palmer, A.G. III, Kroenke, C.D. & Loria, J.P. Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol. 339, 204–238 (2001).
  Article CAS Google Scholar
• Hansen, D.F. et al. Probing chemical shifts of invisible states of proteins with relaxation dispersion NMR spectroscopy: how well can we do? J. Am. Chem. Soc. 130, 2667–2675 (2008).
  Article CAS Google Scholar
• Raju, T.S. Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr. Opin. Immunol. 20, 471–478 (2008).
  Article CAS Google Scholar
• Bock, K., Pedersen, C. & Pedersen, H. Carbon-13 nuclear magnetic resonance data for oligosaccharides. Adv. Carbohydr. Chem. Biochem. 42, 193–225 (1984).
  Article CAS Google Scholar
• Wieruszeski, J.M., Michalski, J.C., Montreuil, J. & Strecker, G. Sequential H-1 and C-13 resonance assignments for an octasaccharide and decasaccharide of the _N_-acetyllactosamine type by multiple-step relayed correlation and hetero-nuclear correlation nuclear magnetic-resonance. Glycoconj. J. 6, 183–194 (1989).
  Article CAS Google Scholar
• Vliegenthart, J.F.G., Dorland, L. & van Halbeek, H. High-resolution, 1H-nuclear magnetic resonance spectroscopy as a tool in the structural analysis of carbohydrates related to glycoproteins. Adv. Carbohydr. Chem. Biochem. 41, 209–374 (1983).
  Article CAS Google Scholar
• Voynov, V. et al. Dynamic fluctuations of protein-carbohydrate interactions promote protein aggregation. PLoS ONE 4, e8425 (2009).
  Article Google Scholar
• Lipari, G. & Szabo, A. Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 1. Theory and range of validity. J. Am. Chem. Soc. 104, 4546–4559 (1982).
  Article CAS Google Scholar
• Lipari, G. & Szabo, A. Model-free approach to the interpretation of nuclear magnetic-resonance relaxation in macromolecules. 2. Analysis of experimental results. J. Am. Chem. Soc. 104, 4559–4570 (1982).
  Article CAS Google Scholar
• Raju, T.S. et al. Glycoengineering of therapeutic glycoproteins: in vitro galactosylation and sialylation of glycoproteins with terminal _N_-acetylglucosamine and galactose residues. Biochemistry 40, 8868–8876 (2001).
  Article CAS Google Scholar
• Lund, J. et al. Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc γ receptor I and influence the synthesis of its oligosaccharide chains. J. Immunol. 157, 4963–4969 (1996).
  CAS PubMed Google Scholar
• DeLano, W.L., Ultsch, M.H., de Vos, A.M. & Wells, J.A. Convergent solutions to binding at a protein-protein interface. Science 287, 1279–1283 (2000).
  Article CAS Google Scholar
• Hirotsu, K. & Shimada, A. Crystal and molecular-structure of β-lactose. Bull. Chem. Soc. Jpn. 47, 1872–1879 (1974).
  Article CAS Google Scholar