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Volumn 63, Issue 4, 2004, Pages 345-354

Molecular studies of anti-HLA-A2 using light-chain shuffling: A structural model for HLa antibody binding

Author keywords

Anti HLA; Antigen binding site; Light chain shuffling

Indexed keywords

HLA A2 ANTIGEN; HLA ANTIBODY;

EID: 1642482846     PISSN: 00012815     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0001-2815.2004.00194.x     Document Type: Article
Times cited : (3)

References (45)
  • 1
    • 0028989830 scopus 로고
    • The immunoglobulin VH gene, VH4-21, specifically encodes autoanti-red cell antibodies against the I or i antigens
    • Smith G, Spellerberg M, Boulton F, Roelcke D, Stevenson F. The immunoglobulin VH gene, VH4-21, specifically encodes autoanti-red cell antibodies against the I or i antigens. Vox Sang 1995: 68: 231-5.
    • (1995) Vox Sang , vol.68 , pp. 231-235
    • Smith, G.1    Spellerberg, M.2    Boulton, F.3    Roelcke, D.4    Stevenson, F.5
  • 2
    • 0029979577 scopus 로고    scopus 로고
    • The I binding specificity of human VH 4-34 (VH 4-21) encoded antibodies is determined by both VH framework region 1 and complementarity determining region 3
    • Li Y, Spellerberg MB, Stevenson FK, Capra JD, Potter KN. The I binding specificity of human VH 4-34 (VH 4-21) encoded antibodies is determined by both VH framework region 1 and complementarity determining region 3. J Mol Biol 1996: 256: 577-89.
    • (1996) J Mol Biol , vol.256 , pp. 577-589
    • Li, Y.1    Spellerberg, M.B.2    Stevenson, F.K.3    Capra, J.D.4    Potter, K.N.5
  • 3
    • 0026052848 scopus 로고
    • Nucleotide sequence analysis of the V regions of two IgM cold agglutinins. Evidence that the VH4-21 gene segment is responsible for the major cross-reactive idiotype
    • Pascual V, Victor K, Lelsz D et al. Nucleotide sequence analysis of the V regions of two IgM cold agglutinins. Evidence that the VH4-21 gene segment is responsible for the major cross-reactive idiotype. J Immunol 1991: 146: 4385-91.
    • (1991) J Immunol , vol.146 , pp. 4385-4391
    • Pascual, V.1    Victor, K.2    Lelsz, D.3
  • 4
    • 0025871514 scopus 로고
    • Human monoclonal antibodies against blood group antigens preferentially express a VH4-21 variable region gene-associated epitope
    • Thompson KM, Sutherland J, Barden G et al. Human monoclonal antibodies against blood group antigens preferentially express a VH4-21 variable region gene-associated epitope. Scand J Immunol 1991: 34: 509-18.
    • (1991) Scand J Immunol , vol.34 , pp. 509-518
    • Thompson, K.M.1    Sutherland, J.2    Barden, G.3
  • 6
    • 0027053660 scopus 로고
    • Germline variable region gene segment derivation of human monoclonal anti-Rh(D) antibodies. Evidence for affinity maturation by somatic hypermutation and repertoire shift
    • Bye JM, Carter C, Cui Y et al. Germline variable region gene segment derivation of human monoclonal anti-Rh(D) antibodies. Evidence for affinity maturation by somatic hypermutation and repertoire shift. J Clin Invest 1992: 90: 2481-90.
    • (1992) J Clin Invest , vol.90 , pp. 2481-2490
    • Bye, J.M.1    Carter, C.2    Cui, Y.3
  • 7
    • 0024512879 scopus 로고
    • Relationship of variable region genes expressed by a human B cell lymphoma secreting pathologic anti-Pr2 erythrocyte autoantibodies
    • Silberstein LE, Litwin S, Carmack CE. Relationship of variable region genes expressed by a human B cell lymphoma secreting pathologic anti-Pr2 erythrocyte autoantibodies. J Exp Med 1989: 168: 1631-43.
    • (1989) J Exp Med , vol.168 , pp. 1631-1643
    • Silberstein, L.E.1    Litwin, S.2    Carmack, C.E.3
  • 8
    • 0028205271 scopus 로고
    • Expression and characterization of recombinant anti-Rh(D) antibodies on filamentous phage: A model system for isolating human red blood cell antibodies by repertoire cloning
    • Siegel DL, Silberstein LE. Expression and characterization of recombinant anti-Rh(D) antibodies on filamentous phage: a model system for isolating human red blood cell antibodies by repertoire cloning. Blood 1994: 83: 2334-44.
