메뉴 건너뛰기




Volumn 1, Issue , 2011, Pages

Polymeric human Fc-fusion proteins with modified effector functions

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT; FC RECEPTOR; FC RECEPTOR, NEONATAL; HLA ANTIGEN CLASS 1; HYBRID PROTEIN; IMMUNOGLOBULIN FC FRAGMENT; IMMUNOGLOBULIN G; PRIMER DNA;

EID: 84859760033     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep00124     Document Type: Article
Times cited : (64)

References (57)
  • 1
    • 70449723296 scopus 로고    scopus 로고
    • Discovery and development of biopharmaceuticals: Current issues
    • Strohl, W. R, Knight, D. M. Discovery and development of biopharmaceuticals: current issues. Curr Opin Biotech 20, 668-672 (2009).
    • (2009) Curr Opin Biotech , vol.20 , pp. 668-672
    • Strohl, W.R.1    Knight, D.M.2
  • 2
    • 70449706366 scopus 로고    scopus 로고
    • Receptor-Fc fusion therapeutics, traps, and MIMETIBODYTM technology
    • Huang, C. Receptor-Fc fusion therapeutics, traps, and MIMETIBODYTM technology. Curr Opin Biotech 20, 692-699 (2009).
    • (2009) Curr Opin Biotech , vol.20 , pp. 692-699
    • Huang, C.1
  • 3
    • 34548229364 scopus 로고    scopus 로고
    • FcRn: The neonatal Fc receptor comes of age
    • DOI 10.1038/nri2155, PII NRI2155
    • Roopenian, D. C. & Akilesh, S. FcRn: the neonatal Fc receptor comes of age. Nat Rev Immunol 7, 715-25 (2007). (Pubitemid 47327396)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.9 , pp. 715-725
    • Roopenian, D.C.1    Akilesh, S.2
  • 5
    • 37549036732 scopus 로고    scopus 로고
    • Fc-receptors as regulators of immune responses
    • Nimmerjahn, F. & Ravetch, J. V. Fc-receptors as regulators of immune responses. Nat Rev Immunol 8, 34-47 (2008).
    • (2008) Nat Rev Immunol , vol.8 , pp. 34-47
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 6
    • 35548955496 scopus 로고    scopus 로고
    • Fc-Receptors as Regulators of Immunity
    • DOI 10.1016/S0065-2776(07)96005-8, PII S0065277607960058
    • Nimmerjahn, F. & Ravetch, J. V. Fc-receptors as regulators of immunity. Adv Immunol 96, 179-204 (2007). (Pubitemid 350018720)
    • (2007) Advances in Immunology , vol.96 , pp. 179-204
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 9
    • 0037033448 scopus 로고    scopus 로고
    • Antitumor monoclonal antibodies enhance cross-presentation of cellular antigens and the generation of myeloma-specific killer T cells by dendritic cells
    • DOI 10.1084/jem.20011097
    • Dhodapkar, K. M., Krasovsky, J., Williamson, B., Dhodapkar, M. V. Antitumour monoclonal Abs enhance cross-presentation of cellular Ags and the generation of myeloma-specific killer T cells by dendritic cells. J Exp Med 195, 125-33 (2002). (Pubitemid 34074502)
    • (2002) Journal of Experimental Medicine , vol.195 , Issue.1 , pp. 125-133
    • Dhodapkar, K.M.1    Krasovsky, J.2    Williamson, B.3    Dhodapkar, M.V.4
  • 11
    • 0036307752 scopus 로고    scopus 로고
    • Immune complex-mediated antigen presentation induces tumor immunity
    • DOI 10.1172/JCI200215640
    • Rafiq, K., Bergtold, A. & Clynes, R. Immune complex-mediated Ag presentation induces tumor immunity. J Clin Invest 110, 71-9 (2002). (Pubitemid 34743467)
    • (2002) Journal of Clinical Investigation , vol.110 , Issue.1 , pp. 71-79
    • Rafiq, K.1    Bergtold, A.2    Clynes, R.3
  • 12
    • 33645775989 scopus 로고    scopus 로고
    • Immune complex-loaded dendritic cells are superior to soluble immune complexes as antitumor vaccine
    • Schuurhuis, D. H, et al. Immune complex-loaded dendritic cells are superior to soluble immune complexes as antitumor vaccine. J Immunol 176, 4573-80 (2006).
