메뉴 건너뛰기




Volumn 215, Issue 5, 2010, Pages 356-369

Polyreactive antibodies in multidonor-derived immunoglobulin G: Theory and conclusions drawn from experiments

Author keywords

Crossreactivity; Human polyclonal IgG; Multireactivity; Multispecificity; Polyreactivity

Indexed keywords

IMMUNOGLOBULIN G ANTIBODY; MONOMER;

EID: 77950934315     PISSN: 01712985     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.imbio.2009.06.015     Document Type: Article
Times cited : (5)

References (48)
  • 1
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the anti-inflammatory activity of IVIG
    • 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 2008, 105:19571-19578.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 19571-19578
    • Anthony, R.M.1    Wermeling, F.2    Karlsson, M.C.3    Ravetch, J.V.4
  • 2
    • 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
  • 3
    • 0025905663 scopus 로고
    • Natural autoantibodies: from 'horror autotoxicus' to 'gnothi seauton'
    • Avrameas S. Natural autoantibodies: from 'horror autotoxicus' to 'gnothi seauton'. Immunol. Today 1991, 12:154-159.
    • (1991) Immunol. Today , vol.12 , pp. 154-159
    • Avrameas, S.1
  • 4
    • 0024409922 scopus 로고
    • High-dose intravenous immunoglobulin modifies complement-mediated in vivo clearance
    • Basta M., Langlois P.F., Marques M., Frank M.M., Fries L.F. High-dose intravenous immunoglobulin modifies complement-mediated in vivo clearance. Blood 1989, 74:326-333.
    • (1989) Blood , vol.74 , pp. 326-333
    • Basta, M.1    Langlois, P.F.2    Marques, M.3    Frank, M.M.4    Fries, L.F.5
  • 5
    • 0024840088 scopus 로고
    • Mechanism of therapeutic effect of high-dose intravenous immunoglobulin. Attenuation of acute, complement-dependent immune damage in a guinea pig model
    • Basta M., Kirshbom P., Frank M.M., Fries L.F. Mechanism of therapeutic effect of high-dose intravenous immunoglobulin. Attenuation of acute, complement-dependent immune damage in a guinea pig model. J. Clin. Invest. 1989, 84:1974-1981.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1974-1981
    • Basta, M.1    Kirshbom, P.2    Frank, M.M.3    Fries, L.F.4
  • 7
    • 62549095425 scopus 로고    scopus 로고
    • DC-SIGN and alpha2,6-sialylated IgG Fc interaction is dispensable for the anti-inflammatory activity of IVIg on human dendritic cells
    • Bayry J., Bansal K., Kazatchkine M.D., Kaveri S.V. DC-SIGN and alpha2,6-sialylated IgG Fc interaction is dispensable for the anti-inflammatory activity of IVIg on human dendritic cells. Proc. Natl. Acad. Sci. USA 2009, 106:E24.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106
    • Bayry, J.1    Bansal, K.2    Kazatchkine, M.D.3    Kaveri, S.V.4
  • 8
    • 4944230185 scopus 로고    scopus 로고
    • Tetramolecular immune complexes are more efficient than IVIg to prevent antibody-dependent in vitro and in vivo phagocytosis of blood cells
    • Bazin R., Lemieux R., Tremblay T., St-Amour I. Tetramolecular immune complexes are more efficient than IVIg to prevent antibody-dependent in vitro and in vivo phagocytosis of blood cells. Br. J. Haematol. 2004, 127:90-96.
    • (2004) Br. J. Haematol. , vol.127 , pp. 90-96
    • Bazin, R.1    Lemieux, R.2    Tremblay, T.3    St-Amour, I.4
  • 9
    • 53849105452 scopus 로고    scopus 로고
    • Subcutaneous administration of IgG. Immunol
    • Berger M. Subcutaneous administration of IgG. Immunol. Allergy Clin. N. Am. 2008, 28:779-802.
    • (2008) Allergy Clin. N. Am. , vol.28 , pp. 779-802
    • Berger, M.1
  • 10
    • 0028828994 scopus 로고
    • The crystal structure of the antibody N10-staphylococcal nuclease complex at 2.9Å resolution