    • (1994) Blood , vol.83 , pp. 2334-2344
    • Siegel, D.L.1    Silberstein, L.E.2
  • 9
    • 0033866336 scopus 로고    scopus 로고
    • V(D)J germline gene repertoire analysis of monoclonal D antibodies and the implications for D epitope specificity
    • Perera WS, Moss MT, Urbaniak SJ. V(D)J germline gene repertoire analysis of monoclonal D antibodies and the implications for D epitope specificity. Transfusion 2000: 40: 846-55.
    • (2000) Transfusion , vol.40 , pp. 846-855
    • Perera, W.S.1    Moss, M.T.2    Urbaniak, S.J.3
  • 10
    • 0031446861 scopus 로고    scopus 로고
    • Cold agglutinin activity is common among human monoclonal IgM Rh system antibodies using the V4-34 heavy chain variable gene segment
    • Thorpe SJ, Boult CE, Stevenson FK et al. Cold agglutinin activity is common among human monoclonal IgM Rh system antibodies using the V4-34 heavy chain variable gene segment Transfusion 1997: 37: 1111-6.
    • (1997) Transfusion , vol.37 , pp. 1111-1116
    • Thorpe, S.J.1    Boult, C.E.2    Stevenson, F.K.3
  • 11
    • 0031939565 scopus 로고    scopus 로고
    • Human monoclonal antibodies encoded by the V4-34 gene segment show cold agglutinin activity and variable multireactivity which correlates with the predicted charge of the heavy-chain variable region
    • Thorpe SJ, Turner CE, Stevenson FK, Spellerberg MB, Thorpe R, Natvig JB. Human monoclonal antibodies encoded by the V4-34 gene segment show cold agglutinin activity and variable multireactivity which correlates with the predicted charge of the heavy-chain variable region. Immunology 1998: 93: 129-36.
    • (1998) Immunology , vol.93 , pp. 129-136
    • Thorpe, S.J.1    Turner, C.E.2    Stevenson, F.K.3    Spellerberg, M.B.4    Thorpe, R.5    Natvig, J.B.6
  • 12
    • 0034053815 scopus 로고    scopus 로고
    • HLA-A, -B and -DR antigen frequencies of the London Cord Blood Bank units differ from those found in established bone marrow donor registries
    • Brown J, Poles A, Brown CJ, Contreras M, Navarrete CV. HLA-A, -B and -DR antigen frequencies of the London Cord Blood Bank units differ from those found in established bone marrow donor registries. Bone Marrow Transplant 2000: 25: 475-81.
    • (2000) Bone Marrow Transplant , vol.25 , pp. 475-481
    • Brown, J.1    Poles, A.2    Brown, C.J.3    Contreras, M.4    Navarrete, C.V.5
  • 13
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 1996: 384: 134-41.
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 14
    • 0029962226 scopus 로고    scopus 로고
    • A recombinant antibody with the antigen-specific, major histocompatibility complex-restricted specificity of T cells
    • Andersen PS, Stryhn A, Hansen BE, Fugger L, Engberg J, Buus S. A recombinant antibody with the antigen-specific, major histocompatibility complex-restricted specificity of T cells. Proc Natl Acad Sci USA 1996: 93: 1820-4.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1820-1824
    • Andersen, P.S.1    Stryhn, A.2    Hansen, B.E.3    Fugger, L.4    Engberg, J.5    Buus, S.6
  • 15
    • 0025780265 scopus 로고
    • Immunomodulation of experimental allergic encephalomyelitis by antibodies to the antigen-Ia complex
    • Aharoni R, Teitelbaum D, Arnon R, Puri J. Immunomodulation of experimental allergic encephalomyelitis by antibodies to the antigen-Ia complex. Nature 1991: 351: 147-50.
    • (1991) Nature , vol.351 , pp. 147-150
    • Aharoni, R.1    Teitelbaum, D.2    Arnon, R.3    Puri, J.4
  • 16
    • 0034608939 scopus 로고    scopus 로고
    • Direct selection of a human antibody fragment directed against the tumor T-cell epitope HLA-A1-MAGE-A1 from a nonimmunized phage-Fab library
    • Chames P, Hufton SE, Coulie PG, Uchanska-Ziegler B, Hoogenboom HR. Direct selection of a human antibody fragment directed against the tumor T-cell epitope HLA-A1-MAGE-A1 from a nonimmunized phage-Fab library. Proc Natl Acad Sci USA 2000: 97: 7969-74.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7969-7974
    • Chames, P.1    Hufton, S.E.2    Coulie, P.G.3    Uchanska-Ziegler, B.4    Hoogenboom, H.R.5
  • 17
    • 0037100289 scopus 로고    scopus 로고
    • TCR-like human antibodies expressed on human CTLs mediate antibody affinity-dependent cytolytic activity
    • Chames P, Willemsen RA, Rojas G et al. TCR-like human antibodies expressed on human CTLs mediate antibody affinity-dependent cytolytic activity. J Immunol 2002: 169: 1110-8.