    • (2006) J Immunol , vol.176 , pp. 4573-4580
    • Schuurhuis, D.H.1
  • 13
    • 79959946173 scopus 로고    scopus 로고
    • Neonatal Fc receptor for IgG (FcRn) regulates cross-presentation of IgG immune-complexes by CD8-CD11b1dendritic cells
    • Baker, K. et al. Neonatal Fc receptor for IgG (FcRn) regulates cross-presentation of IgG immune-complexes by CD8-CD11b1dendritic cells. Proc Natl Acad Sci USA 108, 9927-32 (2011).
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 9927-9932
    • Baker, K.1
  • 14
    • 27744576801 scopus 로고    scopus 로고
    • Cell surface recycling of internalized antigen permits dendritic cell priming of B cells
    • DOI 10.1016/j.immuni.2005.09.013, PII S1074761305003092
    • Bergtold, A., Desai, D. D., Gavhane, A. & Clynes, R. Cell surface recycling of internalized Ag permits dendritic cell priming of B cells. Immunity 23, 503-14 (2005). (Pubitemid 41587890)
    • (2005) Immunity , vol.23 , Issue.5 , pp. 503-514
    • Bergtold, A.1    Desai, D.D.2    Gavhane, A.3    Clynes, R.4
  • 15
    • 0037124367 scopus 로고    scopus 로고
    • Inducing tumor immunity through the selective engagement of activating Fcγ receptors on dendritic cells
    • DOI 10.1084/jem.20020338
    • Kalergis, A. M. & Ravetch, J. V. Inducing tumor immunity through the selective engagement of activating Fcc-receptors on dendritic cells. J Exp Med 195, 1653-59 (2002). (Pubitemid 34666079)
    • (2002) Journal of Experimental Medicine , vol.195 , Issue.12 , pp. 1653-1659
    • Kalergis, A.M.1    Ravetch, J.V.2
  • 18
    • 0028985495 scopus 로고
    • Addition of a mu-tailpiece to IgG results in polymeric Abswith enhanced effector functions including complementmediated cytolysis by IgG4
    • Smith, R. I., Coloma, M. J. & Morrison, S. L. Addition of a mu-tailpiece to IgG results in polymeric Abswith enhanced effector functions including complementmediated cytolysis by IgG4. J Immunol 154, 2226-36 (1995).
    • (1995) J Immunol , vol.154 , pp. 2226-2236
    • Smith, R.I.1    Coloma, M.J.2    Morrison, S.L.3
  • 19
  • 20
    • 49649106080 scopus 로고    scopus 로고
    • Identification of residues in the Cm4 domain of polymeric IgM essential for interaction with Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1)
    • Ghumra, A. et al. Identification of residues in the Cm4 domain of polymeric IgM essential for interaction with Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1).J Immunol 181, 1988-2000 (2008).
    • (2008) J Immunol , vol.181 , pp. 1988-2000
    • Ghumra, A.1
  • 21
    • 70349284531 scopus 로고    scopus 로고
    • The human IgM pentamer is a mushroom-shaped molecule with a flexural bias
    • Czajkowsky, D. M. & Shao, Z. The human IgM pentamer is a mushroom-shaped molecule with a flexural bias. Proc Natl Acad Sci USA 106, 14960-65 (2009).
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14960-14965
    • Czajkowsky, D.M.1    Shao, Z.2
  • 22
    • 77951156788 scopus 로고    scopus 로고
    • Crossspecies binding analyses of mouse and human neonatal Fc receptor show dramatic differences in IgG and albumin binding
    • 36
    • Andersen, J. T., Daba, M. B., Berntzen, G., Michaelsen, T. E. & Sandlie, I. Crossspecies binding analyses of mouse and human neonatal Fc receptor show dramatic differences in IgG and albumin binding. J Biol Chem 285, 4826-36 (2010).
