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Volumn 194, Issue 1, 2016, Pages 78-89

Structural characterization of GASDALIE Fc bound to the activating Fc receptor FcγRIIIa

Author keywords

Affinity; Fc receptors; Fc FcR structure; GASDALIE Fc; IgG Fc; SDALIE Fc

Indexed keywords

FC RECEPTOR; FC RECEPTOR IIIA; GASDALIE FC; IMMUNOGLOBULIN FC FRAGMENT; SDALIIE FC; UNCLASSIFIED DRUG; FCGR3A PROTEIN, HUMAN; FUCOSE; PROTEIN BINDING;

EID: 84958148759     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2016.02.001     Document Type: Article
Times cited : (46)

References (59)
  • 4
    • 77956185954 scopus 로고    scopus 로고
    • A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs
    • Anthony R.M., Ravetch J.V. A novel role for the IgG Fc glycan: the anti-inflammatory activity of sialylated IgG Fcs. J. Clin. Immunol. 2010, 30(Suppl 1). S9-14.
    • (2010) J. Clin. Immunol. , vol.30 , pp. S9-S14
    • Anthony, R.M.1    Ravetch, J.V.2
  • 7
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway
    • Anthony R.M., Kobayashi T., Wermeling F., Ravetch J.V. Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway. Nature 2011, 475:110-113.
    • (2011) Nature , vol.475 , pp. 110-113
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 8
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • Arnold J.N., Wormald M.R., Sim R.B., Rudd P.M., Dwek R.A. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 2007, 25:21-50.
    • (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
    • 84893841403 scopus 로고    scopus 로고
    • Human IgG Fc domain engineering enhances antitoxin neutralizing antibody activity
    • Bournazos S., Chow S.K., Abboud N., Casadevall A., Ravetch J.V. Human IgG Fc domain engineering enhances antitoxin neutralizing antibody activity. J. Clin. Investig. 2014, 124:725-729.
    • (2014) J. Clin. Investig. , vol.124 , pp. 725-729
    • Bournazos, S.1    Chow, S.K.2    Abboud, N.3    Casadevall, A.4    Ravetch, J.V.5
  • 10
    • 84908077691 scopus 로고    scopus 로고
    • Broadly neutralizing anti-HIV-antibodies require Fc effector functions for in vivo activity
    • Bournazos S., Klein F., Pietzsch J., Seaman M.S., Nussenzweig M.C., Ravetch J.V. Broadly neutralizing anti-HIV-antibodies require Fc effector functions for in vivo activity. Cell 2014, 158:1243-1253.
    • (2014) Cell , vol.158 , pp. 1243-1253
    • Bournazos, S.1    Klein, F.2    Pietzsch, J.3    Seaman, M.S.4    Nussenzweig, M.C.5    Ravetch, J.V.6
  • 11
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses
    • Bruhns P., Iannascoli B., England P., Mancardi D.A., Fernandez N., Jorieux S., Daeron M. Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses. Blood 2009, 113:3716-3725.
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1    Iannascoli, B.2    England, P.3    Mancardi, D.A.4    Fernandez, N.5    Jorieux, S.6    Daeron, M.7
  • 12
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister W.P., Huber A.H., Bjorkman P.J. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature 1994, 372:379-383.
    • (1994) Nature , vol.372 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 13
    • 10744225031 scopus 로고    scopus 로고
    • Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis
    • Butler M., Quelhas D., Critchley A.J., Carchon H., Hebestreit H.F., Hibbert R.G., Vilarinho L., Teles E., Matthijs G., Schollen E., et al. Detailed glycan analysis of serum glycoproteins of patients with congenital disorders of glycosylation indicates the specific defective glycan processing step and provides an insight into pathogenesis. Glycobiology 2003, 13:601-622.
    • (2003) Glycobiology , vol.13 , pp. 601-622
    • Butler, M.1    Quelhas, D.2    Critchley, A.J.3    Carchon, H.4    Hebestreit, H.F.5    Hibbert, R.G.6    Vilarinho, L.7    Teles, E.8    Matthijs, G.9    Schollen, E.10
  • 14
    • 84930081913 scopus 로고    scopus 로고