    • Bossart-Whitaker P., Chang C.Y., Novotny J., Benjamin D.C., Sheriff S. The crystal structure of the antibody N10-staphylococcal nuclease complex at 2.9Å resolution. J. Mol. Biol. 1995, 253:559-575.
    • (1995) J. Mol. Biol. , vol.253 , pp. 559-575
    • Bossart-Whitaker, P.1    Chang, C.Y.2    Novotny, J.3    Benjamin, D.C.4    Sheriff, S.5
  • 11
    • 0027268166 scopus 로고
    • The humoral immune response in autoimmunity
    • Calvanico N.J. The humoral immune response in autoimmunity. Dermatol. Clin. 1993, 11:379-389.
    • (1993) Dermatol. Clin. , vol.11 , pp. 379-389
    • Calvanico, N.J.1
  • 13
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia C., Lesk A.M. Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 1987, 196:901-917.
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 15
    • 0033857820 scopus 로고    scopus 로고
    • Natural antibodies and the host immune response to xenografts
    • Cramer D.V. Natural antibodies and the host immune response to xenografts. Xenotransplantation 2000, 7:83-92.
    • (2000) Xenotransplantation , vol.7 , pp. 83-92
    • Cramer, D.V.1
  • 16
    • 0035669179 scopus 로고    scopus 로고
    • IVIg inhibits reticuloendothelial system function and ameliorates murine passive-immune thrombocytopenia independent of anti-idiotype reactivity
    • Crow A.R., Song S., Semple J.W., Freedman J., Lazarus A.H. IVIg inhibits reticuloendothelial system function and ameliorates murine passive-immune thrombocytopenia independent of anti-idiotype reactivity. Br. J. Hematol. 2001, 115:679-686.
    • (2001) Br. J. Hematol. , vol.115 , pp. 679-686
    • Crow, A.R.1    Song, S.2    Semple, J.W.3    Freedman, J.4    Lazarus, A.H.5
  • 17
    • 0030040277 scopus 로고    scopus 로고
    • Interactions of protein antigens with antibodies
    • Davies D.R., Cohen G.H. Interactions of protein antigens with antibodies. Proc. Natl. Acad. Sci. USA 1996, 93:7-12.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7-12
    • Davies, D.R.1    Cohen, G.H.2
  • 19
    • 84968468809 scopus 로고
    • The numerical integration of ordinary differential equations
    • Gear C.W. The numerical integration of ordinary differential equations. Math. Comput. 1967, 21:146-156.
    • (1967) Math. Comput. , vol.21 , pp. 146-156
    • Gear, C.W.1
  • 21
    • 0027938488 scopus 로고
    • Healthy subjects produce both anti-factor VIII and specific anti-idiotypic antibodies
    • Gilles J.G., Saint-Remy J.M. Healthy subjects produce both anti-factor VIII and specific anti-idiotypic antibodies. J. Clin. Invest. 1994, 94:1496-1505.
    • (1994) J. Clin. Invest. , vol.94 , pp. 1496-1505
    • Gilles, J.G.1    Saint-Remy, J.M.2
  • 22
    • 58049202056 scopus 로고    scopus 로고
    • Effect of intravenous immunoglobulin therapy on serum levels of IgG1 and IgG4 antidesmoglein 1 and antidesmoglein 3 antibodies in pemphigus vulgaris
    • Green M.G., Bystryn J.C. Effect of intravenous immunoglobulin therapy on serum levels of IgG1 and IgG4 antidesmoglein 1 and antidesmoglein 3 antibodies in pemphigus vulgaris. Arch. Dermatol. 2008, 144:1621-1624.
    • (2008) Arch. Dermatol. , vol.144 , pp. 1621-1624
    • Green, M.G.1    Bystryn, J.C.2
  • 23
    • 33644858114 scopus 로고    scopus 로고
    • IgG dimers in multidonor-derived immunoglobulins: aspects of generation and function
    • Gronski P. IgG dimers in multidonor-derived immunoglobulins: aspects of generation and function. Curr. Pharm. Des. 2006, 12:181-190.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 181-190
    • Gronski, P.1
  • 24
    • 33846940736 scopus 로고    scopus 로고
    • Off-rate and concentration diversity in multidonor-derived dimers of immunoglobulin G
    • Gronski P., Schridde C., Kanzy E.J. Off-rate and concentration diversity in multidonor-derived dimers of immunoglobulin G. Mol. Immunol. 2007, 44:2528-2540.