    • (2010) J Biol Chem , vol.285
    • Andersen, J.T.1    Daba, M.B.2    Berntzen, G.3    Michaelsen, T.E.4    Sandlie, I.5
  • 23
    • 0032031481 scopus 로고    scopus 로고
    • A vaccine for schistosomiasis: Alternative approaches
    • DOI 10.1016/S0169-4758(97)01204-0
    • Doenhoff, M. J. A vaccine for schistosomiasis: alternative approaches. Trends Parasitol 14, 105-9 (1998). (Pubitemid 28101507)
    • (1998) Parasitology Today , vol.14 , Issue.3 , pp. 105-109
    • Doenhoff, M.J.1
  • 24
    • 0022611355 scopus 로고
    • Localisation of the monocyte-binding region on human immunoglobulin G
    • DOI 10.1016/0161-5890(86)90059-3
    • Woof, J. M., Partridge, L. J., Jefferis, R. & Burton, D. R. Localization of the monocyte-binding region on human immunoglobulin G. Mol Immunol 23, 319-30 (1986). (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
  • 25
    • 1142298744 scopus 로고    scopus 로고
    • Human antibody-Fc receptor interactions illuminated by crystal structures
    • Woof, J. M. & Burton, D. R. Human Ab-Fc receptor interactions illuminated by crystal structures. Nat Rev Immunol 4, 89-99 (2004). (Pubitemid 38209203)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.2 , pp. 89-99
    • Woof, J.M.1    Burton, D.R.2
  • 26
    • 65549114676 scopus 로고    scopus 로고
    • Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses
    • Bruhns, P. et al. Specificity and affinity of human Fcgamma receptors and their polymorphic variants for human IgG subclasses. Blood 113, 3716-25 (2009).
    • (2009) Blood , vol.113 , pp. 3716-3725
    • Bruhns, P.1
  • 28
    • 27144550160 scopus 로고    scopus 로고
    • Arming antibodies: Prospects and challenges for immunoconjugates
    • DOI 10.1038/nbt1141, PII N1141
    • Wu, A. M. & Senter, P. D. Arming Abs: prospects and challenges for immunoconjugates. Nat Biotech 23, 1137-46 (2005). (Pubitemid 41486395)
    • (2005) Nature Biotechnology , vol.23 , Issue.9 , pp. 1137-1146
    • Wu, A.M.1    Senter, P.D.2
  • 29
    • 33645341439 scopus 로고    scopus 로고
    • Use of intravenous immunoglobulin in human disease: A review of eviodence by members of the Primary Immunodeficiency Committee of the American Academy of Allergy, Asthma and Immunology
    • Orange, J. S. et al. Use of intravenous immunoglobulin in human disease: a review of eviodence by members of the Primary Immunodeficiency Committee of the American Academy of Allergy, Asthma and Immunology. J Allergy Clin Immunol 117, S525-53.
    • J Allergy Clin Immunol , vol.117
    • Orange, J.S.1
  • 31
    • 0035910392 scopus 로고    scopus 로고
    • Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor
    • DOI 10.1126/science.291.5503.484
    • Samuelsson, A., Towers, T. L. & Ravetch, J. V. Anti-inflammatory activity of IVIG mediated through the inhibitory Fc receptor. Science 291, 484-6 (2001). (Pubitemid 32097072)
    • (2001) Science , vol.291 , Issue.5503 , pp. 484-486
    • Samuelsson, A.1    Towers, T.L.2    Ravetch, J.V.3
  • 32
    • 33748355349 scopus 로고    scopus 로고
    • Reversal of immune thrombocytopenia in mice by cross-linking human immunoglobulin G with a high-affinity monoclonal antibody
    • DOI 10.1111/j.1365-2141.2006.06245.x
    • Bazin, R. et al. Reversal of immune thrombocytopenia in mice by cross-linking human immunoglobulin G with a high-affinity monoclonal Ab. Br J Haematol 135, 97-100 (2006). (Pubitemid 44337669)
    • (2006) British Journal of Haematology , vol.135 , Issue.1 , pp. 97-100
    • Bazin, R.1    Lemieux, R.2    Tremblay, T.3
  • 34
    • 84859785275 scopus 로고    scopus 로고
    • The inhibitory Fcc receptor is unecessary for IVIG efficacy
    • Leontyev, D. et al. The inhibitory Fcc receptor is unecessary for IVIG efficacy. Nature Preceedings. http://precedings. nature. com/documents/4635/ version/1 (2010)
    • (2010) Nature Preceedings.
    • Leontyev, D.1
  • 35
    • 79953202496 scopus 로고    scopus 로고
    • Intravenous Ig inhibits invariant NKT cell-mediated allergic airway inflammation through FcgRIIIA-dependent mechanisms
    • Araujo, L. M. et al. Intravenous Ig inhibits invariant NKT cell-mediated allergic airway inflammation through FcgRIIIA-dependent mechanisms. J Immunol 186, 3289-93 (2011).
