메뉴 건너뛰기




Volumn 38, Issue 5, 2017, Pages 358-372

The Immunoregulatory Roles of Antibody Glycosylation

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; FC RECEPTOR; IMMUNOGLOBULIN G; NEUTRALIZING ANTIBODY; VACCINE; POLYSACCHARIDE; PROTEIN BINDING;

EID: 85016568747     PISSN: 14714906     EISSN: 14714981     Source Type: Journal    
DOI: 10.1016/j.it.2017.02.004     Document Type: Review
Times cited : (246)

References (98)
  • 1
    • 77954357410 scopus 로고    scopus 로고
    • Correlates of protection induced by vaccination
    • 1 Plotkin, S.A., Correlates of protection induced by vaccination. Clin. Vaccine Immunol. 17 (2010), 1055–1065.
    • (2010) Clin. Vaccine Immunol. , vol.17 , pp. 1055-1065
    • Plotkin, S.A.1
  • 2
    • 84905663895 scopus 로고    scopus 로고
    • Nonneutralizing functional antibodies: a new “old” paradigm for HIV vaccines
    • 2 Excler, J.L., et al. Nonneutralizing functional antibodies: a new “old” paradigm for HIV vaccines. Clin. Vaccine Immunol. 21 (2014), 1023–1036.
    • (2014) Clin. Vaccine Immunol. , vol.21 , pp. 1023-1036
    • Excler, J.L.1
  • 3
    • 84994157121 scopus 로고    scopus 로고
    • Functional antibodies and protection against blood-stage Malaria
    • 3 Teo, A., et al. Functional antibodies and protection against blood-stage Malaria. Trends Parasitol. 32 (2016), 887–898.
    • (2016) Trends Parasitol. , vol.32 , pp. 887-898
    • Teo, A.1
  • 4
    • 84956802630 scopus 로고    scopus 로고
    • Polyfunctional HIV-specific antibody responses are associated with spontaneous HIV control
    • 4 Ackerman, M.E., et al. Polyfunctional HIV-specific antibody responses are associated with spontaneous HIV control. PLoS Pathog., 12, 2016, e1005315.
    • (2016) PLoS Pathog. , vol.12 , pp. e1005315
    • Ackerman, M.E.1
  • 5
    • 84870660384 scopus 로고    scopus 로고
    • Inhibition of Marburg virus budding by nonneutralizing antibodies to the envelope glycoprotein
    • 5 Kajihara, M., et al. Inhibition of Marburg virus budding by nonneutralizing antibodies to the envelope glycoprotein. J. Virol. 86 (2012), 13467–13474.
    • (2012) J. Virol. , vol.86 , pp. 13467-13474
    • Kajihara, M.1
  • 6
    • 84894552888 scopus 로고    scopus 로고
    • Obinutuzumab plus chlorambucil in patients with CLL and coexisting conditions
    • 6 Goede, V., et al. Obinutuzumab plus chlorambucil in patients with CLL and coexisting conditions. N. Engl. J. Med. 370 (2014), 1101–1110.
    • (2014) N. Engl. J. Med. , vol.370 , pp. 1101-1110
    • Goede, V.1
  • 7
    • 77953141926 scopus 로고    scopus 로고
    • Superior in vivo efficacy of afucosylated trastuzumab in the treatment of HER2-amplified breast cancer
    • 7 Junttila, T.T., et al. Superior in vivo efficacy of afucosylated trastuzumab in the treatment of HER2-amplified breast cancer. Cancer Res. 70 (2010), 4481–4489.
    • (2010) Cancer Res. , vol.70 , pp. 4481-4489
    • Junttila, T.T.1
  • 8
    • 84962208068 scopus 로고    scopus 로고
    • Harnessing Fc receptor biology in the design of therapeutic antibodies
    • 8 Sondermann, P., Szymkowski, D.E., Harnessing Fc receptor biology in the design of therapeutic antibodies. Curr. Opin. Immunol. 40 (2016), 78–87.
    • (2016) Curr. Opin. Immunol. , vol.40 , pp. 78-87
    • Sondermann, P.1    Szymkowski, D.E.2
  • 9
    • 84858785688 scopus 로고    scopus 로고
    • Antibody therapy of cancer
    • 9 Scott, A.M., et al. Antibody therapy of cancer. Nat. Rev. Cancer 12 (2012), 278–287.
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 278-287
    • Scott, A.M.1
  • 10
    • 84918825382 scopus 로고    scopus 로고
    • IgG subclasses and allotypes: from structure to effector functions
    • 10 Vidarsson, G., et al. IgG subclasses and allotypes: from structure to effector functions. Front Immunol., 5, 2014, 520.
    • (2014) Front Immunol. , vol.5 , pp. 520
    • Vidarsson, G.1
  • 11
    • 84904627207 scopus 로고    scopus 로고
    • Type I and type II Fc receptors regulate innate and adaptive immunity
    • 11 Pincetic, A., et al. Type I and type II Fc receptors regulate innate and adaptive immunity. Nat. Immunol. 15 (2014), 707–716.
