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Volumn 51, Issue 22, 2012, Pages 4618-4626

NMR characterization of immunoglobulin G Fc glycan motion on enzymatic sialylation

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-INFLAMMATORIES; AUTOIMMUNE DISEASE; BULK SOLVENTS; ENZYMATIC MODIFICATION; IMMUNOGLOBULIN G; N-ACETYLNEURAMINIC ACID; N-GLYCAN; SIALYLATION;

EID: 84861883015     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300319q     Document Type: Article
Times cited : (106)

References (39)
  • 1
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • DOI 10.1146/annurev.immunol.25.022106.141702
    • Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., and Dwek, R. A. (2007) The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 25, 21-50. (Pubitemid 46697901)
    • (2007) Annual Review of Immunology , 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
  • 3
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • DOI 10.1126/science.1129594
    • Kaneko, Y., Nimmerjahn, F., and Ravetch, E. V. (2006) Antiinflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 313, 670-673. (Pubitemid 44201145)
    • (2006) Science , vol.313 , Issue.5787 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 6
    • 0027204803 scopus 로고
    • Human IgG Fc receptor heterogeneity: Molecular aspects and clinical implications
    • van de Winkel, J. G., and Capel, P. J. (1993) Human IgG Fc receptor heterogeneity: molecular aspects and clinical implications. Immunol. Today 14, 215-221.
    • (1993) Immunol. Today , vol.14 , pp. 215-221
    • Van De Winkel, J.G.1    Capel, P.J.2
  • 8
    • 0018652008 scopus 로고
    • Comparison of the binding of radiolabeled human IgG and Fc fragments to murine spleen cells
    • DOI 10.1111/j.1365-3083.1979.tb01368.x
    • Morgan, E. L., Spiegelberg, H. L., and Weigle, W. O. (1979) Comparison of the binding of radiolabelled human IgG and Fc fragments to murine spleen cells. Scand. J. Immunol. 10, 395-402. (Pubitemid 10192805)
    • (1979) Scandinavian Journal of Immunology , vol.10 , Issue.5 , pp. 395-402
    • Morgan, E.L.1    Spiegelberg, H.L.2    Weigle, W.O.3
  • 9
    • 0022414766 scopus 로고
    • Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
    • DOI 10.1038/316452a0
    • Parekh, R. B., Dwek, R. A., Sutton, B. J., Fernandes, D. L., Leung, A., Stanworth, D., Rademacher, T. W., Mizuochi, T., Taniguchi, T., Matsuta, K., et al. (1985) Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 316, 452-457. (Pubitemid 16238456)
    • (1985) Nature , vol.316 , Issue.6027 , pp. 452-457
    • Parekh, R.B.1    Dwek, R.A.2    Sutton, B.J.3
  • 10
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-FcgammaRIII complex
    • DOI 10.1038/35018508
    • Sondermann, P., Huber, R., Oosthuizen, V., and Jacob, U. (2000) The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature 406, 267-273. (Pubitemid 30604397)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthulzen, V.3    Jacob, U.4
  • 11
    • 0035844212 scopus 로고    scopus 로고
    • The structure of a human type III Fcgamma receptor in complex with Fc
    • Radaev, S., Motyka, S., Fridman, W. H., Sautes-Fridman, C., and Sun, P. D. (2001) The structure of a human type III Fcgamma receptor in complex with Fc. J. Biol. Chem. 276, 16469-16477.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16469-16477
    • Radaev, S.1    Motyka, S.2    Fridman, W.H.3    Sautes-Fridman, C.4    Sun, P.D.5
  • 12
    • 77951294515 scopus 로고    scopus 로고
    • Divergent impact of the polysialyltransferases ST8SiaII and ST8SiaIV on polysialic acid expression in immature neurons and interneurons of the adult cerebral cortex
    • Nacher, J., Guirado, R., Varea, E., Alonso-Llosa, G., Rockle, I., and Hildebrandt, H. (2010) Divergent impact of the polysialyltransferases ST8SiaII and ST8SiaIV on polysialic acid expression in immature neurons and interneurons of the adult cerebral cortex. Neuroscience 167, 825-837.