    • Differential Fc-receptor engagement drives an anti-tumor vaccinal effect
    • DiLillo D.J., Ravetch J.V. Differential Fc-receptor engagement drives an anti-tumor vaccinal effect. Cell 2015, 161:1035-1045.
    • (2015) Cell , vol.161 , pp. 1035-1045
    • DiLillo, D.J.1    Ravetch, J.V.2
  • 15
    • 84961938333 scopus 로고    scopus 로고
    • Fc-Receptor interactions regulate both cytotoxic and immunomodulatory therapeutic antibody effector functions
    • DiLillo D.J., Ravetch J.V. Fc-Receptor interactions regulate both cytotoxic and immunomodulatory therapeutic antibody effector functions. Cancer Immunol. Res. 2015, 3:704-713.
    • (2015) Cancer Immunol. Res. , vol.3 , pp. 704-713
    • DiLillo, D.J.1    Ravetch, J.V.2
  • 16
    • 84893797938 scopus 로고    scopus 로고
    • Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR interactions for protection against influenza virus in vivo
    • DiLillo D.J., Tan G.S., Palese P., Ravetch J.V. Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR interactions for protection against influenza virus in vivo. Nat. Med. 2014, 20:143-151.
    • (2014) Nat. Med. , vol.20 , pp. 143-151
    • DiLillo, D.J.1    Tan, G.S.2    Palese, P.3    Ravetch, J.V.4
  • 17
    • 77951939875 scopus 로고    scopus 로고
    • Structure of a clade C HIV-gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity
    • Diskin R., Marcovecchio P.M., Bjorkman P.J. Structure of a clade C HIV-gp120 bound to CD4 and CD4-induced antibody reveals anti-CD4 polyreactivity. Nat. Struct. Mol. Biol. 2010, 17:608-613.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 608-613
    • Diskin, R.1    Marcovecchio, P.M.2    Bjorkman, P.J.3
  • 18
    • 0023933120 scopus 로고
    • Localization of the binding site for the human high-affinity Fc receptor on IgG
    • Duncan A.R., Woof J.M., Partridge L.J., Burton D.R., Winter G. Localization of the binding site for the human high-affinity Fc receptor on IgG. Nature 1988, 332:563-564.
    • (1988) Nature , vol.332 , pp. 563-564
    • Duncan, A.R.1    Woof, J.M.2    Partridge, L.J.3    Burton, D.R.4    Winter, G.5
  • 19
    • 0031572518 scopus 로고    scopus 로고
    • Cell type-specific glycoforms of Fc gamma RIIIa (CD16): differential ligand binding
    • Edberg J.C., Kimberly R.P. Cell type-specific glycoforms of Fc gamma RIIIa (CD16): differential ligand binding. J. Immunol. 1997, 159:3849-3857.
    • (1997) J. Immunol. , vol.159 , pp. 3849-3857
    • Edberg, J.C.1    Kimberly, R.P.2
  • 22
    • 79953747244 scopus 로고    scopus 로고
    • An introduction to data reduction: space-group determination, scaling and intensity statistics
    • Evans P.R. An introduction to data reduction: space-group determination, scaling and intensity statistics. Acta Crystallogr. D Biol. Crystallogr. 2011, 67:282-292.
    • (2011) Acta Crystallogr. D Biol. Crystallogr. , vol.67 , pp. 282-292
    • Evans, P.R.1
  • 23
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms
    • Ferrara C., Stuart F., Sondermann P., Brunker P., Umana P. The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms. J. Biol. Chem. 2006, 281:5032-5036.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5032-5036
    • Ferrara, C.1    Stuart, F.2    Sondermann, P.3    Brunker, P.4    Umana, P.5
  • 25
    • 0028672732 scopus 로고
    • Molecular basis of Fc receptor function
    • Hulett M.D., Hogarth P.M. Molecular basis of Fc receptor function. Adv. Immunol. 1994, 57:1-127.
    • (1994) Adv. Immunol. , vol.57 , pp. 1-127
    • Hulett, M.D.1    Hogarth, P.M.2
  • 27
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • Kaneko Y., Nimmerjahn F., Ravetch J.V. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 2006, 313:670-673.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1    Nimmerjahn, F.2    Ravetch, J.V.3
  • 28
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus P.A., Diederichs K. Linking crystallographic model and data quality. Science 2012, 336:1030-1033.