    • (2014) Nat. Immunol. , vol.15 , pp. 707-716
    • Pincetic, A.1
  • 12
    • 0036676975 scopus 로고    scopus 로고
    • Roles of Fc receptors in autoimmunity
    • 12 Takai, T., Roles of Fc receptors in autoimmunity. Nat. Rev. Immunol. 2 (2002), 580–592.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 580-592
    • Takai, T.1
  • 13
    • 34548496893 scopus 로고    scopus 로고
    • Fc receptor but not complement binding is important in antibody protection against HIV
    • 13 Hessell, A.J., et al. Fc receptor but not complement binding is important in antibody protection against HIV. Nature 449 (2007), 101–104.
    • (2007) Nature , vol.449 , pp. 101-104
    • Hessell, A.J.1
  • 14
    • 0035037372 scopus 로고    scopus 로고
    • Evidence for a correlation between antibody-dependent cellular cytotoxicity-mediating anti-HIV-1 antibodies and prognostic predictors of HIV infection
    • 14 Ahmad, R., et al. Evidence for a correlation between antibody-dependent cellular cytotoxicity-mediating anti-HIV-1 antibodies and prognostic predictors of HIV infection. J. Clin. Immunol. 21 (2001), 227–233.
    • (2001) J. Clin. Immunol. , vol.21 , pp. 227-233
    • Ahmad, R.1
  • 15
    • 84907514857 scopus 로고    scopus 로고
    • Relationship of preexisting influenza hemagglutination inhibition, complement-dependent lytic, and antibody-dependent cellular cytotoxicity antibodies to the development of clinical illness in a prospective study of A(H1N1)pdm09 influenza in children
    • 15 Co, M.D., et al. Relationship of preexisting influenza hemagglutination inhibition, complement-dependent lytic, and antibody-dependent cellular cytotoxicity antibodies to the development of clinical illness in a prospective study of A(H1N1)pdm09 influenza in children. Viral Immunol. 27 (2014), 375–382.
    • (2014) Viral Immunol. , vol.27 , pp. 375-382
    • Co, M.D.1
  • 16
    • 76749113309 scopus 로고    scopus 로고
    • Structure and function of immunoglobulins
    • 16 Schroeder, H.W. Jr., Cavacini, L., Structure and function of immunoglobulins. J. Allergy Clin. Immunol. 125 (2010), S41–S52.
    • (2010) J. Allergy Clin. Immunol. , vol.125 , pp. S41-S52
    • Schroeder, H.W.1    Cavacini, L.2
  • 17
    • 80054016444 scopus 로고    scopus 로고
    • High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations
    • M111.010090
    • 17 Pucic, M., et al. High throughput isolation and glycosylation analysis of IgG-variability and heritability of the IgG glycome in three isolated human populations. Mol. Cell Proteomics, 10, 2011 M111.010090.
    • (2011) Mol. Cell Proteomics , vol.10
    • Pucic, M.1
  • 18
    • 84893411589 scopus 로고    scopus 로고
    • Regulation of immunoglobulin class-switch recombination: choreography of noncoding transcription, targeted DNA deamination, and long-range DNA repair
    • 18 Matthews, A.J., et al. Regulation of immunoglobulin class-switch recombination: choreography of noncoding transcription, targeted DNA deamination, and long-range DNA repair. Adv. Immunol. 122 (2014), 1–57.
    • (2014) Adv. Immunol. , vol.122 , pp. 1-57
    • Matthews, A.J.1
  • 19
    • 0027417869 scopus 로고
    • Shutdown of class switch recombination by deletion of a switch region control element
    • 19 Jung, S., et al. Shutdown of class switch recombination by deletion of a switch region control element. Science 259 (1993), 984–987.
    • (1993) Science , vol.259 , pp. 984-987
    • Jung, S.1
  • 20
    • 33646181086 scopus 로고    scopus 로고
    • Mechanism and control of V(D)J recombination at the immunoglobulin heavy chain locus
    • 20 Jung, D., et al. Mechanism and control of V(D)J recombination at the immunoglobulin heavy chain locus. Annu. Rev. Immunol. 24 (2006), 541–570.
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 541-570
    • Jung, D.1
  • 21
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses
    • 21 Bruhns, P., et al. Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses. Blood 113 (2009), 3716–3725.
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1
  • 22
    • 84896051838 scopus 로고    scopus 로고
    • H435-containing immunoglobulin G3 allotypes are transported efficiently across the human placenta: implications for alloantibody-mediated diseases of the newborn
    • 22 Einarsdottir, H., et al. H435-containing immunoglobulin G3 allotypes are transported efficiently across the human placenta: implications for alloantibody-mediated diseases of the newborn. Transfusion 54 (2014), 665–671.
    • (2014) Transfusion , vol.54 , pp. 665-671
    • Einarsdottir, H.1
  • 23
    • 84455208902 scopus 로고    scopus 로고
    • Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers therapeutic potential
    • 23 Stapleton, N.M., et al. Competition for FcRn-mediated transport gives rise to short half-life of human IgG3 and offers therapeutic potential. Nat. Commun., 2, 2011, 599.