    • (2002) J Immunol , vol.169 , pp. 1110-1118
    • Chames, P.1    Willemsen, R.A.2    Rojas, G.3
  • 18
    • 0034111740 scopus 로고    scopus 로고
    • The isolation and characterisation of human monoclonal HLA-A2 antibodies from an immune V gene phage display library
    • Watkins NA, Brown C, Hurd C, Navarrete C, Ouwehand WH. The isolation and characterisation of human monoclonal HLA-A2 antibodies from an immune V gene phage display library. Tissue Antigens 2000: 55: 219-28.
    • (2000) Tissue Antigens , vol.55 , pp. 219-228
    • Watkins, N.A.1    Brown, C.2    Hurd, C.3    Navarrete, C.4    Ouwehand, W.H.5
  • 19
    • 0016804680 scopus 로고
    • The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-A resolution
    • Epp O, Lattman EE, Schiffer M, Huber R, Palm W. The molecular structure of a dimer composed of the variable portions of the Bence-Jones protein REI refined at 2.0-A resolution. Biochemistry 1975: 14: 4943-52.
    • (1975) Biochemistry , vol.14 , pp. 4943-4952
    • Epp, O.1    Lattman, E.E.2    Schiffer, M.3    Huber, R.4    Palm, W.5
  • 20
    • 0026468883 scopus 로고
    • Three-dimensional structure of an Fv from a human IgM immunoglobulin
    • Fan ZC, Shan L, Guddat LW et al. Three-dimensional structure of an Fv from a human IgM immunoglobulin. J Mol Biol 1992: 228: 188-207.
    • (1992) J Mol Biol , vol.228 , pp. 188-207
    • Fan, Z.C.1    Shan, L.2    Guddat, L.W.3
  • 21
    • 0033527584 scopus 로고    scopus 로고
    • Selection and analysis of an optimized anti-VEGF antibody: Crystal structure of an affinity-matured Fab in complex with antigen
    • Chen Y, Wiesmann C, Fuh G et al. Selection and analysis of an optimized anti-VEGF antibody: crystal structure of an affinity-matured Fab in complex with antigen. J Mol Biol 1999: 293: 865-31.
    • (1999) J Mol Biol , vol.293 , pp. 865-931
    • Chen, Y.1    Wiesmann, C.2    Fuh, G.3
  • 22
    • 0032530717 scopus 로고    scopus 로고
    • VEGF and the Fab fragment of a humanized neutralizing antibody: Crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface
    • Muller YA, Chen Y, Christinger HW et al. VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface. Structure 1998: 6: 1153-67.
    • (1998) Structure , vol.6 , pp. 1153-1167
    • Muller, Y.A.1    Chen, Y.2    Christinger, H.W.3
  • 23
    • 0033557435 scopus 로고    scopus 로고
    • The structure of an entire noncovalent immunoglobulin kappa light-chain dimer (Bence-Jones protein) reveals a weak and unusual constant domains association
    • Roussel A, Spinelli S, Deret S, Navaza J, Aucouturier P, Cambillau C. The structure of an entire noncovalent immunoglobulin kappa light-chain dimer (Bence-Jones protein) reveals a weak and unusual constant domains association. Eur J Biochem 1999: 260: 192-9.
    • (1999) Eur J Biochem , vol.260 , pp. 192-199
    • Roussel, A.1    Spinelli, S.2    Deret, S.3    Navaza, J.4    Aucouturier, P.5    Cambillau, C.6
  • 24
    • 0032988302 scopus 로고    scopus 로고
    • 1.7 A structure of the stabilized REIv mutant T39K. Application local NCS restraints
    • Uson I, Pohl E, Schneider TR et al. 1.7 A structure of the stabilized REIv mutant T39K. Application local NCS restraints. Acta Crystallogr D Biol Crystallogr 1999: 55: 1158-67.
