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Volumn 45, Issue 5, 2008, Pages 1501-1513

The acquisition of narrow binding specificity by polyspecific natural IgM antibodies in a semi-physiological environment

Author keywords

IgM; Natural antibody; Polyspecificity; T7 phage display

Indexed keywords

DNA; HAPTEN; IMMUNOGLOBULIN M ANTIBODY; MYOSIN; THYROGLOBULIN;

EID: 37449031599     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2007.07.043     Document Type: Article
Times cited : (8)

References (36)
  • 1
    • 0032586674 scopus 로고    scopus 로고
    • Alpha2-macroglobulin: an evolutionarily conserved arm of the innate immune system
    • Armstrong P.B., and Quigley J.P. Alpha2-macroglobulin: an evolutionarily conserved arm of the innate immune system. Dev. Comp. Immunol. 23 (1999) 375-390
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 375-390
    • Armstrong, P.B.1    Quigley, J.P.2
  • 2
    • 0034679710 scopus 로고    scopus 로고
    • B-1 and B-2 cell-derived immunoglobulin M antibodies are nonredundant components of the protective response to influenza virus infection
    • Baumgarth N., Herman O.C., et al. B-1 and B-2 cell-derived immunoglobulin M antibodies are nonredundant components of the protective response to influenza virus infection. J. Exp. Med. 192 (2000) 271-280
    • (2000) J. Exp. Med. , vol.192 , pp. 271-280
    • Baumgarth, N.1    Herman, O.C.2
  • 3
    • 0034936968 scopus 로고    scopus 로고
    • Role of natural and immune IgM antibodies in immune responses
    • Boes M. Role of natural and immune IgM antibodies in immune responses. Mol. Immunol. 37 (2000) 1141-1149
    • (2000) Mol. Immunol. , vol.37 , pp. 1141-1149
    • Boes, M.1
  • 4
    • 0034968088 scopus 로고    scopus 로고
    • Induction of natural autoantibody activity following treatment of human immunoglobulin with dissociating agents
    • Bouvet J.P., Stahl D., et al. Induction of natural autoantibody activity following treatment of human immunoglobulin with dissociating agents. J. Autoimmun. 16 (2001) 163-172
    • (2001) J. Autoimmun. , vol.16 , pp. 163-172
    • Bouvet, J.P.1    Stahl, D.2
  • 6
    • 0026040197 scopus 로고
    • Natural auto- and polyreactive antibodies differing from antigen-induced antibodies in the H chain CDR3
    • Chen C., Stenzel-Poore M.P., et al. Natural auto- and polyreactive antibodies differing from antigen-induced antibodies in the H chain CDR3. J. Immunol. 147 (1991) 2359-2367
    • (1991) J. Immunol. , vol.147 , pp. 2359-2367
    • Chen, C.1    Stenzel-Poore, M.P.2
  • 7
    • 0031567901 scopus 로고    scopus 로고
    • Structural and affinity studies of IgM polyreactive natural autoantibodies
    • Diaw L., Magnac C., et al. Structural and affinity studies of IgM polyreactive natural autoantibodies. J. Immunol. 158 (1997) 968-976
    • (1997) J. Immunol. , vol.158 , pp. 968-976
    • Diaw, L.1    Magnac, C.2
  • 8
    • 0021084192 scopus 로고
    • Murine hybridomas secreting natural monoclonal antibodies reacting with self antigens
    • Dighiero G., Lymberi P., et al. Murine hybridomas secreting natural monoclonal antibodies reacting with self antigens. J. Immunol. 131 (1983) 2267-2272
    • (1983) J. Immunol. , vol.131 , pp. 2267-2272
    • Dighiero, G.1    Lymberi, P.2
  • 9
    • 33644871684 scopus 로고    scopus 로고
    • Ferrous ions and reactive oxygen species increase antigen-binding and anti-inflammatory activities of immunoglobulin G
    • Dimitrov J.D., Ivanovska N.D., et al. Ferrous ions and reactive oxygen species increase antigen-binding and anti-inflammatory activities of immunoglobulin G. J. Biol. Chem. 281 (2006) 439-446
