메뉴 건너뛰기




Volumn 159, Issue 10, 1997, Pages 4887-4897

Naturally Occurring A Pocket Polymorphism in HLA-B*2703 Increases the Dependence on an Accessory Anchor Residue at P1 for Optimal Binding of Nonamer Peptides

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; EPITOPE; HLA B ANTIGEN; OLIGOPEPTIDE; VIRUS ANTIGEN;

EID: 0031573143     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (22)

References (55)
  • 1
    • 0023950270 scopus 로고
    • Molecular analysis of the variant alloantigen HLA-B27d (HLA-B*2703) identifies a unique single amino acid substitution
    • Choo, S. Y., T. St. John, H. T. Orr, and J. A. Hansen. 1988. Molecular analysis of the variant alloantigen HLA-B27d (HLA-B*2703) identifies a unique single amino acid substitution. Hum. Immunol. 2:209.
    • (1988) Hum. Immunol. , vol.2 , pp. 209
    • Choo, S.Y.1    St. John, T.2    Orr, H.T.3    Hansen, J.A.4
  • 2
    • 0029091874 scopus 로고
    • HLA-B27 and its subtypes in world populations: Editorial reviews
    • Khan, M. A. 1995. HLA-B27 and its subtypes in world populations: editorial reviews. Curr. Opin. Rheumatol. 7:263.
    • (1995) Curr. Opin. Rheumatol. , vol.7 , pp. 263
    • Khan, M.A.1
  • 3
    • 0026794581 scopus 로고
    • The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
    • Madden, D. R., J. C. Gorga, J. L. Strominger, and D. C. Wiley. 1992. The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC. Cell 70:1035.
    • (1992) Cell , vol.70 , pp. 1035
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 4
    • 0026673724 scopus 로고
    • Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb
    • Fremont, D. H., M. Matsumara, E. A. Stura, P. A. Peterson, and I. A. Wilson. 1992. Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb. Science 257:919.
    • (1992) Science , vol.257 , pp. 919
    • Fremont, D.H.1    Matsumara, M.2    Stura, E.A.3    Peterson, P.A.4    Wilson, I.A.5
  • 5
    • 0026728457 scopus 로고
    • Emerging principles for the recognition of peptide antigens by MHC class I molecules
    • Matsumara, M., D. H. Fremont, P. A. Peterson, and I. A. Wilson. 1992. Emerging principles for the recognition of peptide antigens by MHC class I molecules. Science 257:927.
    • (1992) Science , vol.257 , pp. 927
    • Matsumara, M.1    Fremont, D.H.2    Peterson, P.A.3    Wilson, I.A.4
  • 6
    • 0027525106 scopus 로고
    • The antigenic identity of peptide-MHC complexes: A comparison of the conformations of five viral peptides presented by HLA-A2
    • Madden, D. R., D. N. Garboczi, and D. C. Wiley. 1993. The antigenic identity of peptide-MHC complexes: a comparison of the conformations of five viral peptides presented by HLA-A2. Cell 75:693.
    • (1993) Cell , vol.75 , pp. 693
    • Madden, D.R.1    Garboczi, D.N.2    Wiley, D.C.3
  • 7
    • 0027974989 scopus 로고
    • The three-dimensional structure of H-2Db at 2.4 Å resolution: Implications for antigen-determinant selection
    • Young, A. C. M., W. Zhang, J. C. Sacchettini, and S. G. Nathenson. 1994. The three-dimensional structure of H-2Db at 2.4 Å resolution: implications for antigen-determinant selection. Cell 76:39.
    • (1994) Cell , vol.76 , pp. 39
    • Young, A.C.M.1    Zhang, W.2    Sacchettini, J.C.3    Nathenson, S.G.4
  • 8
    • 0029965954 scopus 로고    scopus 로고
    • An altered position of the α2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501
    • Smith, K. J., S. W. Reid, D. I. Stuart, A. J. McMichael, E. Y. Jones, and J. I. Bell. 1996. An altered position of the α2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501. Immunity 4:203.