    • (1999) Acta Crystallogr D Biol Crystallogr , vol.55 , pp. 1158-1167
    • Uson, I.1    Pohl, E.2    Schneider, T.R.3
  • 25
    • 0030931534 scopus 로고    scopus 로고
    • Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors
    • Fan QR, Mosyak L, Winter CC, Wagtmann N, Long EO, Wiley DC. Structure of the inhibitory receptor for human natural killer cells resembles haematopoietic receptors. Nature 1997: 389: 96-100.
    • (1997) Nature , vol.389 , pp. 96-100
    • Fan, Q.R.1    Mosyak, L.2    Winter, C.C.3    Wagtmann, N.4    Long, E.O.5    Wiley, D.C.6
  • 26
    • 0033616715 scopus 로고    scopus 로고
    • Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2
    • Snyder GA, Brooks AG, Sun PD. Crystal structure of the HLA-Cw3 allotype-specific killer cell inhibitory receptor KIR2DL2. Proc Natl Acad Sci USA 1999: 96: 3864-9.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3864-3869
    • Snyder, G.A.1    Brooks, A.G.2    Sun, P.D.3
  • 27
    • 0028886129 scopus 로고
    • A human monoclonal antibody specific for the leucine-33 (P1A1, HPA-1a) form of platelet glycoprotein IIIa from a V gene phage display library
    • Griffin HM, Ouwehand WH. A human monoclonal antibody specific for the leucine-33 (P1A1, HPA-1a) form of platelet glycoprotein IIIa from a V gene phage display library. Blood 1995: 86: 4430-6.
    • (1995) Blood , vol.86 , pp. 4430-4436
    • Griffin, H.M.1    Ouwehand, W.H.2
  • 28
    • 0029989324 scopus 로고    scopus 로고
    • Isolation of high-affinity monomeric human anti-c-erbB-2 single chain Fv using affinity-driven selection
    • Schier R, Bye J, Apell G et al. Isolation of high-affinity monomeric human anti-c-erbB-2 single chain Fv using affinity-driven selection. J Mol Biol 1996: 255: 28-43.
    • (1996) J Mol Biol , vol.255 , pp. 28-43
    • Schier, R.1    Bye, J.2    Apell, G.3
  • 30
    • 0027175018 scopus 로고
    • Combinatorial infection and in vivo recombination: A strategy for making large phage antibody repertoires
    • Waterhouse P, Griffiths AD, Johnson KS, Winter G. Combinatorial infection and in vivo recombination: a strategy for making large phage antibody repertoires. Nucleic Acids Res 1993: 21: 2265-6.
    • (1993) Nucleic Acids Res , vol.21 , pp. 2265-2266
    • Waterhouse, P.1    Griffiths, A.D.2    Johnson, K.S.3    Winter, G.4
  • 31
    • 0028986982 scopus 로고
    • The human immunoglobulin VH repertoire
    • Cook GP, Tomlinson IM. The human immunoglobulin VH repertoire. Immunol Today 1995: 16: 237-42.
    • (1995) Immunol Today , vol.16 , pp. 237-242
    • Cook, G.P.1    Tomlinson, I.M.2
  • 32
    • 0029618012 scopus 로고
    • Phototyping: Comprehensive DNA typing for HLA-A, B, C, DRB1, DRB3, DRB4, DRB5 & DQB1 by PCR with 144 primer mixes utilizing sequence-specific primers (PCR-SSP)
    • Bunce M, O'Neill CM, Barnardo MC et al. Phototyping: comprehensive DNA typing for HLA-A, B, C, DRB1, DRB3, DRB4, DRB5 & DQB1 by PCR with 144 primer mixes utilizing sequence-specific primers (PCR-SSP). Tissue Antigens 1995: 46: 355-67.
    • (1995) Tissue Antigens , vol.46 , pp. 355-367
    • Bunce, M.1    O'Neill, C.M.2    Barnardo, M.C.3
  • 33
    • 0036008497 scopus 로고    scopus 로고
    • Platelet alphaIIbbeta3 recombinant autoantibodies from the B-cell repertoire of a post-transfusion purpura patient
    • Watkins NA, Smethurst PA, Allen D, Smith GA, Ouwehand WH. Platelet alphaIIbbeta3 recombinant autoantibodies from the B-cell repertoire of a post-transfusion purpura patient. Br J Haematol 2002: 116: 677-85.