    • (2011) Nat. Commun. , vol.2 , pp. 599
    • Stapleton, N.M.1
  • 24
    • 84875805834 scopus 로고    scopus 로고
    • An IgG3 switch variant of rituximab mediates enhanced complement-dependent cytotoxicity against tumour cells with low CD20 expression levels
    • 24 Rosner, T., et al. An IgG3 switch variant of rituximab mediates enhanced complement-dependent cytotoxicity against tumour cells with low CD20 expression levels. Br. J. Haematol. 161 (2013), 282–286.
    • (2013) Br. J. Haematol. , vol.161 , pp. 282-286
    • Rosner, T.1
  • 25
    • 0037474543 scopus 로고    scopus 로고
    • Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity
    • 25 Krapp, S., et al. Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. J. Mol. Biol. 325 (2003), 979–989.
    • (2003) J. Mol. Biol. , vol.325 , pp. 979-989
    • Krapp, S.1
  • 26
    • 84906217310 scopus 로고    scopus 로고
    • Structural characterization of anti-inflammatory immunoglobulin G Fc proteins
    • 26 Ahmed, A.A., et al. Structural characterization of anti-inflammatory immunoglobulin G Fc proteins. J. Mol. Biol. 426 (2014), 3166–3179.
    • (2014) J. Mol. Biol. , vol.426 , pp. 3166-3179
    • Ahmed, A.A.1
  • 27
    • 84958559635 scopus 로고    scopus 로고
    • The emerging importance of IgG Fab glycosylation in immunity
    • 27 van de Bovenkamp, F.S., The emerging importance of IgG Fab glycosylation in immunity. J Immunol. 196 (2016), 1435–1441.
    • (2016) J Immunol. , vol.196 , pp. 1435-1441
    • van de Bovenkamp, F.S.1
  • 28
    • 84947032537 scopus 로고    scopus 로고
    • The structural role of antibody N-glycosylation in receptor interactions
    • 28 Subedi, G.P., Barb, A.W., The structural role of antibody N-glycosylation in receptor interactions. Structure 23 (2015), 1573–1583.
    • (2015) Structure , vol.23 , pp. 1573-1583
    • Subedi, G.P.1    Barb, A.W.2
  • 29
    • 84922360962 scopus 로고    scopus 로고
    • Structure of FcgammaRI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding
    • 29 Lu, J., et al. Structure of FcgammaRI in complex with Fc reveals the importance of glycan recognition for high-affinity IgG binding. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), 833–838.
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. 833-838
    • Lu, J.1
  • 30
    • 67649839223 scopus 로고    scopus 로고
    • N-glycans
    • A. Varki 2nd edn Cold Spring Harbor Laboratory Press
    • 30 Stanley, P., et al. N-glycans. Varki, A., (eds.) Essentials of Glycobiology, 2nd edn, 2009, Cold Spring Harbor Laboratory Press.
    • (2009) Essentials of Glycobiology
    • Stanley, P.1
  • 31
    • 0034685691 scopus 로고    scopus 로고
    • Pairing of oligosaccharides in the Fc region of immunoglobulin G
    • 31 Masuda, K., et al. Pairing of oligosaccharides in the Fc region of immunoglobulin G. FEBS Lett. 473 (2000), 349–357.
    • (2000) FEBS Lett. , vol.473 , pp. 349-357
    • Masuda, K.1
  • 32
    • 84864245160 scopus 로고    scopus 로고
    • Effect of bisecting GlcNAc and core fucosylation on conformational properties of biantennary complex-type N-glycans in solution
    • 32 Nishima, W., et al. Effect of bisecting GlcNAc and core fucosylation on conformational properties of biantennary complex-type N-glycans in solution. J. Phys. Chem. B 116 (2012), 8504–8512.
    • (2012) J. Phys. Chem. B , vol.116 , pp. 8504-8512
    • Nishima, W.1
  • 33
    • 0028962403 scopus 로고
    • Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein
    • 33 Malhotra, R., et al. Glycosylation changes of IgG associated with rheumatoid arthritis can activate complement via the mannose-binding protein. Nat. Med. 1 (1995), 237–243.
    • (1995) Nat. Med. , vol.1 , pp. 237-243
    • Malhotra, R.1
  • 34
    • 84962382941 scopus 로고    scopus 로고
    • Fc-galactosylation modulates antibody-dependent cellular cytotoxicity of therapeutic antibodies
    • 34 Thomann, M., et al. Fc-galactosylation modulates antibody-dependent cellular cytotoxicity of therapeutic antibodies. Mol. Immunol. 73 (2016), 69–75.
    • (2016) Mol. Immunol. , vol.73 , pp. 69-75
    • Thomann, M.1
  • 35
    • 42349085035 scopus 로고    scopus 로고
    • Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc
    • 35 Anthony, R.M., et al. Recapitulation of IVIG anti-inflammatory activity with a recombinant IgG Fc. Science 320 (2008), 373–376.
    • (2008) Science , vol.320 , pp. 373-376
    • Anthony, R.M.1
  • 36
    • 33746888249 scopus 로고    scopus 로고
    • Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation
    • 36 Kaneko, Y., et al. Anti-inflammatory activity of immunoglobulin G resulting from Fc sialylation. Science 313 (2006), 670–673.
