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Volumn 162, Issue 8, 1999, Pages 4663-4670

DNA binding by the VH domain of anti-Z-DNA antibody and its modulation by association of the VL domain

Author keywords

[No Author keywords available]

Indexed keywords

DNA ANTIBODY; IMMUNOGLOBULIN LIGHT CHAIN;

EID: 0033561751     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (17)

References (56)
  • 2
    • 0028096717 scopus 로고
    • Structure-function correlates of autoantibodies to nucleic acids: Lessons from immunochemical, genetic and structural studies
    • Eilat, D., and W. F. Anderson. 1994. Structure-function correlates of autoantibodies to nucleic acids: lessons from immunochemical, genetic and structural studies. Mol. Immunol. 31:1377.
    • (1994) Mol. Immunol. , vol.31 , pp. 1377
    • Eilat, D.1    Anderson, W.F.2
  • 4
    • 0022351071 scopus 로고
    • Murine monoclonal anti-DNA autoantibodies bind to endogenous bacteria
    • Carroll, P., D. Stafford, R. S. Schwartz, and B. D. Stollar. 1985. Murine monoclonal anti-DNA autoantibodies bind to endogenous bacteria. J. Immunol. 135: 1086.
    • (1985) J. Immunol. , vol.135 , pp. 1086
    • Carroll, P.1    Stafford, D.2    Schwartz, R.S.3    Stollar, B.D.4
  • 5
    • 0024559855 scopus 로고
    • A murine nephritogenic monoclonal anti-DNA autoantibody binds directly to mouse laminin, the major non-collagenous protein component of the glomerular basement membrane
    • Sabbaga, J., S. R. P. Line, P. Potocnjak, and M. P. Madaio. 1989. A murine nephritogenic monoclonal anti-DNA autoantibody binds directly to mouse laminin, the major non-collagenous protein component of the glomerular basement membrane. Eur. J. Immunol. 19:137.
    • (1989) Eur. J. Immunol. , vol.19 , pp. 137
    • Sabbaga, J.1    Line, S.R.P.2    Potocnjak, P.3    Madaio, M.P.4
  • 6
    • 0023277281 scopus 로고
    • Murine monoclonal anti-DNA antibodies bind directly to glomerular antigens and form immune deposits
    • Madaio, M. P., J. Carlson, J. Cataldo, A. Ucci, P. Migliorini, and O. Pankewycz. 1987. Murine monoclonal anti-DNA antibodies bind directly to glomerular antigens and form immune deposits. J. Immunol. 138:2883.
    • (1987) J. Immunol. , vol.138 , pp. 2883
    • Madaio, M.P.1    Carlson, J.2    Cataldo, J.3    Ucci, A.4    Migliorini, P.5    Pankewycz, O.6
  • 7
    • 0024506642 scopus 로고
    • Anti-DNA antibodies bind directly to renal antigens and induce kidney dysfunction in the isolated perfused rat kidney
    • Raz, E., M. Brezis, E. Rosenmann, and D. Eilat. 1989. Anti-DNA antibodies bind directly to renal antigens and induce kidney dysfunction in the isolated perfused rat kidney. J. Immunol. 142:3076.
    • (1989) J. Immunol. , vol.142 , pp. 3076
    • Raz, E.1    Brezis, M.2    Rosenmann, E.3    Eilat, D.4
  • 8
    • 0030916550 scopus 로고    scopus 로고
    • Monoclonal anti-DNA antibodies: Structure, specificity, and biology
    • Marion, T. N., M. R. Krishnan, D. D. Desai, N. T. Jou, and D. M. Tillman. 1997. Monoclonal anti-DNA antibodies: structure, specificity, and biology. Methods 11:3.
    • (1997) Methods , vol.11 , pp. 3
    • Marion, T.N.1    Krishnan, M.R.2    Desai, D.D.3    Jou, N.T.4    Tillman, D.M.5
  • 10
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • Padlan, E. A. 1994. Anatomy of the antibody molecule. Mol. Immunol. 31:169.