    • (1996) Immunity , vol.4 , pp. 203
    • Smith, K.J.1    Reid, S.W.2    Stuart, D.I.3    McMichael, A.J.4    Jones, E.Y.5    Bell, J.I.6
  • 9
    • 0029969665 scopus 로고    scopus 로고
    • Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53
    • Smith, K. J., S. W. Reid, K. Harlos, A. J. McMichael, D. I. Stuart, J. I. Bell, and E. Y. Jones. 1996. Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53. Immunity 4:215.
    • (1996) Immunity , vol.4 , pp. 215
    • Smith, K.J.1    Reid, S.W.2    Harlos, K.3    McMichael, A.J.4    Stuart, D.I.5    Bell, J.I.6    Jones, E.Y.7
  • 10
    • 0026641803 scopus 로고
    • A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells
    • Latron, F., L. Pazmany, J. Morrison, R. Moots, M. A. Saper, A. McMichael, and J. L. Strominger. 1992. A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells. Science 257:964.
    • (1992) Science , vol.257 , pp. 964
    • Latron, F.1    Pazmany, L.2    Morrison, J.3    Moots, R.4    Saper, M.A.5    McMichael, A.6    Strominger, J.L.7
  • 11
    • 0028426881 scopus 로고
    • Differences in peptide presentation between B27 subtypes: The importance of the P1 side chain in maintaining high affinity peptide binding to B*2703
    • Colbert, R. A., S. L. Rowland-Jones, A. J. McMichael, and J. A. Frelinger. 1994. Differences in peptide presentation between B27 subtypes: the importance of the P1 side chain in maintaining high affinity peptide binding to B*2703. Immunity 1:121.
    • (1994) Immunity , vol.1 , pp. 121
    • Colbert, R.A.1    Rowland-Jones, S.L.2    McMichael, A.J.3    Frelinger, J.A.4
  • 12
    • 0025324091 scopus 로고
    • Structure, function, and diversity of class I major histocompatibility complex molecules
    • Bjorkman, P. J., and P. Parham. 1990. Structure, function, and diversity of class I major histocompatibility complex molecules. Annu. Rev. Biochem. 59:253.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 253
    • Bjorkman, P.J.1    Parham, P.2
  • 13
    • 0030031623 scopus 로고    scopus 로고
    • Binding of nonamer peptides to three HLA-B51 molecules which differ by a single amino acid substitution in the A-pocket
    • Kikuchi, A., T. Sakaguchi, K. Miwa, Y. Takamiya, H.-G. Rammensee, Y. Kaneko, and M. Takiguchi. 1996. Binding of nonamer peptides to three HLA-B51 molecules which differ by a single amino acid substitution in the A-pocket. Immunogenetics 43:268.
    • (1996) Immunogenetics , vol.43 , pp. 268
    • Kikuchi, A.1    Sakaguchi, T.2    Miwa, K.3    Takamiya, Y.4    Rammensee, H.-G.5    Kaneko, Y.6    Takiguchi, M.7
  • 14
    • 0028199663 scopus 로고
    • Antigen presentation by major histocompatibility complex class I-B molecules
    • Shawar, S. M., J. M. Vyas, J. R. Rodgers, and R. R. Rich. 1994. Antigen presentation by major histocompatibility complex class I-B molecules. Annu. Rev. Immunol. 12:839.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 839
    • Shawar, S.M.1    Vyas, J.M.2    Rodgers, J.R.3    Rich, R.R.4
  • 15
    • 0029091980 scopus 로고
    • Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3
    • Wang, C.-R., A. R. Castano, P. A. Peterson, C. Slaughter, K. Fischer Lindahl, and J. Deisenhofer. 1995. Nonclassical binding of formylated peptide in crystal structure of the MHC class Ib molecule H2-M3. Cell 62:655.
