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Volumn 25, Issue 3, 2012, Pages 147-154

Avidity confers FcγR binding and immune effector function to aglycosylated immunoglobulin G1

Author keywords

avidity; Fc gamma receptor; glycosylation; imune effector function; monoclonal antibodies

Indexed keywords

FC RECEPTOR; GLYCOPEPTIDASE; IMMUNOGLOBULIN G; LEUKOCYTE ANTIGEN;

EID: 84858176295     PISSN: 09523499     EISSN: 10991352     Source Type: Journal    
DOI: 10.1002/jmr.2155     Document Type: Article
Times cited : (45)

References (36)
  • 4
    • 77953677176 scopus 로고    scopus 로고
    • Cleavage of IgGs by proteases associated with invasive diseases: An evasion tactic against host immunity?
    • Brezski RJ, Jordan RE,. 2010. Cleavage of IgGs by proteases associated with invasive diseases: An evasion tactic against host immunity? MAbs 2 (3): 212-220.
    • (2010) MAbs , vol.2 , Issue.3 , pp. 212-220
    • Brezski, R.J.1    Jordan, R.E.2
  • 5
    • 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 DA, Fernandez N, Jorieux S, Daeron M,. 2009. Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses. Blood 113 (16): 3716-25.
    • (2009) Blood , vol.113 , Issue.16 , 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
  • 6
    • 0141756175 scopus 로고    scopus 로고
    • Integrin avidity regulation: Are changes in affinity and conformation underemphasized?
    • DOI 10.1016/j.ceb.2003.08.003
    • Carman CV, Springer TA,. 2003. Integrin avidity regulation: are changes in affinity and conformation underemphasized? Curr. Opin. Cell Biol. 15 (5): 547-56. (Pubitemid 37176963)
    • (2003) Current Opinion in Cell Biology , vol.15 , Issue.5 , pp. 547-556
    • Carman, C.V.1    Springer, T.A.2
  • 7
    • 34547230077 scopus 로고    scopus 로고
    • CD3-specific antibodies: A portal to the treatment of autoimmunity
    • DOI 10.1038/nri2134, PII NRI2134
    • Chatenoud L, Bluestone JA,. 2007. CD3-specific antibodies: a portal to the treatment of autoimmunity. Nat. Rev. Immunol. 7 (8): 622-32. (Pubitemid 47123550)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.8 , pp. 622-632
    • Chatenoud, L.1    Bluestone, J.A.2
  • 8
    • 53749095475 scopus 로고    scopus 로고
    • Fc-disabled anti-mouse CD40L antibodies retain efficacy in promoting transplantation tolerance
    • Daley SR, Cobbold SP, Waldmann H,. 2008. Fc-disabled anti-mouse CD40L antibodies retain efficacy in promoting transplantation tolerance. Am. J. Transplant. 8 (11): 2265-71.
    • (2008) Am. J. Transplant. , vol.8 , Issue.11 , pp. 2265-2271
    • Daley, S.R.1    Cobbold, S.P.2    Waldmann, H.3
  • 11
    • 0034691520 scopus 로고    scopus 로고
    • Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα
    • DOI 10.1038/35018500
    • Garman SC, Wurzburg BA, Tarchevskaya SS, Kinet JP, Jardetzky TS,. 2000. Structure of the Fc fragment of human IgE bound to its high-affinity receptor Fc epsilonRI alpha. Nature 406 (6793): 259-66. (Pubitemid 30604396)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 259-266
    • Garman, S.C.1    Wurzburg, B.A.2    Tarchevskaya, S.S.3    Klnet, J.-P.4    Jardetzky, T.S.5
  • 12
    • 34748865088 scopus 로고    scopus 로고
    • Antibody therapeutics: Isotype and glycoform selection
    • DOI 10.1517/14712598.7.9.1401
    • Jefferis R, 2007. Antibody therapeutics: isotype and glycoform selection. Expert Opin. Biol. Ther. 7 (9): 1401-13. (Pubitemid 47475656)
    • (2007) Expert Opinion on Biological Therapy , vol.7 , Issue.9 , pp. 1401-1413