    • (2010) Neuroscience , vol.167 , pp. 825-837
    • Nacher, J.1    Guirado, R.2    Varea, E.3    Alonso-Llosa, G.4    Rockle, I.5    Hildebrandt, H.6
  • 13
    • 33751181881 scopus 로고    scopus 로고
    • Altered granulopoietic profile and exaggerated acute neutrophilic inflammation in mice with targeted deficiency in the sialyltransferase ST6Gal I
    • Nasirikenari, M., Segal, B. H., Ostberg, J. R., Urbasic, A., and Lau, J. T. (2006) Altered granulopoietic profile and exaggerated acute neutrophilic inflammation in mice with targeted deficiency in the sialyltransferase ST6Gal I. Blood 108, 3397-3405.
    • (2006) Blood , vol.108 , pp. 3397-3405
    • Nasirikenari, M.1    Segal, B.H.2    Ostberg, J.R.3    Urbasic, A.4    Lau, J.T.5
  • 15
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway
    • Anthony, R. M., Kobayashi, T., Wermeling, F., and Ravetch, J. V. (2011) Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway. Nature 475, 110-U133.
    • (2011) Nature , vol.475
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 16
    • 70350055478 scopus 로고    scopus 로고
    • Branchspecific sialylation of IgG-Fc glycans by ST6Gal-I
    • Barb, A. W., Brady, E. K., and Prestegard, J. H. (2009) Branchspecific sialylation of IgG-Fc glycans by ST6Gal-I. Biochemistry 48, 9705-9707.
    • (2009) Biochemistry , vol.48 , pp. 9705-9707
    • Barb, A.W.1    Brady, E.K.2    Prestegard, J.H.3
  • 17
    • 0019522383 scopus 로고
    • 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-A resolution
    • Deisenhofer, J. (1981) 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-A resolution. Biochemistry 20, 2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 18
    • 0023654072 scopus 로고
    • Branch specificity of bovine colostrum CMP-sialic acid: Gal beta 1-4GlcNAc-R alpha 2-6-sialyltransferase. Sialylation of bi-, tri-, and tetraantennary oligosaccharides and glycopeptides of the N-acetyllactosamine type
    • Joziasse, D. H., Schiphorst, W. E., Van den Eijnden, D. H., Van Kuik, J. A., Van Halbeek, H., and Vliegenthart, J. F. (1987) Branch specificity of bovine colostrum CMP-sialic acid: Gal beta 1-4GlcNAc-R alpha 2-6-sialyltransferase. Sialylation of bi-, tri-, and tetraantennary oligosaccharides and glycopeptides of the N-acetyllactosamine type. J. Biol. Chem. 262, 2025-2033.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2025-2033
    • Joziasse, D.H.1    Schiphorst, W.E.2    Van Den Eijnden, D.H.3    Van Kuik, J.A.4    Van Halbeek, H.5    Vliegenthart, J.F.6
  • 19
    • 79951838374 scopus 로고    scopus 로고
    • NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic
    • Barb, A. W., and Prestegard, J. H. (2011) NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic. Nat. Chem. Biol. 7, 147-153.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 147-153
    • Barb, A.W.1    Prestegard, J.H.2
  • 20
    • 0032440743 scopus 로고    scopus 로고
    • Cloning, expression, purification, and characterization of the acid α-mannosidase from Trypanosoma cruzi
    • DOI 10.1093/glycob/8.12.1183
    • Vandersall-Nairn, A. S., Merkle, R. K., O'Brien, K., Oeltmann, T. N., and Moremen, K. W. (1998) Cloning, expression, purification, and characterization of the acid α-mannosidase from Trypanosoma cruzi. Glycobiology 8, 1183-1194. (Pubitemid 29008359)