    • (2011) J Immunol , vol.186 , pp. 3289-3293
    • Araujo, L.M.1
  • 36
    • 79952471213 scopus 로고    scopus 로고
    • Effect of IgG interchain disulfide bond cleavage on efficacy of IVIg for immune thrombocytopenic purpura (ITP)
    • Machino, Y. et al. Effect of IgG interchain disulfide bond cleavage on efficacy of IVIg for immune thrombocytopenic purpura (ITP).Clin Exp Immunol. 162, 415-24 (2010).
    • (2010) Clin Exp Immunol , vol.162 , pp. 415-424
    • MacHino, Y.1
  • 37
    • 58149378347 scopus 로고    scopus 로고
    • Identification of a receptor required for the antiinflammatory activity of IVIG
    • Anthony, R. M. et al. Identification of a receptor required for the antiinflammatory activity of IVIG. Proc Natl Acad Sci USA 105, 19571-78 (2008).
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19571-19578
    • Anthony, R.M.1
  • 38
    • 77956566546 scopus 로고    scopus 로고
    • IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes
    • Sé̈te J. F. et al. IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes. Blood 116, 1698-704 (2010).
    • (2010) Blood , vol.116 , pp. 1698-1704
    • Sé̈te, J.F.1
  • 39
    • 79960046406 scopus 로고    scopus 로고
    • Intravenous gammaglobulin suppresses inflammation through a novel TH2 pathway
    • Anthony, R. M., Kobayashi, T., Wermeling, F. & Ravetch, J. V. Intravenous gammaglobulin suppresses inflammation through a novel TH2 pathway. Nature 475, 110-116 (2011).
    • (2011) Nature , vol.475 , pp. 110-116
    • Anthony, R.M.1    Kobayashi, T.2    Wermeling, F.3    Ravetch, J.V.4
  • 40
    • 0025101122 scopus 로고
    • A view of the human idiotypic repertoire. Electron microscopic and immunologic analyses of spontaneous idiotype-anti-idiotype dimers in pooled human IgG
    • Roux, K. H. & Tankersley, D. L. Aview of the human idiotypic repertoire. Electron microscopic and immunologic analyses of spontaneous idiotype-anti-idiotype dimmers in pooled human IgG. J Immunol 144, 1387-95 (1990). (Pubitemid 20072911)
    • (1990) Journal of Immunology , vol.144 , Issue.4 , pp. 1387-1395
    • Roux, K.H.1    Tankersley, D.L.2
  • 42
    • 73949155239 scopus 로고    scopus 로고
    • Human IgG2 Abs against epidermal growth factor receptor effectively trigger Ab-dependent cellular cytotoxicity but, in contrast to IgG1, only by cells of the myeloid lineage
    • Schneider-Merck, T. et al. Human IgG2 Abs against epidermal growth factor receptor effectively trigger Ab-dependent cellular cytotoxicity but, in contrast to IgG1, only by cells of the myeloid lineage. J Immunol 512-20 (2010).
    • (2010) J Immunol , pp. 512-520
    • Schneider-Merck, T.1
  • 43
    • 61849115735 scopus 로고    scopus 로고
    • Circulating non-immune IgG complexes in health and disease
    • Nezlin, R. Circulating non-immune IgG complexes in health and disease. Immunol Lett 122, 141-4 (2009).