    • (1994) Mol. Immunol. , vol.31 , pp. 169
    • Padlan, E.A.1
  • 11
    • 0025939121 scopus 로고
    • An autoantibody to single-stranded DNA: Comparison of the three-dimensional structures of the unliganded Fab and a deoxynucleotide-Fab complex
    • Herron, J. N., X. M. He, D. W Ballȧrd, P. R. Blier, P. E. Pace, A. L. M. Bothwell, E. W. Voss, Jr., and A. B. Edmundson. 1991. An autoantibody to single-stranded DNA: comparison of the three-dimensional structures of the unliganded Fab and a deoxynucleotide-Fab complex. Proteins 11:159.
    • (1991) Proteins , vol.11 , pp. 159
    • Herron, J.N.1    He, X.M.2    Ballard, D.W.3    Blier, P.R.4    Pace, P.E.5    Bothwell, A.L.M.6    Voss E.W., Jr.7    Edmundson, A.B.8
  • 12
    • 0028074942 scopus 로고
    • Sequencing and modeling of anti-DNA immunoglobulin Fv domains
    • Barry, M. M., C. D. Mol, W. F. Anderson, and J. S. Lee. 1994. Sequencing and modeling of anti-DNA immunoglobulin Fv domains. J. Biol. Chem. 269:3623.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3623
    • Barry, M.M.1    Mol, C.D.2    Anderson, W.F.3    Lee, J.S.4
  • 13
    • 0026612988 scopus 로고
    • Selection of immunoglobulin variable regions in autoimmunity to DNA
    • Marion, T. N., D. M. Tillman, N.-T. Jou, and R. J. Hill. 1992. Selection of immunoglobulin variable regions in autoimmunity to DNA. Immunol. Rev. 128: 123.
    • (1992) Immunol. Rev. , vol.128 , pp. 123
    • Marion, T.N.1    Tillman, D.M.2    Jou, N.-T.3    Hill, R.J.4
  • 14
    • 0028292951 scopus 로고
    • Genetic and structural evidence for antigen selection of anti-DNA antibodies
    • Radic, M. Z., and M. Weigert. 1994. Genetic and structural evidence for antigen selection of anti-DNA antibodies. Annu. Rev. Immunol. 12:487.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 487
    • Radic, M.Z.1    Weigert, M.2
  • 17
    • 0025200545 scopus 로고
    • Ultraviolet cross-linking of helical oligonucleotides to two monoclonal MRL-1pr/1pr anti-DNA autoantibodies: Variations in H and L chain binding to DNA
    • Jang, Y. J., and B. D. Stollar. 1990. Ultraviolet cross-linking of helical oligonucleotides to two monoclonal MRL-1pr/1pr anti-DNA autoantibodies: variations in H and L chain binding to DNA. J. Immunol. 145:3353.
    • (1990) J. Immunol. , vol.145 , pp. 3353
    • Jang, Y.J.1    Stollar, B.D.2
  • 18
    • 0027315950 scopus 로고
    • Cloning and expression of an autoimmune DNA-binding single chain Fv: Only the heavy chain is required for binding
    • Barry, M. M., and J. S. Lee. 1993. Cloning and expression of an autoimmune DNA-binding single chain Fv: only the heavy chain is required for binding. Mol. Immunol. 30:833.
    • (1993) Mol. Immunol. , vol.30 , pp. 833
    • Barry, M.M.1    Lee, J.S.2
  • 19
    • 0028172241 scopus 로고
    • Isolated VH4 heavy chain variable regions bind DNA: Characterization of a recombinant antibody heavy chain library derived from patient(s) with active SLE
    • Kieber-Emmons, T., J. M. von Feldt, A. P. Godillot, D. McCallus, D. Srikantan, D. B. Weiner, and W. V. Williams. 1994. Isolated VH4 heavy chain variable regions bind DNA: characterization of a recombinant antibody heavy chain library derived from patient(s) with active SLE. Lupus 3:379.