    • Jefferis, R.1
  • 13
    • 76249100176 scopus 로고    scopus 로고
    • Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells
    • Jung ST, Reddy ST, Kang TH, Borrok MJ, Sandlie I, Tucker PW, Georgiou G,. 2010. Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells. Proc. Natl. Acad. Sci. U.S.A. 107 (2): 604-9.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , Issue.2 , pp. 604-609
    • Jung, S.T.1    Reddy, S.T.2    Kang, T.H.3    Borrok, M.J.4    Sandlie, I.5    Tucker, P.W.6    Georgiou, G.7
  • 14
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • DOI 10.1016/S0022-2836(02)01250-0
    • Krapp S, Mimura Y, Jefferis R, Huber R, Sondermann P,. 2003. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 325 (5): 979-89. (Pubitemid 36263407)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 979-989
    • Krapp, S.1    Mimura, Y.2    Jefferis, R.3    Huber, R.4    Sondermann, P.5
  • 15
    • 48549107351 scopus 로고    scopus 로고
    • When binding is enough: Nonactivating antibody formats
    • Labrijn AF, Aalberse RC, Schuurman J,. 2008. When binding is enough: nonactivating antibody formats. Curr. Opin. Immunol. 20 (4): 479-85.
    • (2008) Curr. Opin. Immunol. , vol.20 , Issue.4 , pp. 479-485
    • Labrijn, A.F.1    Aalberse, R.C.2    Schuurman, J.3
  • 16
    • 0030470557 scopus 로고    scopus 로고
    • Multiple Interactions of IgG with Its Core Oligosaccharide Can Modulate Recognition by Complement and Human Fcγ Receptor I and Influence the Synthesis of Its Oligosaccharide Chains
    • Lund J, Takahashi N, Pound JD, Goodall M, Jefferis R,. 1996. Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human Fc gamma receptor I and influence the synthesis of its oligosaccharide chains. J. Immunol. 157 (11): 4963-9. (Pubitemid 126449574)
    • (1996) Journal of Immunology , vol.157 , Issue.11 , pp. 4963-4969
    • Lund, J.1    Takahashi, N.2    Pound, J.D.3    Goodall, M.4    Jefferis, R.5
  • 17
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: Properties of a series of truncated glycoforms
    • DOI 10.1016/S0161-5890(00)00105-X, PII S016158900000105X
    • Mimura Y, Church S, Ghirlando R, Ashton PR, Dong S, Goodall M, Lund J, Jefferis R,. 2000. 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. 37 (12-13): 697-706. (Pubitemid 32244118)
    • (2001) Molecular Immunology , vol.37 , Issue.12-13 , pp. 697-706
    • Mimura, Y.1    Church, S.2    Ghirlando, R.3    Ashton, P.R.4    Dong, S.5    Goodall, M.6    Lund, J.7    Jefferis, R.8
  • 18
    • 0020512683 scopus 로고
    • Modulation of surface antigens of a human monocyte cell line, U937, during incubation with T lymphocyte-conditioned medium: Detection of T4 antigen and its presence on normal blood monocytes
    • Moscicki RA, Amento EP, Krane SM, Kurnick JT, Colvin RB,. 1983. Modulation of surface antigens of a human monocyte cell line, U937, during incubation with T lymphocyte-conditioned medium: detection of T4 antigen and its presence on normal blood monocytes. J. Immunol. 131 (2): 743-8. (Pubitemid 13077782)
    • (1983) Journal of Immunology , vol.131 , Issue.2 , pp. 743-748
    • Moscicki, R.A.1    Amento, E.P.2    Krane, S.M.3
  • 20
    • 37549036732 scopus 로고    scopus 로고
    • Fcgamma receptors as regulators of immune responses
    • Nimmerjahn F, Ravetch JV,. 2008. Fcgamma receptors as regulators of immune responses. Nat. Rev. Immunol. 8 (1): 34-47.