    • (2006) J. Biol. Chem. , vol.281 , pp. 439-446
    • Dimitrov, J.D.1    Ivanovska, N.D.2
  • 10
    • 34548171876 scopus 로고    scopus 로고
    • Transition towards antigen-binding promiscuity of a monospecific antibody
    • Dimitrov J.D., Lacroix-Desmazes S., et al. Transition towards antigen-binding promiscuity of a monospecific antibody. Mol. Immunol. 44 (2007) 1854-1863
    • (2007) Mol. Immunol. , vol.44 , pp. 1854-1863
    • Dimitrov, J.D.1    Lacroix-Desmazes, S.2
  • 11
    • 0032544110 scopus 로고    scopus 로고
    • Targeted gene disruption reveals a role for natural secretory IgM in the maturation of the primary immune response
    • Ehrenstein M.R., O'Keefe T.L., et al. Targeted gene disruption reveals a role for natural secretory IgM in the maturation of the primary immune response. Proc. Nat. Acad. Sci. U.S.A. 95 (1998) 10089-10093
    • (1998) Proc. Nat. Acad. Sci. U.S.A. , vol.95 , pp. 10089-10093
    • Ehrenstein, M.R.1    O'Keefe, T.L.2
  • 12
    • 0034599499 scopus 로고    scopus 로고
    • Deficiency in serum immunoglobulin (Ig)M predisposes to development of IgG autoantibodies
    • Ehrenstein M.R., Cook H.T., et al. Deficiency in serum immunoglobulin (Ig)M predisposes to development of IgG autoantibodies. J. Exp. Med. 191 (2000) 1253-1258
    • (2000) J. Exp. Med. , vol.191 , pp. 1253-1258
    • Ehrenstein, M.R.1    Cook, H.T.2
  • 13
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: obvious but underappreciated
    • Ellis R.J. Macromolecular crowding: obvious but underappreciated. Trends Biochem. Sci. 26 (2001) 597-604
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 14
    • 0018167397 scopus 로고
    • Serum immunoglobulins in aborted and non-aborted bovine foetuses
    • Ellis W.A., Logan E.F., et al. Serum immunoglobulins in aborted and non-aborted bovine foetuses. Clin. Exp. Immunol. 33 (1978) 136-141
    • (1978) Clin. Exp. Immunol. , vol.33 , pp. 136-141
    • Ellis, W.A.1    Logan, E.F.2
  • 15
    • 0027943261 scopus 로고
    • Conformational isomerism and the diversity of antibodies
    • Foote J., and Milstein C. Conformational isomerism and the diversity of antibodies. Proc. Nat. Acad. Sci. U.S.A. 91 (1994) 10370-10374
    • (1994) Proc. Nat. Acad. Sci. U.S.A. , vol.91 , pp. 10370-10374
    • Foote, J.1    Milstein, C.2
  • 16
    • 0020577078 scopus 로고
    • Multiple organ-reactive monoclonal autoantibodies
    • Haspel M.V., Onodera T., et al. Multiple organ-reactive monoclonal autoantibodies. Nature 304 (1983) 73-76
    • (1983) Nature , vol.304 , pp. 73-76
    • Haspel, M.V.1    Onodera, T.2
  • 17
    • 0037470496 scopus 로고    scopus 로고
    • Antibody multispecificity mediated by conformational diversity
    • James L.C., Roversi P., et al. Antibody multispecificity mediated by conformational diversity. Science 299 (2003) 1362-1367
    • (2003) Science , vol.299 , pp. 1362-1367
    • James, L.C.1    Roversi, P.2
  • 18
    • 0037100251 scopus 로고    scopus 로고
    • The primary antibody repertoire represents a linked network of degenerate antigen specificities
    • Manivel V., Bayiroglu F., et al. The primary antibody repertoire represents a linked network of degenerate antigen specificities. J. Immunol. 169 (2002) 888-897
    • (2002) J. Immunol. , vol.169 , pp. 888-897
    • Manivel, V.1    Bayiroglu, F.2
  • 19
    • 7044245628 scopus 로고    scopus 로고
    • The appearance and disappearance of antiphospholipid autoantibodies subsequent to oxidation-reduction reactions