    • (1994) Lupus , vol.3 , pp. 379
    • Kieber-Emmons, T.1    Von Feldt, J.M.2    Godillot, A.P.3    McCallus, D.4    Srikantan, D.5    Weiner, D.B.6    Williams, W.V.7
  • 20
    • 0028917925 scopus 로고
    • Domain interactions and antigen binding of recombinant anti-Z-DNA antibody variable domains: The role of heavy and light chains measured by surface plasmon resonance
    • Polymenis, M., and B. D. Stollar. 1995. Domain interactions and antigen binding of recombinant anti-Z-DNA antibody variable domains: the role of heavy and light chains measured by surface plasmon resonance. J. Immunol. 154:2198.
    • (1995) J. Immunol. , vol.154 , pp. 2198
    • Polymenis, M.1    Stollar, B.D.2
  • 21
    • 0029868522 scopus 로고    scopus 로고
    • Heavy chain dominance in the binding of DNA by a lupus mouse monoclonal autoantibody
    • Jang, Y. J., and B. D. Stollar. 1996. Heavy chain dominance in the binding of DNA by a lupus mouse monoclonal autoantibody. Mol. Immunol. 33:197.
    • (1996) Mol. Immunol. , vol.33 , pp. 197
    • Jang, Y.J.1    Stollar, B.D.2
  • 22
    • 0032146032 scopus 로고    scopus 로고
    • Autoreactivity of human VH domains from cDNA libraries: Analysis with a bacterial expression vector
    • Lecerf, J.-M., Y. Chen, P. Richalet-Sécordel, X. Wang, and B. D. Stollar. 1998. Autoreactivity of human VH domains from cDNA libraries: analysis with a bacterial expression vector. J. Immunol. 161:1274.
    • (1998) J. Immunol. , vol.161 , pp. 1274
    • Lecerf, J.-M.1    Chen, Y.2    Richalet-Sécordel, P.3    Wang, X.4    Stollar, B.D.5
  • 23
    • 0025089408 scopus 로고
    • Characterization of anti-Z-DNA antibody binding sites on Z-DNA by nuclear magnetic resonance spectroscopy
    • Sanford, D. G., and B. D. Stollar. 1990. Characterization of anti-Z-DNA antibody binding sites on Z-DNA by nuclear magnetic resonance spectroscopy. J. Biol. Chem. 265:18608.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18608
    • Sanford, D.G.1    Stollar, B.D.2
  • 24
    • 0027335509 scopus 로고
    • The role of mouse VH10 and VL gene segments in the specific binding of antibody to Z-DNA, analyzed with recombinant single chain Fv molecules
    • Brigido, M. M., M. Polymenis, and B. D. Stollar. 1993. The role of mouse VH10 and VL gene segments in the specific binding of antibody to Z-DNA, analyzed with recombinant single chain Fv molecules. J. Immunol. 150:469.
    • (1993) J. Immunol. , vol.150 , pp. 469
    • Brigido, M.M.1    Polymenis, M.2    Stollar, B.D.3
  • 25
    • 0028232621 scopus 로고
    • Critical binding site amino acids of anti-Z-DNA single chain Fv molecules: The role of heavy and light chain CDR3 and relationship to autoantibody activity
    • Polymenis, M., and B. D. Stollar. 1994. Critical binding site amino acids of anti-Z-DNA single chain Fv molecules: the role of heavy and light chain CDR3 and relationship to autoantibody activity. J. Immunol. 152:5319.
    • (1994) J. Immunol. , vol.152 , pp. 5319
    • Polymenis, M.1    Stollar, B.D.2
  • 26
    • 0029095842 scopus 로고
    • Kinetic analysis of the interactions of recombinant human VpreB and IgV domains
    • Hirabayashi, Y., J.-M. Lecerf, Z. Dong, and B. D. Stollar. 1995. Kinetic analysis of the interactions of recombinant human VpreB and IgV domains. J. Immunol. 155:1218.