    • (2006) Science , vol.313 , pp. 670-673
    • Kaneko, Y.1
  • 37
    • 84925324765 scopus 로고    scopus 로고
    • Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity
    • 37 Washburn, N., et al. Controlled tetra-Fc sialylation of IVIg results in a drug candidate with consistent enhanced anti-inflammatory activity. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), E1297–E1306.
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. E1297-E1306
    • Washburn, N.1
  • 38
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway
    • 38 Anthony, R.M., et al. Intravenous gammaglobulin suppresses inflammation through a novel T(H)2 pathway. Nature 475 (2011), 110–113.
    • (2011) Nature , vol.475 , pp. 110-113
    • Anthony, R.M.1
  • 39
    • 84878963540 scopus 로고    scopus 로고
    • General mechanism for modulating immunoglobulin effector function
    • 39 Sondermann, P., et al. General mechanism for modulating immunoglobulin effector function. Proc. Natl. Acad. Sci. U. S. A. 110 (2013), 9868–9872.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 9868-9872
    • Sondermann, P.1
  • 40
    • 84875749746 scopus 로고    scopus 로고
    • Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain
    • 40 Yu, X., et al. Dissecting the molecular mechanism of IVIg therapy: the interaction between serum IgG and DC-SIGN is independent of antibody glycoform or Fc domain. J. Mol. Biol. 425 (2013), 1253–1258.
    • (2013) J. Mol. Biol. , vol.425 , pp. 1253-1258
    • Yu, X.1
  • 41
    • 77956566546 scopus 로고    scopus 로고
    • IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes
    • 41 Seite, J.F., et al. IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes. Blood 116 (2010), 1698–1704.
    • (2010) Blood , vol.116 , pp. 1698-1704
    • Seite, J.F.1
  • 42
    • 84896692591 scopus 로고    scopus 로고
    • Dendritic cell immunoreceptor: a novel receptor for intravenous immunoglobulin mediates induction of regulatory T cells
    • e5
    • 42 Massoud, A.H., et al. Dendritic cell immunoreceptor: a novel receptor for intravenous immunoglobulin mediates induction of regulatory T cells. J. Allergy Clin. Immunol. 133 (2014), 853–863 e5.
    • (2014) J. Allergy Clin. Immunol. , vol.133 , pp. 853-863
    • Massoud, A.H.1
  • 43
    • 34547455672 scopus 로고    scopus 로고
    • Fc receptor-like 5 inhibits B cell activation via SHP-1 tyrosine phosphatase recruitment
    • 43 Haga, C.L., et al. Fc receptor-like 5 inhibits B cell activation via SHP-1 tyrosine phosphatase recruitment. Proc. Natl. Acad. Sci. U. S. A. 104 (2007), 9770–9775.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 9770-9775
    • Haga, C.L.1
  • 44
    • 0037178791 scopus 로고    scopus 로고
    • Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity
    • 44 Shields, R.L., et al. Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human Fcgamma RIII and antibody-dependent cellular toxicity. J. Biol. Chem. 277 (2002), 26733–26740.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26733-26740
    • Shields, R.L.1
  • 45
    • 0037474276 scopus 로고    scopus 로고
    • 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
    • 45 Shinkawa, T., 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. 278 (2003), 3466–3473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3466-3473
    • Shinkawa, T.1
  • 46
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex
    • 46 Sondermann, P., et al. The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature 406 (2000), 267–273.
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1
  • 47
    • 33646172632 scopus 로고    scopus 로고
    • The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms
    • 47 Ferrara, C., et al. The carbohydrate at FcgammaRIIIa Asn-162. An element required for high affinity binding to non-fucosylated IgG glycoforms. J. Biol. Chem. 281 (2006), 5032–5036.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5032-5036
    • Ferrara, C.1
  • 48
    • 79961233787 scopus 로고    scopus 로고
    • Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose
    • 48 Ferrara, C., et al. Unique carbohydrate-carbohydrate interactions are required for high affinity binding between FcgammaRIII and antibodies lacking core fucose. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 12669–12674.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 12669-12674
    • Ferrara, C.1
  • 49
    • 0035921175 scopus 로고    scopus 로고
    • Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII
    • 49 Davies, J., et al. Expression of GnTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies with altered glycoforms leads to an increase in ADCC through higher affinity for FC gamma RIII. Biotechnol. Bioeng. 74 (2001), 288–294.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 288-294
    • Davies, J.1
  • 50
    • 84899427302 scopus 로고    scopus 로고
    • The absence of core fucose up-regulates GnT-III and Wnt target genes: a possible mechanism for an adaptive response in terms of glycan function
    • 50 Kurimoto, A., et al. The absence of core fucose up-regulates GnT-III and Wnt target genes: a possible mechanism for an adaptive response in terms of glycan function. J. Biol. Chem. 289 (2014), 11704–11714.
    • (2014) J. Biol. Chem. , vol.289 , pp. 11704-11714
    • Kurimoto, A.1
  • 51
    • 84863874149 scopus 로고    scopus 로고
    • Mechanisms of Fc receptor and dectin-1 activation for phagocytosis
    • 51 Goodridge, H.S., et al. Mechanisms of Fc receptor and dectin-1 activation for phagocytosis. Traffic 13 (2012), 1062–1071.