    • (2007) Mol. Immunol. , vol.44 , pp. 2528-2540
    • Gronski, P.1    Schridde, C.2    Kanzy, E.J.3
  • 25
    • 0031868555 scopus 로고    scopus 로고
    • IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation
    • Jefferis R., Lund J., Pound J.D. IgG-Fc-mediated effector functions: molecular definition of interaction sites for effector ligands and the role of glycosylation. Immunol. Rev. 1998, 163:59-76.
    • (1998) Immunol. Rev. , vol.163 , pp. 59-76
    • Jefferis, R.1    Lund, J.2    Pound, J.D.3
  • 26
    • 0015956495 scopus 로고
    • Towards a network theory of the immune system
    • C
    • Jerne N.K. Towards a network theory of the immune system. Ann. Immunol. 1974, 125C:373-386.
    • (1974) Ann. Immunol. , vol.125 , pp. 373-386
    • Jerne, N.K.1
  • 27
    • 0020340081 scopus 로고
    • Recurrent idiotopes and internal images
    • Jerne N.K., Cazenave P.A. Recurrent idiotopes and internal images. EMBO J. 1982, 1:243-247.
    • (1982) EMBO J. , vol.1 , pp. 243-247
    • Jerne, N.K.1    Cazenave, P.A.2
  • 28
    • 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
  • 30
    • 3242691647 scopus 로고    scopus 로고
    • Autoantibodies purified from therapeutic preparations of intravenous immunoglobulins (IVIg) induce the formation of autoimmune complexes in normal human serum: a role in the in vivo mechanisms of action of IVIg?
    • Lamoureux J., Aubin E., Lemieux R. Autoantibodies purified from therapeutic preparations of intravenous immunoglobulins (IVIg) induce the formation of autoimmune complexes in normal human serum: a role in the in vivo mechanisms of action of IVIg?. Int. Immunol. 2004, 16:929-936.
    • (2004) Int. Immunol. , vol.16 , pp. 929-936
    • Lamoureux, J.1    Aubin, E.2    Lemieux, R.3
  • 31
    • 33644861543 scopus 로고    scopus 로고
    • Autoantibody-induced formation of immune complexes in normal human serum
    • Lemieux R., Bazin R. Autoantibody-induced formation of immune complexes in normal human serum. Curr. Pharm. Des. 2006, 12:173-179.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 173-179
    • Lemieux, R.1    Bazin, R.2
  • 33
    • 25444525680 scopus 로고    scopus 로고
    • Comparative analysis of antigen specificities in the monomeric and dimeric fractions of intravenous immunoglobulin
    • Miescher S.M., Schaub A., Ghielmetti M., Baumann M., Vogel M., Bolli R., Stadler B. Comparative analysis of antigen specificities in the monomeric and dimeric fractions of intravenous immunoglobulin. Ann. N. Y. Acad. Sci. 2005, 1051:582-590.
    • (2005) Ann. N. Y. Acad. Sci. , vol.1051 , pp. 582-590
    • Miescher, S.M.1    Schaub, A.2    Ghielmetti, M.3    Baumann, M.4    Vogel, M.5    Bolli, R.6    Stadler, B.7
  • 34
    • 0032516765 scopus 로고    scopus 로고
    • Structural basis for the binding of an anti-cytochrome c antibody to its antigen: crystal structures of FabE8-cytochrome c complex to 1.8Å resolution and FabE8 to 2.26Å resolution
    • Mylvaganam S.E., Paterson Y., Getzoff E.D. Structural basis for the binding of an anti-cytochrome c antibody to its antigen: crystal structures of FabE8-cytochrome c complex to 1.8Å resolution and FabE8 to 2.26Å resolution. J. Mol. Biol. 1998, 281:301-322.
    • (1998) J. Mol. Biol. , vol.281 , pp. 301-322
    • Mylvaganam, S.E.1    Paterson, Y.2    Getzoff, E.D.3
  • 35
    • 0018567632 scopus 로고
    • Theoretical studies of clonal selection: minimal antibody repertoire size and reliability of self-non-self discrimination
    • Perelson A.S., Oster G.F. Theoretical studies of clonal selection: minimal antibody repertoire size and reliability of self-non-self discrimination. J. Theor. Biol. 1979, 81:645-670.
    • (1979) J. Theor. Biol. , vol.81 , pp. 645-670
    • Perelson, A.S.1    Oster, G.F.2
  • 36