    • (1995) J. Immunol. , vol.155 , pp. 1218
    • Hirabayashi, Y.1    Lecerf, J.-M.2    Dong, Z.3    Stollar, B.D.4
  • 27
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F. W. 1991. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219:37.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37
    • Studier, F.W.1
  • 28
    • 0021753953 scopus 로고
    • Bromination stabilizes poly(dG-dC) in the Z-DNA form under low-salt conditions
    • Möller, A., A. Nordheim, S. A. Kozlowski, D. J. Patel, and A. Rich. 1984. Bromination stabilizes poly(dG-dC) in the Z-DNA form under low-salt conditions. Biochemistry 23:54.
    • (1984) Biochemistry , vol.23 , pp. 54
    • Möller, A.1    Nordheim, A.2    Kozlowski, S.A.3    Patel, D.J.4    Rich, A.5
  • 29
    • 0022468296 scopus 로고
    • A rapid ELISA for measurement of antibodies to nucleic acid antigens using UV-treated polystyrene microplates
    • Zouali, M., and B. D. Stollar. 1986. A rapid ELISA for measurement of antibodies to nucleic acid antigens using UV-treated polystyrene microplates. J. Immunol. Methods 90:105.
    • (1986) J. Immunol. Methods , vol.90 , pp. 105
    • Zouali, M.1    Stollar, B.D.2
  • 30
    • 0030250670 scopus 로고    scopus 로고
    • Affinity improvement of single antibody VH domains: Residues in all three hypervariable regions affect antigen binding
    • Davies, J., and L. Riechmann. 1996. Affinity improvement of single antibody VH domains: residues in all three hypervariable regions affect antigen binding. Immunotechnology 2:169.
    • (1996) Immunotechnology , vol.2 , pp. 169
    • Davies, J.1    Riechmann, L.2
  • 31
    • 0030588617 scopus 로고    scopus 로고
    • An endogenous sialoprotein and a bacterial B cell superantigen compete in their VH family-specific binding interactions with human Igs
    • Silverman, G. J., R. Pires, and J. P. Bouvet. 1996. An endogenous sialoprotein and a bacterial B cell superantigen compete in their VH family-specific binding interactions with human Igs. J. Immunol. 157:4496.
    • (1996) J. Immunol. , vol.157 , pp. 4496
    • Silverman, G.J.1    Pires, R.2    Bouvet, J.P.3
  • 32
    • 0028314030 scopus 로고
    • Enhanced in vitro refolding of insulin-like growth factor 1 using a solubilizing fusion partner
    • Samuelsson, E., T. Moks, B. Nilsson, and M. Uhlen. 1994. Enhanced in vitro refolding of insulin-like growth factor 1 using a solubilizing fusion partner. Biochemistry 33:4207.
    • (1994) Biochemistry , vol.33 , pp. 4207
    • Samuelsson, E.1    Moks, T.2    Nilsson, B.3    Uhlen, M.4
  • 33
    • 0029365465 scopus 로고
    • Backbone assignment, secondary structure and protein A binding of an isolated, human antibody VH domain
    • Riechmann, L., and J. Davies. 1995. Backbone assignment, secondary structure and protein A binding of an isolated, human antibody VH domain. J. Biomol. NMR 6:141.
    • (1995) J. Biomol. NMR , vol.6 , pp. 141
    • Riechmann, L.1    Davies, J.2
  • 35
    • 0007814204 scopus 로고
    • Studies on structural units of the g-globulins
    • Edelman, G. M., and M. D. Poulik. 1961. Studies on structural units of the g-globulins. J. Exp. Med. 113:861.