    • (2008) Nat. Rev. Immunol. , vol.8 , Issue.1 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 21
    • 0027450137 scopus 로고
    • Aglycosylated chimaeric human IgG3 can trigger the human phagocyte respiratory burst
    • Pound JD, Lund J, Jefferis R,. 1993. Aglycosylated chimaeric human IgG3 can trigger the human phagocyte respiratory burst. Mol. Immunol. 30 (3): 233-41.
    • (1993) Mol. Immunol. , vol.30 , Issue.3 , pp. 233-241
    • Pound, J.D.1    Lund, J.2    Jefferis, R.3
  • 22
    • 48549105161 scopus 로고    scopus 로고
    • Molecular engineering and design of therapeutic antibodies
    • Presta LG,. 2008. Molecular engineering and design of therapeutic antibodies. Curr. Opin. Immunol. 20 (4): 460-70.
    • (2008) Curr. Opin. Immunol. , vol.20 , Issue.4 , pp. 460-470
    • Presta, L.G.1
  • 23
    • 0035844212 scopus 로고    scopus 로고
    • The structure of a human type III Fcgamma receptor in complex with Fc
    • Radaev S, Motyka S, Fridman WH, Sautes-Fridman C, Sun PD,. 2001. The structure of a human type III Fcgamma receptor in complex with Fc. J. Biol. Chem. 276 (19): 16469-77.
    • (2001) J. Biol. Chem. , vol.276 , Issue.19 , pp. 16469-16477
    • Radaev, S.1    Motyka, S.2    Fridman, W.H.3    Sautes-Fridman, C.4    Sun, P.D.5
  • 24
    • 77951573241 scopus 로고    scopus 로고
    • Antibodies to watch in 2010
    • Reichert JM,. 2010. Antibodies to watch in 2010. MAbs 2 (1).
    • (2010) MAbs , vol.2 , Issue.1
    • Reichert, J.M.1
  • 25
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • DOI 10.1038/nri2155, PII NRI2155
    • Roopenian DC, Akilesh S,. 2007. FcRn: the neonatal Fc receptor comes of age. Nat. Rev. Immunol. 7 (9): 715-25. (Pubitemid 47327396)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.9 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 26
    • 34247378189 scopus 로고    scopus 로고
    • Quantitative in vivo comparisons of the Fcγ receptor-dependent agonist activities of different fucosylation variants of an immunoglobulin G antibody
    • DOI 10.1016/j.intimp.2007.01.014, PII S1567576907000343
    • Scallon B, McCarthy S, Radewonuk J, Cai A, Naso M, Raju TS, Capocasale R,. 2007. Quantitative in vivo comparisons of the Fc gamma receptor-dependent agonist activities of different fucosylation variants of an immunoglobulin G antibody. Int. Immunopharmacol. 7 (6): 761-72. (Pubitemid 46635275)
    • (2007) International Immunopharmacology , vol.7 , Issue.6 , pp. 761-772
    • Scallon, B.1    McCarthy, S.2    Radewonuk, J.3    Cai, A.4    Naso, M.5    Raju, T.S.6    Capocasale, R.7
  • 27
    • 33645892299 scopus 로고    scopus 로고
    • A conformation- and avidity-based proofreading mechanism for the TCR-CD3 complex
    • Schamel WW, Risueno RM, Minguet S, Ortiz AR, Alarcon B,. 2006. A conformation- and avidity-based proofreading mechanism for the TCR-CD3 complex. Trends Immunol. 27 (4): 176-82.
    • (2006) Trends Immunol. , vol.27 , Issue.4 , pp. 176-182
    • Schamel, W.W.1    Risueno, R.M.2    Minguet, S.3    Ortiz, A.R.4    Alarcon, B.5
  • 28
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity
    • DOI 10.1074/jbc.M202069200
    • Shields RL, Lai J, Keck R, O'Connell LY, Hong K, Meng YG, Weikert SH, Presta LG,. 2002. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277 (30): 26733-40. (Pubitemid 34951677)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.30 , pp. 26733-26740
    • Shields, R.L.1    Lai, J.2    Keck, R.3    O'Connell, L.Y.4    Hong, K.5    Gloria Meng, Y.6    Weikert, S.H.A.7    Presta, L.G.8