    • McIntyre J.A. The appearance and disappearance of antiphospholipid autoantibodies subsequent to oxidation-reduction reactions. Thromb. Res. 114 (2004) 579-587
    • (2004) Thromb. Res. , vol.114 , pp. 579-587
    • McIntyre, J.A.1
  • 20
    • 0034738752 scopus 로고    scopus 로고
    • Polyreactivity as an acquired artefact, rather than a physiologic property, of antibodies: evidence that monoreactive antibodies may gain the ability to bind to multiple antigens after exposure to low pH
    • McMahon M.J., and O'Kennedy R. Polyreactivity as an acquired artefact, rather than a physiologic property, of antibodies: evidence that monoreactive antibodies may gain the ability to bind to multiple antigens after exposure to low pH. J. Immunol. Methods 241 (2000) 1-10
    • (2000) J. Immunol. Methods , vol.241 , pp. 1-10
    • McMahon, M.J.1    O'Kennedy, R.2
  • 21
    • 0026612499 scopus 로고
    • Affinity chromatographic purification of immunoglobulin M antibodies utilizing immobilized mannan binding protein
    • Nevens J.R., Mallia A.K., et al. Affinity chromatographic purification of immunoglobulin M antibodies utilizing immobilized mannan binding protein. J. Chromatogr. A 597 (1992) 247-256
    • (1992) J. Chromatogr. A , vol.597 , pp. 247-256
    • Nevens, J.R.1    Mallia, A.K.2
  • 22
    • 1642315560 scopus 로고    scopus 로고
    • Polyreactivity of antibody molecules
    • Notkins A.L. Polyreactivity of antibody molecules. Trends Immunol. 25 (2004) 174-179
    • (2004) Trends Immunol. , vol.25 , pp. 174-179
    • Notkins, A.L.1
  • 23
    • 0032787091 scopus 로고    scopus 로고
    • Control of early viral and bacterial distribution and disease by natural antibodies
    • Ochsenbein A.F., Fehr T., et al. Control of early viral and bacterial distribution and disease by natural antibodies. Science 286 (1999) 2156-2159
    • (1999) Science , vol.286 , pp. 2156-2159
    • Ochsenbein, A.F.1    Fehr, T.2
  • 24
    • 0031939933 scopus 로고    scopus 로고
    • Angiotensin II generation at the cell surface of activated neutrophils: novel cathepsin G-mediated catalytic activity that is resistant to inhibition
    • Owen C.A., and Campbell E.J. Angiotensin II generation at the cell surface of activated neutrophils: novel cathepsin G-mediated catalytic activity that is resistant to inhibition. J. Immunol. 160 (1998) 1436-1443
    • (1998) J. Immunol. , vol.160 , pp. 1436-1443
    • Owen, C.A.1    Campbell, E.J.2
  • 25
    • 0026009904 scopus 로고
    • Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modelling. A possible mechanism for complement activation
    • Perkins S.J., Nealis A.S., et al. Solution structure of human and mouse immunoglobulin M by synchrotron X-ray scattering and molecular graphics modelling. A possible mechanism for complement activation. J. Mol. Biol. 221 (1991) 1345-1366
    • (1991) J. Mol. Biol. , vol.221 , pp. 1345-1366
    • Perkins, S.J.1    Nealis, A.S.2
  • 26
    • 0017875779 scopus 로고
    • Binding site of a dextran-specific homogeneous IgM: thermodynamic and spectroscopic mapping by dansylated oligosaccharides
    • Schepers G., Blatt Y., et al. Binding site of a dextran-specific homogeneous IgM: thermodynamic and spectroscopic mapping by dansylated oligosaccharides. Biochemistry 17 (1978) 2239-2245
    • (1978) Biochemistry , vol.17 , pp. 2239-2245
    • Schepers, G.1    Blatt, Y.2
  • 27
    • 0026575008 scopus 로고
    • Caveats for the use of surface-adsorbed protein antigen to test the specificity of antibodies
    • Schwab C., and Bosshard H.R. Caveats for the use of surface-adsorbed protein antigen to test the specificity of antibodies. J. Immunol. Methods 147 (1992) 125-134