    • (1998) Glycobiology , vol.8 , Issue.12 , pp. 1183-1194
    • Vandersall-Nairn, A.S.1    Merkle, R.K.2    O'Brien, K.3    Oeltmann, T.N.4    Moremen, K.W.5
  • 21
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett, D., Kovaleva, E., and Schatz, P. J. (1999) A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8, 921-929. (Pubitemid 29165423)
    • (1999) Protein Science , vol.8 , Issue.4 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 22
    • 30544433196 scopus 로고    scopus 로고
    • Engineering and characterization of a superfolder green fluorescent protein
    • DOI 10.1038/nbt1172, PII NBT1172
    • Pedelacq, J. D., Cabantous, S., Tran, T., Terwilliger, T. C., and Waldo, G. S. (2006) Engineering and characterization of a superfolder green fluorescent protein. Nat. Biotechnol. 24, 79-88. (Pubitemid 43083170)
    • (2006) Nature Biotechnology , vol.24 , Issue.1 , pp. 79-88
    • Pedelacq, J.-D.1    Cabantous, S.2    Tran, T.3    Terwilliger, T.C.4    Waldo, G.S.5
  • 23
    • 38449121649 scopus 로고    scopus 로고
    • High-density transfection with HEK-293 cells allows doubling of transient titers and removes need for a priori DNA complex formation with PEI
    • DOI 10.1002/bit.21596
    • Backliwal, G., Hildinger, M., Hasija, V., and Wurm, F. M. (2008) High-density transfection with HEK-293 cells allows doubling of transient titers and removes need for a priori DNA complex formation with PEI. Biotechnol. Bioeng. 99, 721-727. (Pubitemid 351158270)
    • (2008) Biotechnology and Bioengineering , vol.99 , Issue.3 , pp. 721-727
    • Backliwal, G.1    Hildinger, M.2    Hasija, V.3    Wurm, F.M.4
  • 24
    • 79956153138 scopus 로고    scopus 로고
    • Universal phosphatase-coupled glycosyltransferase assay
    • Wu, Z. L., Ethen, C. M., Prather, B., Machacek, M., and Jiang, W. (2011) Universal phosphatase-coupled glycosyltransferase assay. Glycobiology 21, 727-733.
    • (2011) Glycobiology , vol.21 , pp. 727-733
    • Wu, Z.L.1    Ethen, C.M.2    Prather, B.3    Machacek, M.4    Jiang, W.5
  • 26
    • 0019433474 scopus 로고
    • Glycosyltransferases of the human cervical epithelium. I. Characterization of a Beta-galactoside Alpha-2-L-fucosyltransferase and the identification of a Beta-N-acetylglucosaminide Alpha-3-L-fucosyltransferase
    • Scudder, P. R., and Chantler, E. N. (1981) Glycosyltransferases of the Human Cervical Epithelium 0.1. Characterization of a Beta- Galactoside Alpha-2-6-Fucosyltransferase and the Identification of a Beta-N- Acetylglucosaminide Alpha-3-L-Fucosyltransferase. Biochim. Biophys. Acta 660, 128-135. (Pubitemid 11045617)
    • (1981) Biochimica et Biophysica Acta , vol.660 , Issue.1 , pp. 128-135
    • Scudder, P.R.1    Chantler, E.N.2
  • 27
    • 33947472850 scopus 로고
    • A Schematic Method of Deriving the Rate Laws for Enzyme-Catalyzed Reactions
    • King, E. L., and Altman, C. (1956) A Schematic Method of Deriving the Rate Laws for Enzyme-Catalyzed Reactions. J. Phys. Chem. 60, 1375-1378.
    • (1956) J. Phys. Chem. , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 29
    • 33847534249 scopus 로고
    • Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance Experiments
    • Carr, H. Y., and Purcell, E. M. (1954) Effects of Diffusion on Free Precession in Nuclear Magnetic Resonance Experiments. Phys. Rev. 94, 630-638.