    • (2009) Immunol Lett , vol.122 , pp. 141-144
    • Nezlin, R.1
  • 44
    • 28544449847 scopus 로고    scopus 로고
    • Immunology: Divergent immunoglobulin G subclass activity through selective Fc receptor binding
    • DOI 10.1126/science.1118948
    • Nimmerjahn, F. & Ravetch, J. V. Divergent immunoglobulin G subclass activity through selective Fc receptor binding. Science 310, 1510-2 (2005). (Pubitemid 41746349)
    • (2005) Science , vol.310 , Issue.5753 , pp. 1510-1512
    • Nimmerjahn, F.1    Ravetch, J.V.2
  • 45
    • 0031005855 scopus 로고    scopus 로고
    • Cloning, heterologous expression and antigenicity of a schistosome cercarial protease
    • DOI 10.1017/S0031182096008657
    • Price, H. P., Doenhoff, M. J. & Sayers, J. R. Cloning, heterologous expression and Agicity of a schistosome cercarial protease. Parasitology 114, 447-53 (1997). (Pubitemid 27210013)
    • (1997) Parasitology , vol.114 , Issue.5 , pp. 447-453
    • Price, H.P.1    Doenhoff, M.J.2    Sayers, J.R.3
  • 46
    • 34848892100 scopus 로고    scopus 로고
    • The different effector function capabilities of the seven equine IgG subclasses have implications for vaccine strategies
    • DOI 10.1016/j.molimm.2007.06.158, PII S0161589007004208, Theories and Modelling of T Cell Behaviour
    • Lewis, M. J., Wagner, B. & Woof, J. M. The different effector function capabilities of the seven equine IgG subclasses have implications for vaccine strategies. Mol Immunol 45, 818-27 (2008). (Pubitemid 47498575)
    • (2008) Molecular Immunology , vol.45 , Issue.3 , pp. 818-827
    • Lewis, M.J.1    Wagner, B.2    Woof, J.M.3
  • 47
    • 0037449141 scopus 로고    scopus 로고
    • Crystal structure of a Fab complex formed with PfMSP1-19, the C-terminal fragment of merozoite surface protein 1 from Plasmodium falciparum: A malaria vaccine candidate
    • DOI 10.1016/S0022-2836(03)00376-0
    • Pizarro, J. C. et al. Crystal structure of a Fab complex formed with PfMSP1-19, the C-terminal fragment ofmerozoite surface protein 1 from Plasmodium falciparum: a malaria vaccine candidate. J Mol Biol 328, 1091-103 (2003). (Pubitemid 36506876)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.5 , pp. 1091-1103
    • Pizarro, J.C.1    Chitarra, V.2    Verger, D.3    Holm, I.4    Petres, S.5    Dartevelle, S.6    Nato, F.7    Longacre, S.8    Bentley, G.A.9
  • 48
    • 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
    • DOI 10.1021/bi00512a001
    • Deisenhofer, J. 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, 2361-70 (1981). (Pubitemid 11089772)
    • (1981) Biochemistry , vol.20 , Issue.9 , pp. 2361-2370
    • Deisenhofer, J.1
  • 51
    • 0041784950 scopus 로고    scopus 로고
    • All atom empirical potential for molecular modeling and dynamics studies of proteins
    • MacKerell, A. D., et al. All atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102, 3586-616 (1998).
    • (1998) J Phys Chem B , vol.102 , pp. 3586-3616
    • MacKerell, A.D.1
  • 53
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • DOI 10.1002/elps.1150181505
    • Guex, N. & Peitsch, M. C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative modeling. Electrophoresis 18, 2714-23 (1997). (Pubitemid 28059943)
    • (1997) Electrophoresis , vol.18 , Issue.15 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 54
    • 34249703970 scopus 로고    scopus 로고
    • The importance of human FcgammaRI in mediating protection to malaria
    • 3
    • McIntosh, R. S. et al. The importance of human FcgammaRI in mediating protection to malaria. PLoS Pathogens 18;3(5), e72 (2007).
    • (2007) PLoS Pathogens , vol.18 , Issue.5
    • McIntosh, R.S.1
  • 55
    • 0035012654 scopus 로고    scopus 로고
    • Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: Mechanism of pH-dependent binding
    • DOI 10.1016/S1097-2765(01)00230-1
    • Martin, W. L., West, A. P., Gan, L. & Bjorkman, P. J. Crystal structure at 2. 8Aof an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding. Mol Cell 7, 867-77 (2001). (Pubitemid 32436446)
    • (2001) Molecular Cell , vol.7 , Issue.4 , pp. 867-877
    • Martin, W.L.1    West Jr., A.P.2    Gan, L.3    Bjorkman, P.J.4
  • 56
    • 0029644247 scopus 로고
    • Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG
    • Sauer-Eriksson, A. E., Kleywegt, G. J., Uhle, M., & Jones, T. A. Crystal structure of the C2 fragment of streptococcal protein G in complex with the Fc domain of human IgG. Structure 3, 265-78 (1995).
    • (1995) Structure , vol.3 , pp. 265-278
    • Sauer-Eriksson, A.E.1    Kleywegt, G.J.2    Uhle, M.3    Jones, T.A.4
  • 57
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-FcγRIII complex
    • DOI 10.1038/35018508
    • Sondermann, P., Huber, R., Oosthuizen, V., & Jacob, U. The 3. 2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature 406, 267-273 (2000). (Pubitemid 30604397)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthulzen, V.3    Jacob, U.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.