    • (1961) J. Exp. Med. , vol.113 , pp. 861
    • Edelman, G.M.1    Poulik, M.D.2
  • 36
    • 0001303221 scopus 로고
    • Recombination of a mixture of univalent antibody fragments of different specificities
    • Nisonoff, A., and M. M. Rivers. 1961. Recombination of a mixture of univalent antibody fragments of different specificities. Arch. Biochem. Biophys. 93:460.
    • (1961) Arch. Biochem. Biophys. , vol.93 , pp. 460
    • Nisonoff, A.1    Rivers, M.M.2
  • 37
    • 0005734368 scopus 로고
    • Reconstitution of antiphage antibodies from L and H polypeptide chains and the formation of interspecies molecular hybrids
    • Fougereau, M., D. E. Olins, and G. M. Edelman. 1964. Reconstitution of antiphage antibodies from L and H polypeptide chains and the formation of interspecies molecular hybrids. J. Exp. Med 120:349.
    • (1964) J. Exp. Med , vol.120 , pp. 349
    • Fougereau, M.1    Olins, D.E.2    Edelman, G.M.3
  • 38
    • 0001497394 scopus 로고
    • The participation of A and B polypeptide chains in the active sites of antibody molecules
    • Metzger, H., L. Wofsy, and S. J. Singer. 1964. The participation of A and B polypeptide chains in the active sites of antibody molecules. Proc. Natl. Acad. Sci. USA 51:612.
    • (1964) Proc. Natl. Acad. Sci. USA , vol.51 , pp. 612
    • Metzger, H.1    Wofsy, L.2    Singer, S.J.3
  • 39
    • 0345489680 scopus 로고
    • Chemical basis for antibody diversity and specificity
    • Tanford, C. 1968. Chemical basis for antibody diversity and specificity. Accts. Chem. Res. 1:161.
    • (1968) Accts. Chem. Res. , vol.1 , pp. 161
    • Tanford, C.1
  • 40
    • 0013931616 scopus 로고
    • Antibody active sites and immunoglobulin molecules
    • Singer, S. J., and R. F. Doolittle. 1966. Antibody active sites and immunoglobulin molecules. Science 153:13.
    • (1966) Science , vol.153 , pp. 13
    • Singer, S.J.1    Doolittle, R.F.2
  • 41
    • 0001047001 scopus 로고
    • The subunits of purified rabbit antibody
    • Utsumi, S., and F. Karush. 1964. The subunits of purified rabbit antibody. Biochemistry 3:1329.
    • (1964) Biochemistry , vol.3 , pp. 1329
    • Utsumi, S.1    Karush, F.2
  • 43
    • 0024461313 scopus 로고
    • Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli
    • Ward, E. S., D. Gussow, A. D. Griffiths, P. T. Jones, and G. Winter. 1989. Binding activities of a repertoire of single immunoglobulin variable domains secreted from Escherichia coli. Nature 341:544.
    • (1989) Nature , vol.341 , pp. 544
    • Ward, E.S.1    Gussow, D.2    Griffiths, A.D.3    Jones, P.T.4    Winter, G.5
  • 45
  • 46
    • 0027532192 scopus 로고
    • B lymphocytes may escape tolerance by revising their antigen receptors
    • Radic, M. Z., J. Erikson, S. Litwin, and M. Weigert. 1993. B lymphocytes may escape tolerance by revising their antigen receptors. J. Exp. Med. 177:1165.
    • (1993) J. Exp. Med. , vol.177 , pp. 1165
    • Radic, M.Z.1    Erikson, J.2    Litwin, S.3    Weigert, M.4
  • 47
    • 0030947976 scopus 로고    scopus 로고
    • Light chain usage in anti-double-stranded DNA B cell subsets: Role in cell fate determination
    • Spatz, L., V. Saenko, A. Iliev, L. Jones, L. Geskin, and B. Diamond. 1997. Light chain usage in anti-double-stranded DNA B cell subsets: role in cell fate determination. J. Exp. Med. 185:1317.