    • (1954) Phys. Rev. , vol.94 , pp. 630-638
    • Carr, H.Y.1    Purcell, E.M.2
  • 30
    • 72749106549 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structural characterization of substrates bound to the alpha-2,6-sialyltransferase, ST6Gal-I
    • Liu, S., Meng, L., Moremen, K. W., and Prestegard, J. H. (2009) Nuclear magnetic resonance structural characterization of substrates bound to the alpha-2,6-sialyltransferase, ST6Gal-I. Biochemistry 48, 11211-11219.
    • (2009) Biochemistry , vol.48 , pp. 11211-11219
    • Liu, S.1    Meng, L.2    Moremen, K.W.3    Prestegard, J.H.4
  • 31
    • 0017902906 scopus 로고
    • Sialyl- and fucosyltransferase in the biosynthesis of asparaginyl-linked oligosaccharides in glycoproteins. Mutually exclusive glylcosylation by beta-galactoside alpha2 goes to 6 sialyltransferase and N-acetylglucosaminide alpha1 goes to 3 fucosyltransferase
    • Paulson, J. C., Prieels, J. P., Glasgow, L. R., and Hill, R. L. (1978) Sialyl- and fucosyltransferases in the biosynthesis of asparaginyl-linked oligosaccharides in glycoproteins. Mutually exclusive glycosylation by beta-galactoside alpha2 goes to 6 sialyltransferase and N-acetylglucosaminide alpha1 goes to 3 fucosyltransferase. J. Biol. Chem. 253, 5617-5624. (Pubitemid 8403690)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.16 , pp. 5617-5624
    • Paulson, J.C.1    Prieels, J.P.2    Glasgow, L.R.3    Hill, R.L.4
  • 32
    • 33645080442 scopus 로고    scopus 로고
    • Pathology and protection in nephrotoxic nephritis is determined by selective engagement of specific Fc receptors
    • Kaneko, Y., Nimmerjahn, F., Madaio, M. P., and Ravetch, J. V. (2006) Pathology and protection in nephrotoxic nephritis is determined by selective engagement of specific Fc receptors. J. Exp. Med. 203, 789-797.
    • (2006) J. Exp. Med. , vol.203 , pp. 789-797
    • Kaneko, Y.1    Nimmerjahn, F.2    Madaio, M.P.3    Ravetch, J.V.4
  • 33
    • 37549036732 scopus 로고    scopus 로고
    • Fcgamma receptors as regulators of immune responses
    • Nimmerjahn, F., and Ravetch, J. V. (2008) Fcgamma receptors as regulators of immune responses. Nat. Rev. Immunol. 8, 34-47.
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 35
    • 40749147518 scopus 로고    scopus 로고
    • The N-linked sugar chains of human immunoglobulin G: Their unique pattern, and their functional roles
    • Kobata, A. (2008) The N-linked sugar chains of human immunoglobulin G: their unique pattern, and their functional roles. Biochim. Biophys. Acta 1780, 472-478.
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 472-478
    • Kobata, A.1
  • 36
    • 48549090941 scopus 로고    scopus 로고
    • Terminal sugars of Fc glycans influence antibody effector functions of IgGs
    • Raju, T. S. (2008) Terminal sugars of Fc glycans influence antibody effector functions of IgGs. Curr. Opin. Immunol. 20, 471-478.
    • (2008) Curr. Opin. Immunol. , vol.20 , pp. 471-478
    • Raju, T.S.1
  • 38
    • 80052310703 scopus 로고    scopus 로고
    • Comparative analysis reveals selective recognition of glycans by the dendritic cell receptors DCSIGN and Langerin
    • Holla, A., and Skerra, A. (2011) Comparative analysis reveals selective recognition of glycans by the dendritic cell receptors DCSIGN and Langerin. Protein Eng., Des. Sel. 24, 659-669.
    • (2011) Protein Eng., Des. Sel. , vol.24 , pp. 659-669
    • Holla, A.1    Skerra, A.2
  • 39
    • 0004106191 scopus 로고    scopus 로고
    • 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Varki, A. (2009) Essentials of Glycobiology, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
    • (2009) Essentials of Glycobiology
    • Varki, A.1


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