    • (2012) Traffic , vol.13 , pp. 1062-1071
    • Goodridge, H.S.1
  • 52
    • 84945315708 scopus 로고    scopus 로고
    • Of ITIMs, ITAMs, and ITAMis: revisiting immunoglobulin Fc receptor signaling
    • 52 Getahun, A., Cambier, J.C., Of ITIMs, ITAMs, and ITAMis: revisiting immunoglobulin Fc receptor signaling. Immunol. Rev. 268 (2015), 66–73.
    • (2015) Immunol. Rev. , vol.268 , pp. 66-73
    • Getahun, A.1    Cambier, J.C.2
  • 53
    • 84945292492 scopus 로고    scopus 로고
    • Cross-talk between pathogen recognizing Toll-like receptors and immunoglobulin Fc receptors in immunity
    • 53 van Egmond, M., et al. Cross-talk between pathogen recognizing Toll-like receptors and immunoglobulin Fc receptors in immunity. Immunol. Rev. 268 (2015), 311–327.
    • (2015) Immunol. Rev. , vol.268 , pp. 311-327
    • van Egmond, M.1
  • 54
    • 26444577543 scopus 로고    scopus 로고
    • Activating and inhibitory IgG Fc receptors on human DCs mediate opposing functions
    • 54 Boruchov, A.M., et al. Activating and inhibitory IgG Fc receptors on human DCs mediate opposing functions. J. Clin. Invest. 115 (2005), 2914–2923.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2914-2923
    • Boruchov, A.M.1
  • 55
    • 0036151027 scopus 로고    scopus 로고
    • ITAMs versus ITIMs: striking a balance during cell regulation
    • 55 Billadeau, D.D., Leibson, P.J., ITAMs versus ITIMs: striking a balance during cell regulation. J. Clin. Invest. 109 (2002), 161–168.
    • (2002) J. Clin. Invest. , vol.109 , pp. 161-168
    • Billadeau, D.D.1    Leibson, P.J.2
  • 56
    • 84866017430 scopus 로고    scopus 로고
    • The immunoglobulin, IgG Fc receptor and complement triangle in autoimmune diseases
    • 56 Karsten, C.M., Kohl, J., The immunoglobulin, IgG Fc receptor and complement triangle in autoimmune diseases. Immunobiology 217 (2012), 1067–1079.
    • (2012) Immunobiology , vol.217 , pp. 1067-1079
    • Karsten, C.M.1    Kohl, J.2
  • 57
    • 84886309053 scopus 로고    scopus 로고
    • Overview of complement activation and regulation
    • 57 Noris, M., Remuzzi, G., Overview of complement activation and regulation. Semin. Nephrol. 33 (2013), 479–492.
    • (2013) Semin. Nephrol. , vol.33 , pp. 479-492
    • Noris, M.1    Remuzzi, G.2
  • 58
    • 84896055730 scopus 로고    scopus 로고
    • Complement is activated by IgG hexamers assembled at the cell surface
    • 58 Diebolder, C.A., et al. Complement is activated by IgG hexamers assembled at the cell surface. Science 343 (2014), 1260–1263.
    • (2014) Science , vol.343 , pp. 1260-1263
    • Diebolder, C.A.1
  • 59
    • 70349437186 scopus 로고    scopus 로고
    • Complement regulators and inhibitory proteins
    • 59 Zipfel, P.F., Skerka, C., Complement regulators and inhibitory proteins. Nat. Rev. Immunol. 9 (2009), 729–740.
    • (2009) Nat. Rev. Immunol. , vol.9 , pp. 729-740
    • Zipfel, P.F.1    Skerka, C.2
  • 60
    • 84877152391 scopus 로고    scopus 로고
    • Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity
    • 60 Ackerman, M.E., et al. Natural variation in Fc glycosylation of HIV-specific antibodies impacts antiviral activity. J. Clin. Invest 123 (2013), 2183–2192.
    • (2013) J. Clin. Invest , vol.123 , pp. 2183-2192
    • Ackerman, M.E.1
  • 61
    • 33749159828 scopus 로고    scopus 로고
    • Galactosylation of IgG from rheumatoid arthritis (RA) patients – changes during therapy
    • 61 Pasek, M., et al. Galactosylation of IgG from rheumatoid arthritis (RA) patients – changes during therapy. Glycoconj. J. 23 (2006), 463–471.
    • (2006) Glycoconj. J. , vol.23 , pp. 463-471
    • Pasek, M.1
  • 62
    • 84893121418 scopus 로고    scopus 로고
    • A prominent lack of IgG1-Fc fucosylation of platelet alloantibodies in pregnancy
    • 62 Kapur, R., et al. A prominent lack of IgG1-Fc fucosylation of platelet alloantibodies in pregnancy. Blood 123 (2014), 471–480.
    • (2014) Blood , vol.123 , pp. 471-480
    • Kapur, R.1
  • 63
    • 84891958414 scopus 로고    scopus 로고
    • Glycosylation of immunoglobulin G: role of genetic and epigenetic influences
    • 63 Menni, C., et al. Glycosylation of immunoglobulin G: role of genetic and epigenetic influences. PLoS One, 8, 2013, e82558.