    • (1995) Cell , vol.62 , pp. 655
    • Wang, C.-R.1    Castano, A.R.2    Peterson, P.A.3    Slaughter, C.4    Fischer Lindahl, K.5    Deisenhofer, J.6
  • 16
    • 0025305927 scopus 로고
    • Structural homologies between two HLA B27-restricted peptides suggest residues important for interaction with HLA-B27
    • Huet, S., D. F. Nixon, J. B. Rothbard, A. Townsend, S. A. Ellis, and A. J. McMichael. 1990. Structural homologies between two HLA B27-restricted peptides suggest residues important for interaction with HLA-B27. Int. Immunol. 2:311.
    • (1990) Int. Immunol. , vol.2 , pp. 311
    • Huet, S.1    Nixon, D.F.2    Rothbard, J.B.3    Townsend, A.4    Ellis, S.A.5    McMichael, A.J.6
  • 18
    • 0027261331 scopus 로고
    • Different HLA-B27 subtypes present the same immunodominant Epstein-Barr virus peptide
    • Brooks, J. M., R. J. Murray, W. A. Thomas, M. G. Kurilla, and A. B. Rickinson. 1993. Different HLA-B27 subtypes present the same immunodominant Epstein-Barr virus peptide. J. Exp. Med. 178:879.
    • (1993) J. Exp. Med. , vol.178 , pp. 879
    • Brooks, J.M.1    Murray, R.J.2    Thomas, W.A.3    Kurilla, M.G.4    Rickinson, A.B.5
  • 19
    • 0027526075 scopus 로고
    • Gag-specific cytotoxic T lymphocytes from human immunodeficiency virus type-1 infected individuals: Gag epitopes are clustered in three regions of the p24gag protein
    • Buseyne, F., M. McChesney, F. Porrot, S. Kovarik, B. Guy, and Y. Riviere. 1993. Gag-specific cytotoxic T lymphocytes from human immunodeficiency virus type-1 infected individuals: Gag epitopes are clustered in three regions of the p24gag protein. J. Virol. 67:694.
    • (1993) J. Virol. , vol.67 , pp. 694
    • Buseyne, F.1    McChesney, M.2    Porrot, F.3    Kovarik, S.4    Guy, B.5    Riviere, Y.6
  • 21
    • 0026766950 scopus 로고
    • Role of binding pockets for amino terminal peptide residues in HLA-B27 allorecognition
    • Villadangos, J. A., B. Galocha, D. Lopez, V. Calvo, and J. A. Lopez de Castro. 1992. Role of binding pockets for amino terminal peptide residues in HLA-B27 allorecognition. J. Immunol. 149:505.
    • (1992) J. Immunol. , vol.149 , pp. 505
    • Villadangos, J.A.1    Galocha, B.2    Lopez, D.3    Calvo, V.4    Lopez De Castro, J.A.5
  • 22
    • 0028200021 scopus 로고
    • Clonal analysis of alloreactive T cell responses against the closely related B*2705 and B*2703 subtypes
    • Lopez, D., R. Garcia-Hoyo, and J. A. Lopez de Castro. 1994. Clonal analysis of alloreactive T cell responses against the closely related B*2705 and B*2703 subtypes. J. Immunol. 152:5557.
    • (1994) J. Immunol. , vol.152 , pp. 5557
    • Lopez, D.1    Garcia-Hoyo, R.2    Lopez De Castro, J.A.3
  • 23
    • 0028022913 scopus 로고
    • Structure of HLA-B27-specific T cell epitopes. Antigen presentation in B*2703 is limited to a subset of the antigenic determinants on B*2705
    • Villadangos, J. A., B. Galocha, R. Garcia-Hoyo, D. Lopez, H. Garcia, and J. A. Lopez de Castro. 1994. Structure of HLA-B27-specific T cell epitopes. Antigen presentation in B*2703 is limited to a subset of the antigenic determinants on B*2705. Eur. J. Immunol. 24:2548.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 2548
    • Villadangos, J.A.1    Galocha, B.2    Garcia-Hoyo, R.3    Lopez, D.4    Garcia, H.5    Lopez De Castro, J.A.6
  • 24
    • 0023129169 scopus 로고
    • NK susceptibility varies inversely with target cell class I HLA antigen expression
    • Storkus, W. J., D. N. Howell, R. D. Salter, J. R. Dawson, and P. Cresswell. 1987. NK susceptibility varies inversely with target cell class I HLA antigen expression. J. Immunol. 138:1657.