    • 17344368340 scopus 로고    scopus 로고
    • Divergent roles for Fc receptors and complement in vivo
    • Ravetch J.V., Clynes R.A. Divergent roles for Fc receptors and complement in vivo. Annu. Rev. Immunol. 1998, 16:421-432.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 421-432
    • Ravetch, J.V.1    Clynes, R.A.2
  • 38
    • 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
  • 40
    • 0023744302 scopus 로고
    • Immunoglobulin G dimer: an idiotype-anti-idiotype complex
    • Tankersley D.L., Preston M.S., Finlayson J.S. Immunoglobulin G dimer: an idiotype-anti-idiotype complex. Mol. Immunol. 1988, 25:41-48.
    • (1988) Mol. Immunol. , vol.25 , pp. 41-48
    • Tankersley, D.L.1    Preston, M.S.2    Finlayson, J.S.3
  • 41
    • 0035883092 scopus 로고    scopus 로고
    • Therapeutic efficacy of intravenous immunoglobulin preparations depends on the IgG dimers: studies in experimental immune thrombocytopenia
    • Teeling J.L., Jansen-Hendriks T., Kuijpers T.W., Haas M., Winkel J.G.J., Hack C.E., Bleeker W.K. Therapeutic efficacy of intravenous immunoglobulin preparations depends on the IgG dimers: studies in experimental immune thrombocytopenia. Blood 2001, 98:1095-1099.
    • (2001) Blood , vol.98 , pp. 1095-1099
    • Teeling, J.L.1    Jansen-Hendriks, T.2    Kuijpers, T.W.3    Haas, M.4    Winkel, J.G.J.5    Hack, C.E.6    Bleeker, W.K.7
  • 43
    • 0026781840 scopus 로고
    • Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex
    • Tulip W.R., Varghese J.N., Laver W.G., Webster R.G., Colman P.M. Refined crystal structure of the influenza virus N9 neuraminidase-NC41 Fab complex. J. Mol. Biol. 1992, 227:122-148.
    • (1992) J. Mol. Biol. , vol.227 , pp. 122-148
    • Tulip, W.R.1    Varghese, J.N.2    Laver, W.G.3    Webster, R.G.4    Colman, P.M.5
  • 44
    • 0025091498 scopus 로고
    • On the mechanism of high-dose intravenous immunoglobulin treatment of patients with chronic inflammatory demyelinating polyneuropathy
    • Doorn P.A., Rossi F., Brand A., Lint M., Vermeulen M., Kazatchkine M.D. On the mechanism of high-dose intravenous immunoglobulin treatment of patients with chronic inflammatory demyelinating polyneuropathy. J. Neuroimmunol. 1990, 29:57-64.
    • (1990) J. Neuroimmunol. , vol.29 , pp. 57-64
    • Doorn, P.A.1    Rossi, F.2    Brand, A.3    Lint, M.4    Vermeulen, M.5    Kazatchkine, M.D.6
  • 46
    • 0029553186 scopus 로고
    • The effector functions of immunoglobulins: implications for therapy
    • Ward E.S., Ghetie V. The effector functions of immunoglobulins: implications for therapy. Ther. Immunol. 1995, 2:77-94.
    • (1995) Ther. Immunol. , vol.2 , pp. 77-94
    • Ward, E.S.1    Ghetie, V.2
  • 47
    • 40849104949 scopus 로고    scopus 로고
    • Monomerization of dimeric IgG of intravenous immunoglobulin (IVIg) increases the antibody reactivity against intracellular antigens
    • Wymann S., Ghielmetti M., Schaub A., Baumann M.J., Stadler B.M., Bolli R., Miescher S.M. Monomerization of dimeric IgG of intravenous immunoglobulin (IVIg) increases the antibody reactivity against intracellular antigens. Mol. Immunol. 2008, 45:2621-2628.
    • (2008) Mol. Immunol. , vol.45 , pp. 2621-2628
    • Wymann, S.1    Ghielmetti, M.2    Schaub, A.3    Baumann, M.J.4    Stadler, B.M.5    Bolli, R.6    Miescher, S.M.7
  • 48
    • 35448975223 scopus 로고    scopus 로고
    • Properties and function of polyreactive antibodies and polyreactive antigen-binding B cells
    • Zhou Z.H., Tzioufas A.G., Notkins A.L. Properties and function of polyreactive antibodies and polyreactive antigen-binding B cells. J. Autoimmun. 2007, 29:219-228.
    • (2007) J. Autoimmun. , vol.29 , pp. 219-228
    • Zhou, Z.H.1    Tzioufas, A.G.2    Notkins, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.