    • (2013) PLoS One , vol.8 , pp. e82558
    • Menni, C.1
  • 64
    • 0022414766 scopus 로고
    • Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
    • 64 Parekh, R.B., et al. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 316 (1985), 452–457.
    • (1985) Nature , vol.316 , pp. 452-457
    • Parekh, R.B.1
  • 65
    • 84946023390 scopus 로고    scopus 로고
    • Association of systemic lupus erythematosus with decreased immunosuppressive potential of the IgG glycome
    • 65 Vuckovic, F., et al. Association of systemic lupus erythematosus with decreased immunosuppressive potential of the IgG glycome. Arthritis Rheumatol. 67 (2015), 2978–2989.
    • (2015) Arthritis Rheumatol. , vol.67 , pp. 2978-2989
    • Vuckovic, F.1
  • 66
    • 40549142075 scopus 로고    scopus 로고
    • Induction of macrophage secretion of tumor necrosis factor alpha through Fcgamma receptor IIa engagement by rheumatoid arthritis-specific autoantibodies to citrullinated proteins complexed with fibrinogen
    • 66 Clavel, C., et al. Induction of macrophage secretion of tumor necrosis factor alpha through Fcgamma receptor IIa engagement by rheumatoid arthritis-specific autoantibodies to citrullinated proteins complexed with fibrinogen. Arthritis Rheum. 58 (2008), 678–688.
    • (2008) Arthritis Rheum. , vol.58 , pp. 678-688
    • Clavel, C.1
  • 67
    • 84907008496 scopus 로고    scopus 로고
    • Shifting FcgammaRIIA-ITAM from activation to inhibitory configuration ameliorates arthritis
    • 67 Ben Mkaddem, S., et al. Shifting FcgammaRIIA-ITAM from activation to inhibitory configuration ameliorates arthritis. J. Clin. Invest. 124 (2014), 3945–3959.
    • (2014) J. Clin. Invest. , vol.124 , pp. 3945-3959
    • Ben Mkaddem, S.1
  • 68
    • 84864484027 scopus 로고    scopus 로고
    • IgG glycan hydrolysis by endoglycosidase S diminishes the proinflammatory properties of immune complexes from patients with systemic lupus erythematosus: a possible new treatment?
    • 68 Lood, C., et al. IgG glycan hydrolysis by endoglycosidase S diminishes the proinflammatory properties of immune complexes from patients with systemic lupus erythematosus: a possible new treatment?. Arthritis Rheum. 64 (2012), 2698–2706.
    • (2012) Arthritis Rheum. , vol.64 , pp. 2698-2706
    • Lood, C.1
  • 69
    • 84962467040 scopus 로고    scopus 로고
    • Antigen-specific antibody glycosylation is regulated via vaccination
    • 69 Mahan, A.E., et al. Antigen-specific antibody glycosylation is regulated via vaccination. PLoS Pathog., 12, 2016, e1005456.
    • (2016) PLoS Pathog. , vol.12 , pp. e1005456
    • Mahan, A.E.1
  • 70
    • 1542283730 scopus 로고    scopus 로고
    • Mechanisms of hypergammaglobulinemia and impaired antigen-specific humoral immunity in HIV-1 infection
    • 70 De Milito, A., et al. Mechanisms of hypergammaglobulinemia and impaired antigen-specific humoral immunity in HIV-1 infection. Blood 103 (2004), 2180–2186.
    • (2004) Blood , vol.103 , pp. 2180-2186
    • De Milito, A.1
  • 71
    • 84975061761 scopus 로고    scopus 로고
    • IgG1 Fc N-glycan galactosylation as a biomarker for immune activation
    • 71 de Jong, S.E., et al. IgG1 Fc N-glycan galactosylation as a biomarker for immune activation. Sci. Rep., 6, 2016, 28207.
    • (2016) Sci. Rep. , vol.6 , pp. 28207
    • de Jong, S.E.1
  • 72
    • 84859877617 scopus 로고    scopus 로고
    • Changes in antigen-specific IgG1 Fc N-glycosylation upon influenza and tetanus vaccination
    • M111.014563
    • 72 Selman, M.H., et al. Changes in antigen-specific IgG1 Fc N-glycosylation upon influenza and tetanus vaccination. Mol. Cell. Proteomics, 11, 2012 M111.014563.
    • (2012) Mol. Cell. Proteomics , vol.11
    • Selman, M.H.1
  • 73
    • 61849180382 scopus 로고    scopus 로고
    • Variability, heritability and environmental determinants of human plasma N-glycome
    • 73 Knezevic, A., et al. Variability, heritability and environmental determinants of human plasma N-glycome. J. Proteome Res. 8 (2009), 694–701.
    • (2009) J. Proteome Res. , vol.8 , pp. 694-701
    • Knezevic, A.1
  • 74
    • 84872685546 scopus 로고    scopus 로고
    • Genomics and epigenomics of the human glycome
    • 74 Zoldos, V., et al. Genomics and epigenomics of the human glycome. Glycoconj. J. 30 (2013), 41–50.