    • (1987) J. Immunol. , vol.138 , pp. 1657
    • Storkus, W.J.1    Howell, D.N.2    Salter, R.D.3    Dawson, J.R.4    Cresswell, P.5
  • 25
    • 0021952907 scopus 로고
    • Genes regulating HLA class I antigen expression in T-B lymphoblast hybrids
    • Salter, R. D., D. M. Howell, and P. Cresswell. 1985. Genes regulating HLA class I antigen expression in T-B lymphoblast hybrids. Immunogenetics 21:235.
    • (1985) Immunogenetics , vol.21 , pp. 235
    • Salter, R.D.1    Howell, D.M.2    Cresswell, P.3
  • 26
    • 0018154865 scopus 로고
    • Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens - New tools for genetic analysis
    • Barnstable, C. J., W. J. Bodmer, G. Brown, G. Galfre, C. Milstein, A. F. Williams, and A. Zeigler. 1978. Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens - new tools for genetic analysis. Cell 14:9.
    • (1978) Cell , vol.14 , pp. 9
    • Barnstable, C.J.1    Bodmer, W.J.2    Brown, G.3    Galfre, G.4    Milstein, C.5    Williams, A.F.6    Zeigler, A.7
  • 27
    • 0025855156 scopus 로고
    • Allele-specific motifs revealed by sequencing self peptides eluted from MHC molecules
    • Falk, K., O. Rotzschke, S. Stevanovic, G. Jung, and H.-G. Rammensee. 1991. Allele-specific motifs revealed by sequencing self peptides eluted from MHC molecules. Nature 351:290.
    • (1991) Nature , vol.351 , pp. 290
    • Falk, K.1    Rotzschke, O.2    Stevanovic, S.3    Jung, G.4    Rammensee, H.-G.5
  • 28
    • 0027399839 scopus 로고
    • A method to quantitate binding of unlabeled peptides to class I MHC molecules and detect their allele specificity
    • Elvin, J., C. Potter, T. Elliott, V. Cerundolo, and A. Townsend. 1993. A method to quantitate binding of unlabeled peptides to class I MHC molecules and detect their allele specificity. J. Immunol. Methods 158:161.
    • (1993) J. Immunol. Methods , vol.158 , pp. 161
    • Elvin, J.1    Potter, C.2    Elliott, T.3    Cerundolo, V.4    Townsend, A.5
  • 29
    • 0028341891 scopus 로고
    • Pocket mutations of HLA-B27 show that anchor residues act cumulatively to stabilize peptide binding
    • Parker, K. C., W. E. Biddison, and J. E. Coligan. 1994. Pocket mutations of HLA-B27 show that anchor residues act cumulatively to stabilize peptide binding. Biochemistry 33:7736.
    • (1994) Biochemistry , vol.33 , pp. 7736
    • Parker, K.C.1    Biddison, W.E.2    Coligan, J.E.3
  • 30
  • 31
    • 0025873357 scopus 로고
    • The binding affinity and dissociation rates of peptides for class I major histocompatibility complex molecules
    • Cerundolo, V., T. Elliott, J. Elvin, J. Bastin, H.-G. Rammensee, and A. Townsend. 1991. The binding affinity and dissociation rates of peptides for class I major histocompatibility complex molecules. Eur. J. Immunol. 21:2069.