  • 29
    • 70449727004 scopus 로고    scopus 로고
    • Optimization of Fc-mediated effector functions of monoclonal antibodies
    • Strohl WR,. 2009. Optimization of Fc-mediated effector functions of monoclonal antibodies. Curr. Opin. Biotechnol. 20 (6): 685-91.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , Issue.6 , pp. 685-691
    • Strohl, W.R.1
  • 30
    • 0024438061 scopus 로고
    • Studies of aglycosylated chimeric mouse-human IgG. Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region
    • Tao M-H, Morrison SL,. 1989. Studies of aglycosylated chimeric mouse-human IgG Role of carbohydrate in the structure and effector functions mediated by the human IgG constant region. J. Immunol. 143: 2595-2601. (Pubitemid 19260070)
    • (1989) Journal of Immunology , vol.143 , Issue.8 , pp. 2595-2601
    • Tao, M.-H.1    Morrison, S.L.2
  • 31
    • 0021152074 scopus 로고
    • Fc receptors for mouse IgG1 on human monocytes: Polymorphism and role in antibody-induced T cell proliferation
    • Tax WJ, Hermes FF, Willems RW, Capel PJ, Koene RA,. 1984. Fc receptors for mouse IgG1 on human monocytes: polymorphism and role in antibody-induced T cell proliferation. J. Immunol. 133 (3): 1185-9. (Pubitemid 14060063)
    • (1984) Journal of Immunology , vol.133 , Issue.3 , pp. 1185-1189
    • Tax, W.J.M.1    Hermes, F.F.M.2    Willems, R.W.3
  • 32
    • 0025877975 scopus 로고
    • Differences in the stimulating capacity of immobilized anti-CD3 monoclonal antibodies: Variable dependence on interleukin-1 as a helper signal for T-cell activation
    • Verwilghen J, Baroja ML, Van Vaeck F, Van Damme J, Ceuppens JL,. 1991. Differences in the stimulating capacity of immobilized anti-CD3 monoclonal antibodies: variable dependence on interleukin-1 as a helper signal for T-cell activation. Immunology 72 (2): 269-76.
    • (1991) Immunology , vol.72 , Issue.2 , pp. 269-276
    • Verwilghen, J.1    Baroja, M.L.2    Van Vaeck, F.3    Van Damme, J.4    Ceuppens, J.L.5
  • 33
    • 0024544730 scopus 로고
    • Aglycosylation of human IgG1 and IgG3 monoclonal antibodies can eliminate recognition by human cells expressing FcγRI and/or FcγRII receptors
    • Walker MR, Lund J, Thompson KM, Jefferis R,. 1989. Aglycosylation of human IgG1 and IgG3 monoclonal antibodies can eliminate recognition by human cells expressing Fc gamma RI and/or Fc gamma RII receptors. Biochem. J. 259 (2): 347-53. (Pubitemid 19111668)
    • (1989) Biochemical Journal , vol.259 , Issue.2 , pp. 347-353
    • Walker, M.R.1    Lund, J.2    Thompson, K.M.3    Jefferis, R.4
  • 34
    • 77951614830 scopus 로고    scopus 로고
    • Monoclonal antibodies: Versatile platforms for cancer immunotherapy
    • Weiner LM, Surana R, Wang S,. 2010. Monoclonal antibodies: versatile platforms for cancer immunotherapy. Nat. Rev. Immunol. 10 (5): 317-27.
    • (2010) Nat. Rev. Immunol. , vol.10 , Issue.5 , pp. 317-327
    • Weiner, L.M.1    Surana, R.2    Wang, S.3
  • 35
    • 0022611355 scopus 로고
    • Localisation of the monocyte-binding region on human immunoglobulin G
    • DOI 10.1016/0161-5890(86)90059-3
    • Woof JM, Partridge LJ, Jefferis R, Burton DR,. 1986. Localisation of the monocyte-binding region on human immunoglobulin G. Mol. Immunol. 23 (3): 319-30. (Pubitemid 16128895)
    • (1986) Molecular Immunology , vol.23 , Issue.3 , pp. 319-330
    • Woof, J.M.1    Partridge, L.J.2    Jefferis, R.3    Burton, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.