    • (1992) J. Immunol. Methods , vol.147 , pp. 125-134
    • Schwab, C.1    Bosshard, H.R.2
  • 28
    • 33746265976 scopus 로고    scopus 로고
    • Mechanism of plasmid delivery by hydrodynamic tail vein injection. I. Hepatocyte uptake of various molecules
    • Sebestyen M.G., Budker V.G., et al. Mechanism of plasmid delivery by hydrodynamic tail vein injection. I. Hepatocyte uptake of various molecules. J. Gene Med. 8 (2006) 852-873
    • (2006) J. Gene Med. , vol.8 , pp. 852-873
    • Sebestyen, M.G.1    Budker, V.G.2
  • 29
    • 0030994404 scopus 로고    scopus 로고
    • Frequent occurrence of identical heavy and light chain Ig rearrangements
    • Seidl K.J., MacKenzie J.D., et al. Frequent occurrence of identical heavy and light chain Ig rearrangements. Int. Immunol. 9 (1997) 689-702
    • (1997) Int. Immunol. , vol.9 , pp. 689-702
    • Seidl, K.J.1    MacKenzie, J.D.2
  • 30
    • 0027999391 scopus 로고
    • The mechanism of autoantibody production in an autoimmune MRL/lpr mouse
    • Shan H., Shlomchik M.J., et al. The mechanism of autoantibody production in an autoimmune MRL/lpr mouse. J. Immunol. 153 (1994) 5104-5120
    • (1994) J. Immunol. , vol.153 , pp. 5104-5120
    • Shan, H.1    Shlomchik, M.J.2
  • 31
    • 0034950895 scopus 로고    scopus 로고
    • Specific recognition of protein carboxy-terminal sequences by natural IgM antibodies in normal serum
    • Sokoloff A.V., Bock I., et al. Specific recognition of protein carboxy-terminal sequences by natural IgM antibodies in normal serum. Mol. Ther. 3 (2001) 821-830
    • (2001) Mol. Ther. , vol.3 , pp. 821-830
    • Sokoloff, A.V.1    Bock, I.2
  • 32
    • 0034242702 scopus 로고    scopus 로고
    • The interactions of peptides with the innate immune system studied with use of T7 phage peptide display
    • Sokoloff A.V., Bock I., et al. The interactions of peptides with the innate immune system studied with use of T7 phage peptide display. Mol. Ther. 2 (2000) 131-139
    • (2000) Mol. Ther. , vol.2 , pp. 131-139
    • Sokoloff, A.V.1    Bock, I.2
  • 33
    • 2542567205 scopus 로고    scopus 로고
    • Sequence-specific binding of normal serum IgM to exposed protein C-termini
    • Sokoloff A.V., Puckett M., et al. Sequence-specific binding of normal serum IgM to exposed protein C-termini. Immunology 112 (2004) 237-249
    • (2004) Immunology , vol.112 , pp. 237-249
    • Sokoloff, A.V.1    Puckett, M.2
  • 34
    • 0028268506 scopus 로고
    • Natural antibody and complement-mediated antigen processing and presentation by B lymphocytes
    • Thornton B.P., Vetvicka V., et al. Natural antibody and complement-mediated antigen processing and presentation by B lymphocytes. J. Immunol. 152 (1994) 1727-1737
    • (1994) J. Immunol. , vol.152 , pp. 1727-1737
    • Thornton, B.P.1    Vetvicka, V.2
  • 35
    • 0036110280 scopus 로고    scopus 로고
    • IgM are associated to Sp alpha (CD5 antigen-like)
    • Tissot J.D., Sanchez J.C., et al. IgM are associated to Sp alpha (CD5 antigen-like). Electrophoresis 23 (2002) 1203-1206
    • (2002) Electrophoresis , vol.23 , pp. 1203-1206
    • Tissot, J.D.1    Sanchez, J.C.2
  • 36
    • 31344460778 scopus 로고    scopus 로고
    • Identification of the target self-antigens in reperfusion injury
    • Zhang M., Alicot E.M., et al. Identification of the target self-antigens in reperfusion injury. J. Exp. Med. 203 (2006) 141-152
    • (2006) J. Exp. Med. , vol.203 , pp. 141-152
    • Zhang, M.1    Alicot, E.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.