    • (1991) Eur. J. Immunol. , vol.21 , pp. 2069
    • Cerundolo, V.1    Elliott, T.2    Elvin, J.3    Bastin, J.4    Rammensee, H.-G.5    Townsend, A.6
  • 33
    • 0029618012 scopus 로고
    • Phenotyping: Comprehensive DNA typing for HLA-A, B, C, DRB1, DRB3, DRB4, DRB5, & DQB1 by PCR with 144 primer mixes utilizing sequence-specific primers
    • Bunce, M., C. M. O'Neill, M. C. Barnardo, P. Krausa, M. J. Browning, P. J. Morris, and K. I. Welsh. 1995. Phenotyping: comprehensive DNA typing for HLA-A, B, C, DRB1, DRB3, DRB4, DRB5, & DQB1 by PCR with 144 primer mixes utilizing sequence-specific primers. Tissue Antigens 46:355.
    • (1995) Tissue Antigens , vol.46 , pp. 355
    • Bunce, M.1    O'Neill, C.M.2    Barnardo, M.C.3    Krausa, P.4    Browning, M.J.5    Morris, P.J.6    Welsh, K.I.7
  • 34
    • 0023685463 scopus 로고
    • HIV-1 gag-speciftc cytotoxic T lymphocytes defined with recombinant vaccinia virus and synthetic peptides
    • Nixon, D. F., A. R. M. Townsend, J. G. Elvin, C. R. Rizza, J. Gallwey, and A. J. McMichael. 1988. HIV-1 gag-speciftc cytotoxic T lymphocytes defined with recombinant vaccinia virus and synthetic peptides. Nature 336:484.
    • (1988) Nature , vol.336 , pp. 484
    • Nixon, D.F.1    Townsend, A.R.M.2    Elvin, J.G.3    Rizza, C.R.4    Gallwey, J.5    McMichael, A.J.6
  • 37
  • 38
    • 0027304399 scopus 로고
    • Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules
    • Ruppert, J., J. Sidney, E. Celis, R. T. Kubo, H. M. Grey, and A. Sette. 1993. Prominent role of secondary anchor residues in peptide binding to HLA-A2.1 molecules. Cell 74:929.
    • (1993) Cell , vol.74 , pp. 929
    • Ruppert, J.1    Sidney, J.2    Celis, E.3    Kubo, R.T.4    Grey, H.M.5    Sette, A.6
  • 39
    • 0028344533 scopus 로고
    • Structure of peptides associated with class I and class II MHC molecules
    • Engelhard, V. H. 1994. Structure of peptides associated with class I and class II MHC molecules. Annu. Rev. Immunol. 12:181.
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 181
    • Engelhard, V.H.1
  • 43
    • 0029152771 scopus 로고
    • Amino-terminal alteration of the HLA-A*0201-restricted human immunodeficiency virus pol peptide increase complex stability and in vitro immunogenicity
    • Rogue, R. R., J. Eron, J. A. Frelinger, and M. Matsui. 1995. Amino-terminal alteration of the HLA-A*0201-restricted human immunodeficiency virus pol peptide increase complex stability and in vitro immunogenicity. Proc. Natl. Acad. Sci. USA 92:8166.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8166
    • Rogue, R.R.1    Eron, J.2    Frelinger, J.A.3    Matsui, M.4
  • 46
    • 0028052724 scopus 로고
    • Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual side-chains
    • Parker, K., M. A. Bednarek, and J. E. Coligan. 1994. Scheme for ranking potential HLA-A2 binding peptides based on independent binding of individual side-chains. J. Immunol. 152:163.
    • (1994) J. Immunol. , vol.152 , pp. 163
    • Parker, K.1    Bednarek, M.A.2    Coligan, J.E.3
  • 49
    • 0029094240 scopus 로고
    • Modulation of peptide binding by HLA-B27 polymorphism in pockets A and B, and peptide specificity of B*2703
    • Villadangos, J. A., B. Galocha, F. Garcia, J. P. Albar, and J. A. Lopez de Castro. 1995. Modulation of peptide binding by HLA-B27 polymorphism in pockets A and B, and peptide specificity of B*2703. Eur. J. Immunol. 25:2370.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 2370
    • Villadangos, J.A.1    Galocha, B.2    Garcia, F.3    Albar, J.P.4    Lopez De Castro, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.