    • (2002) Br J Haematol , vol.116 , pp. 677-685
    • Watkins, N.A.1    Smethurst, P.A.2    Allen, D.3    Smith, G.A.4    Ouwehand, W.H.5
  • 34
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL. Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol 1993: 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 35
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994: 22: 4673-80.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 36
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991: 11: 281-96.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 37
    • 0020523712 scopus 로고
    • A simple method for ranking the affinities of monoclonal antibodies
    • Van Heyningen V, Brock DJ, Van Heyningen S. A simple method for ranking the affinities of monoclonal antibodies. J Immunol Methods 1983: 62: 147-53.
    • (1983) J Immunol Methods , vol.62 , pp. 147-153
    • Van Heyningen, V.1    Brock, D.J.2    Van Heyningen, S.3
  • 39
    • 0033593356 scopus 로고    scopus 로고
    • Analysis of heavy and light chain pairings indicates that receptor editing shapes the human antibody repertoire
    • de Wildt RM, Hoet RM, van Venrooij WJ, Tomlinson IM, Winter G. Analysis of heavy and light chain pairings indicates that receptor editing shapes the human antibody repertoire. J Mol Biol 1999: 285: 895-901.
    • (1999) J Mol Biol , vol.285 , pp. 895-901
    • De Wildt, R.M.1    Hoet, R.M.2    Van Venrooij, W.J.3    Tomlinson, I.M.4    Winter, G.5
  • 40
    • 0033567978 scopus 로고    scopus 로고
    • The importance of the light chain for the epitope specificity of human anti-U1 small nuclear RNA autoantibodies present in systemic lupus erythematosus patients
    • Hoet RM, Pieffers M, Stassen MH et al. The importance of the light chain for the epitope specificity of human anti-U1 small nuclear RNA autoantibodies present in systemic lupus erythematosus patients. J Immunol 1999: 163: 3304-12.
    • (1999) J Immunol , vol.163 , pp. 3304-3312
    • Hoet, R.M.1    Pieffers, M.2    Stassen, M.H.3
  • 41
    • 0029981792 scopus 로고    scopus 로고
    • Light chain shuffling of a high affinity antibody results in a drift in epitope recognition
    • Ohlin M, Owman H, Mach M, Borrebaeck CA. Light chain shuffling of a high affinity antibody results in a drift in epitope recognition. Mol Immunol 1996: 33: 47-56.
    • (1996) Mol Immunol , vol.33 , pp. 47-56
    • Ohlin, M.1    Owman, H.2    Mach, M.3    Borrebaeck, C.A.4
  • 42
    • 0029059812 scopus 로고
    • Light chain contribution to specificity in anti-DNA antibodies
    • Ibrahim SM, Weigert M, Basu C, Erikson J, Radic MZ. Light chain contribution to specificity in anti-DNA antibodies. J Immunol 1995: 155: 3223-33.
    • (1995) J Immunol , vol.155 , pp. 3223-3233
    • Ibrahim, S.M.1    Weigert, M.2    Basu, C.3    Erikson, J.4    Radic, M.Z.5
  • 43
    • 0027227926 scopus 로고
    • Modeling study of antibody combining sites to (alpha 1-6) dextrans. Predictions of the conformational contribution of VL-CDR3 and J kappa segments to groove-type combining sites
    • Wang D, Hubbard JM, Rabat EA. Modeling study of antibody combining sites to (alpha 1-6) dextrans. Predictions of the conformational contribution of VL-CDR3 and J kappa segments to groove-type combining sites. J Biol Chem 1993: 268: 20584-9.
    • (1993) J Biol Chem , vol.268 , pp. 20584-20589
    • Wang, D.1    Hubbard, J.M.2    Rabat, E.A.3
  • 44
    • 0034213423 scopus 로고    scopus 로고
    • Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand
    • Boyington JC, Motyka SA, Schuck P, Brooks AG, Sun PD. Crystal structure of an NK cell immunoglobulin-like receptor in complex with its class I MHC ligand. Nature 2000: 405: 537-43.
    • (2000) Nature , vol.405 , pp. 537-543
    • Boyington, J.C.1    Motyka, S.A.2    Schuck, P.3    Brooks, A.G.4    Sun, P.D.5
  • 45
    • 0032810008 scopus 로고    scopus 로고
    • Recombinant human IgG molecules lacking Fcgamma receptor I binding and monocyte triggering activities
    • Armour KL, Clark MR, Hadley AG, Williamson LM. Recombinant human IgG molecules lacking Fcgamma receptor I binding and monocyte triggering activities. Eur J Immunol 1999: 29: 2613-24.
    • (1999) Eur J Immunol , vol.29 , pp. 2613-2624
    • Armour, K.L.1    Clark, M.R.2    Hadley, A.G.3    Williamson, L.M.4


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