    • (2013) Glycoconj. J. , vol.30 , pp. 41-50
    • Zoldos, V.1
  • 75
    • 81855226434 scopus 로고    scopus 로고
    • Polymorphisms in B3GAT1, SLC9A9 and MGAT5 are associated with variation within the human plasma N-glycome of 3533 European adults
    • 75 Huffman, J.E., et al. Polymorphisms in B3GAT1, SLC9A9 and MGAT5 are associated with variation within the human plasma N-glycome of 3533 European adults. Hum. Mol. Genet. 20 (2011), 5000–5011.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 5000-5011
    • Huffman, J.E.1
  • 76
    • 65549131351 scopus 로고    scopus 로고
    • Elevated Golgi pH impairs terminal N-glycosylation by inducing mislocalization of Golgi glycosyltransferases
    • 76 Rivinoja, A., et al. Elevated Golgi pH impairs terminal N-glycosylation by inducing mislocalization of Golgi glycosyltransferases. J. Cell. Physiol. 220 (2009), 144–154.
    • (2009) J. Cell. Physiol. , vol.220 , pp. 144-154
    • Rivinoja, A.1
  • 77
    • 84873495247 scopus 로고    scopus 로고
    • Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers
    • 77 Lauc, G., et al. Loci associated with N-glycosylation of human immunoglobulin G show pleiotropy with autoimmune diseases and haematological cancers. PLoS Genet., 9, 2013, e1003225.
    • (2013) PLoS Genet. , vol.9 , pp. e1003225
    • Lauc, G.1
  • 78
    • 84902271562 scopus 로고    scopus 로고
    • Glycans are a novel biomarker of chronological and biological ages
    • 78 Kristic, J., et al. Glycans are a novel biomarker of chronological and biological ages. J. Gerontol. A Biol. Sci. Med. Sci. 69 (2014), 779–789.
    • (2014) J. Gerontol. A Biol. Sci. Med. Sci. , vol.69 , pp. 779-789
    • Kristic, J.1
  • 79
    • 84862826701 scopus 로고    scopus 로고
    • Human IgG Fc-glycosylation profiling reveals associations with age, sex, female sex hormones and thyroid cancer
    • 79 Chen, G., et al. Human IgG Fc-glycosylation profiling reveals associations with age, sex, female sex hormones and thyroid cancer. J. Proteomics 75 (2012), 2824–2834.
    • (2012) J. Proteomics , vol.75 , pp. 2824-2834
    • Chen, G.1
  • 80
    • 77954518174 scopus 로고    scopus 로고
    • Effects of aging, body mass index, plasma lipid profiles, and smoking on human plasma N-glycans
    • 80 Knezevic, A., et al. Effects of aging, body mass index, plasma lipid profiles, and smoking on human plasma N-glycans. Glycobiology 20 (2010), 959–969.
    • (2010) Glycobiology , vol.20 , pp. 959-969
    • Knezevic, A.1
  • 81
    • 84899105650 scopus 로고    scopus 로고
    • Polyfunctional Fc-effector profiles mediated by IgG subclass selection distinguish RV144 and VAX003 vaccines
    • 81 Chung, A.W., et al. Polyfunctional Fc-effector profiles mediated by IgG subclass selection distinguish RV144 and VAX003 vaccines. Sci. Transl. Med., 6, 2014, 228ra38.
    • (2014) Sci. Transl. Med. , vol.6 , pp. 228ra38
    • Chung, A.W.1
  • 82
    • 84899087118 scopus 로고    scopus 로고
    • Vaccine-induced Env V1-V2 IgG3 correlates with lower HIV-1 infection risk and declines soon after vaccination
    • 82 Yates, N.L., et al. Vaccine-induced Env V1-V2 IgG3 correlates with lower HIV-1 infection risk and declines soon after vaccination. Sci. Transl. Med., 6, 2014, 228ra39.
    • (2014) Sci. Transl. Med. , vol.6 , pp. 228ra39
    • Yates, N.L.1
  • 83
    • 56149123448 scopus 로고    scopus 로고
    • A novel role for non-neutralizing antibodies against nucleoprotein in facilitating resistance to influenza virus
    • 83 Carragher, D.M., et al. A novel role for non-neutralizing antibodies against nucleoprotein in facilitating resistance to influenza virus. J. Immunol. 181 (2008), 4168–4176.
    • (2008) J. Immunol. , vol.181 , pp. 4168-4176
    • Carragher, D.M.1
  • 84
    • 78149323035 scopus 로고    scopus 로고
    • A requirement for FcgammaR in antibody-mediated bacterial toxin neutralization
    • 84 Abboud, N., et al. A requirement for FcgammaR in antibody-mediated bacterial toxin neutralization. J. Exp. Med. 207 (2010), 2395–2405.
    • (2010) J. Exp. Med. , vol.207 , pp. 2395-2405
    • Abboud, N.1
  • 85
    • 84990842088 scopus 로고    scopus 로고
    • A functional role for antibodies in tuberculosis
    • e14
    • 85 Lu, L.L., et al. A functional role for antibodies in tuberculosis. Cell 167 (2016), 433–443 e14.
    • (2016) Cell , vol.167 , pp. 433-443
    • Lu, L.L.1
  • 86
    • 15944399015 scopus 로고    scopus 로고
    • Increased levels of galactose-deficient IgG in sera of HIV-1-infected individuals
    • 86 Moore, J.S., et al. Increased levels of galactose-deficient IgG in sera of HIV-1-infected individuals. AIDS 19 (2005), 381–389.