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 29
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E., Henrick K. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 2007, 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 38
    • 0030039913 scopus 로고    scopus 로고
    • Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics
    • Nieba L., Krebber A., Pluckthun A. Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. Anal. Biochem. 1996, 234:155-165.
    • (1996) Anal. Biochem. , vol.234 , pp. 155-165
    • Nieba, L.1    Krebber, A.2    Pluckthun, A.3
  • 39
    • 42649089750 scopus 로고    scopus 로고
    • Anti-inflammatory actions of intravenous immunoglobulin
    • Nimmerjahn F., Ravetch J.V. Anti-inflammatory actions of intravenous immunoglobulin. Annu. Rev. Immunol. 2008, 26:513-533.
    • (2008) Annu. Rev. Immunol. , vol.26 , pp. 513-533
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 40
  • 47
    • 53349120501 scopus 로고    scopus 로고
    • Optimization of antibody binding to FcgammaRIIa enhances macrophage phagocytosis of tumor cells
    • Richards J.O., Karki S., Lazar G.A., Chen H., Dang W., Desjarlais J.R. Optimization of antibody binding to FcgammaRIIa enhances macrophage phagocytosis of tumor cells. Mol. Cancer Ther. 2008, 7:2517-2527.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 2517-2527
    • Richards, J.O.1    Karki, S.2    Lazar, G.A.3    Chen, H.4    Dang, W.5    Desjarlais, J.R.6
  • 48
    • 0035910392 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor
    • Samuelsson A., Towers T.L., Ravetch J.V. Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor. Science 2001, 291:484-486.
    • (2001) Science , vol.291 , pp. 484-486
    • Samuelsson, A.1    Towers, T.L.2    Ravetch, J.V.3
  • 52
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R
    • Shields R.L., Namenuk A.K., Hong K., Meng Y.G., Rae J., Briggs J., Xie D., Lai J., Stadlen A., Li B., et al. High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R. J. Biol. Chem. 2001, 276:6591-6604.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6    Xie, D.7    Lai, J.8    Stadlen, A.9    Li, B.10
  • 53
  • 54
    • 0033106166 scopus 로고    scopus 로고
    • Crystal structure of the soluble form of the human fcgamma-receptor IIb: a new member of the immunoglobulin superfamily at 1.7 A resolution
    • Sondermann P., Huber R., Jacob U. Crystal structure of the soluble form of the human fcgamma-receptor IIb: a new member of the immunoglobulin superfamily at 1.7 A resolution. EMBO J. 1999, 18:1095-1103.
    • (1999) EMBO J. , vol.18 , pp. 1095-1103
    • Sondermann, P.1    Huber, R.2    Jacob, U.3
  • 55
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex
    • Sondermann P., Huber R., Oosthuizen V., Jacob U. The 3.2-crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature 2000, 406:267-273.
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 56
    • 0035827222 scopus 로고    scopus 로고
    • Molecular basis for immune complex recognition: a comparison of Fc-receptor structures
    • Sondermann P., Kaiser J., Jacob U. Molecular basis for immune complex recognition: a comparison of Fc-receptor structures. J. Mol. Biol. 2001, 309:737-749.
    • (2001) J. Mol. Biol. , vol.309 , pp. 737-749
    • Sondermann, P.1    Kaiser, J.2    Jacob, U.3
  • 58
    • 1842639396 scopus 로고    scopus 로고
    • PH dependence and stoichiometry of binding to the Fc region of IgG by the herpes simplex virus Fc receptor gE-gI
    • Sprague E.R., Martin W.L., Bjorkman P.J. PH dependence and stoichiometry of binding to the Fc region of IgG by the herpes simplex virus Fc receptor gE-gI. J. Biol. Chem. 2004, 279:14184-14193.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14184-14193
    • Sprague, E.R.1    Martin, W.L.2    Bjorkman, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.