    • (1997) J. Exp. Med. , vol.185 , pp. 1317
    • Spatz, L.1    Saenko, V.2    Iliev, A.3    Jones, L.4    Geskin, L.5    Diamond, B.6
  • 48
    • 0028931042 scopus 로고
    • Breakdown of B cell tolerance in a mouse model of systemic lupus erythematosus
    • Roark, J. H., C. L. Kuntz, K.-A. Nguyen, A. J. Caton, and J. Erikson. 1995. Breakdown of B cell tolerance in a mouse model of systemic lupus erythematosus. J. Exp. Med. 181:1157.
    • (1995) J. Exp. Med. , vol.181 , pp. 1157
    • Roark, J.H.1    Kuntz, C.L.2    Nguyen, K.-A.3    Caton, A.J.4    Erikson, J.5
  • 49
    • 0020040257 scopus 로고
    • Naturally occurring antibodies against nine common antigens in human sera. I. Detection, isolation and characterization
    • Guilbert, B., G. Dighiero, and S. Avrameas. 1982. Naturally occurring antibodies against nine common antigens in human sera. I. Detection, isolation and characterization. J. Immunol. 128:2779.
    • (1982) J. Immunol. , vol.128 , pp. 2779
    • Guilbert, B.1    Dighiero, G.2    Avrameas, S.3
  • 52
    • 0000025154 scopus 로고
    • The antigenic determinants of denatured DNA reactive with lupus erythematosus serum
    • Stollar, D., L. Levine, H. I. Lehrer, and H. Van Vunakis. 1962. The antigenic determinants of denatured DNA reactive with lupus erythematosus serum. Proc. Natl. Acad. Sci. USA 48:874.
    • (1962) Proc. Natl. Acad. Sci. USA , vol.48 , pp. 874
    • Stollar, D.1    Levine, L.2    Lehrer, H.I.3    Van Vunakis, H.4
  • 53
    • 0015095932 scopus 로고
    • Antibodies to polynucleotides in human sera: Antigenic specificity and relation to disease
    • Koffler, D., R. Carr, V. Agnello, R. Thoburn, and H. G. Kunkel. 1971. Antibodies to polynucleotides in human sera: antigenic specificity and relation to disease. J. Exp. Med. 134:294.
    • (1971) J. Exp. Med. , vol.134 , pp. 294
    • Koffler, D.1    Carr, R.2    Agnello, V.3    Thoburn, R.4    Kunkel, H.G.5
  • 54
    • 0020395777 scopus 로고
    • Specificity of autoimmune monoclonal Fab fragments binding to single-stranded deoxyribonucleic acid
    • Lee, J. S., D. F. Dombroski, and T. R. Mosmann. 1982. Specificity of autoimmune monoclonal Fab fragments binding to single-stranded deoxyribonucleic acid. Biochemistry 21:4940.
    • (1982) Biochemistry , vol.21 , pp. 4940
    • Lee, J.S.1    Dombroski, D.F.2    Mosmann, T.R.3
  • 55
    • 0025794226 scopus 로고
    • Two induced anti-Z-DNA monoclonal antibodies use VH gene segments related to those of anti-DNA autoantibodies
    • Brigido, M. M., and B. D. Stollar. 1991. Two induced anti-Z-DNA monoclonal antibodies use VH gene segments related to those of anti-DNA autoantibodies. J. Immunol. 146:2005.
    • (1991) J. Immunol. , vol.146 , pp. 2005
    • Brigido, M.M.1    Stollar, B.D.2
  • 56
    • 0026611508 scopus 로고
    • Autoimmune VH gene family: PCR-generated murine germline VH10 genes
    • Chao, M., and E. W. Voss, Jr. 1992. Autoimmune VH gene family: PCR-generated murine germline VH10 genes. Mol. Immunol. 29:439.
    • (1992) Mol. Immunol. , vol.29 , pp. 439
    • Chao, M.1    Voss E.W., Jr.2


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