    • (2005) AIDS , vol.19 , pp. 381-389
    • Moore, J.S.1
  • 87
    • 84872576077 scopus 로고    scopus 로고
    • Specific antibody-dependent cellular cytotoxicity responses associated with slow progression of HIV infection
    • 87 Wren, L.H., et al. Specific antibody-dependent cellular cytotoxicity responses associated with slow progression of HIV infection. Immunology 138 (2013), 116–123.
    • (2013) Immunology , vol.138 , pp. 116-123
    • Wren, L.H.1
  • 88
    • 84934290153 scopus 로고    scopus 로고
    • Anti-HA glycoforms drive B cell affinity selection and determine influenza vaccine efficacy
    • 88 Wang, T.T., et al. Anti-HA glycoforms drive B cell affinity selection and determine influenza vaccine efficacy. Cell 162 (2015), 160–169.
    • (2015) Cell , vol.162 , pp. 160-169
    • Wang, T.T.1
  • 89
    • 79955757689 scopus 로고    scopus 로고
    • Fc-glycosylation of IgG1 is modulated by B-cell stimuli
    • M110.004655
    • 89 Wang, J., et al. Fc-glycosylation of IgG1 is modulated by B-cell stimuli. Mol. Cell. Proteomics, 10, 2011 M110.004655.
    • (2011) Mol. Cell. Proteomics , vol.10
    • Wang, J.1
  • 90
    • 33750939466 scopus 로고    scopus 로고
    • Glycan analysis of monoclonal antibodies secreted in deposition disorders indicates that subsets of plasma cells differentially process IgG glycans
    • 90 Omtvedt, L.A., et al. Glycan analysis of monoclonal antibodies secreted in deposition disorders indicates that subsets of plasma cells differentially process IgG glycans. Arthritis Rheum. 54 (2006), 3433–3440.
    • (2006) Arthritis Rheum. , vol.54 , pp. 3433-3440
    • Omtvedt, L.A.1
  • 91
    • 84862728161 scopus 로고    scopus 로고
    • Vertebrate protein glycosylation: diversity, synthesis and function
    • 91 Moremen, K.W., et al. Vertebrate protein glycosylation: diversity, synthesis and function. Nat. Rev. Mol. Cell Biol. 13 (2012), 448–462.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 448-462
    • Moremen, K.W.1
  • 92
    • 84918808671 scopus 로고    scopus 로고
    • Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylation
    • 92 Voss, M., et al. Shedding of glycan-modifying enzymes by signal peptide peptidase-like 3 (SPPL3) regulates cellular N-glycosylation. EMBO J. 33 (2014), 2890–2905.
    • (2014) EMBO J. , vol.33 , pp. 2890-2905
    • Voss, M.1
  • 93
    • 84885121957 scopus 로고    scopus 로고
    • Effects of microRNAs on fucosyltransferase 8 (FUT8) expression in hepatocarcinoma cells
    • 93 Bernardi, C., et al. Effects of microRNAs on fucosyltransferase 8 (FUT8) expression in hepatocarcinoma cells. PLoS One, 8, 2013, e76540.
    • (2013) PLoS One , vol.8 , pp. e76540
    • Bernardi, C.1
  • 94
    • 84896320475 scopus 로고    scopus 로고
    • Changes in IgG and total plasma protein glycomes in acute systemic inflammation
    • 94 Novokmet, M., et al. Changes in IgG and total plasma protein glycomes in acute systemic inflammation. Sci. Rep., 4, 2014, 4347.
    • (2014) Sci. Rep. , vol.4 , pp. 4347
    • Novokmet, M.1
  • 95
    • 84860848749 scopus 로고    scopus 로고
    • Anti-inflammatory IgG production requires functional P1 promoter in beta-galactoside alpha2,6-sialyltransferase 1 (ST6Gal-1) gene
    • 95 Jones, M.B., et al. Anti-inflammatory IgG production requires functional P1 promoter in beta-galactoside alpha2,6-sialyltransferase 1 (ST6Gal-1) gene. J. Biol. Chem. 287 (2012), 15365–15370.
    • (2012) J. Biol. Chem. , vol.287 , pp. 15365-15370
    • Jones, M.B.1
  • 96
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: the neonatal Fc receptor comes of age
    • 96 Roopenian, D.C., Akilesh, S., FcRn: the neonatal Fc receptor comes of age. Nat. Rev. Immunol. 7 (2007), 715–725.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 97
    • 84862495640 scopus 로고    scopus 로고
    • Properties of mouse and human IgG receptors and their contribution to disease models
    • 97 Bruhns, P., Properties of mouse and human IgG receptors and their contribution to disease models. Blood 119 (2012), 5640–5649.
    • (2012) Blood , vol.119 , pp. 5640-5649
    • Bruhns, P.1
  • 98
    • 34247122497 scopus 로고    scopus 로고
    • The impact of glycosylation on the biological function and structure of human immunoglobulins
    • 98 Arnold, J.N., et al. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 25 (2007), 21–50.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 21-50
    • Arnold, J.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.