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Volumn 164, Issue 1, 2000, Pages 329-337

Limited diversity of peptides related to an alloreactive T cell epitope in the HLA-B27-bound peptide repertoire results from restrictions at multiple steps along the processing-loading pathway

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; HLA B27 ANTIGEN;

EID: 0033961477     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.164.1.329     Document Type: Article
Times cited : (38)

References (40)
  • 1
    • 0031568653 scopus 로고    scopus 로고
    • MHC affinity, peptide liberation, T cell repertoire, and immunodominance all contribute to the paucity of MHC class I-restricted peptides recognized by antiviral CTL
    • Deng, Y., J. W. Yewdell, L. C. Eisenlohr, and J. R. Bennink. 1997. MHC affinity, peptide liberation, T cell repertoire, and immunodominance all contribute to the paucity of MHC class I-restricted peptides recognized by antiviral CTL. J. Immunol. 158:1507.
    • (1997) J. Immunol. , vol.158 , pp. 1507
    • Deng, Y.1    Yewdell, J.W.2    Eisenlohr, L.C.3    Bennink, J.R.4
  • 2
    • 0032971227 scopus 로고    scopus 로고
    • Degradation of cell proteins and the generation of MHC class I-presented peptides
    • Rock, K. L., and A. Goldberg. 1999. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17:739.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 739
    • Rock, K.L.1    Goldberg, A.2
  • 3
    • 0033561553 scopus 로고    scopus 로고
    • Specific proteolytic cleavages limit the diversity of the pool of peptides available to MHC class I molecules in living cells
    • Serwold, T., and N. Shastri. 1999. Specific proteolytic cleavages limit the diversity of the pool of peptides available to MHC class I molecules in living cells. J. Immunol. 162:4712.
    • (1999) J. Immunol. , vol.162 , pp. 4712
    • Serwold, T.1    Shastri, N.2
  • 5
    • 0028096715 scopus 로고
    • Trimming of antigenic peptides in an early secretory compartment
    • Snyder, H. L., J. W. Yewdell, and J. R. Bennink. 1994. Trimming of antigenic peptides in an early secretory compartment. J. Exp. Med. 180:2389.
    • (1994) J. Exp. Med. , vol.180 , pp. 2389
    • Snyder, H.L.1    Yewdell, J.W.2    Bennink, J.R.3
  • 6
    • 0027943180 scopus 로고
    • Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling
    • Roelse, J., M. Gromme, F. Momburg, G. Hammerling, and J. Neefjes. 1994. Trimming of TAP-translocated peptides in the endoplasmic reticulum and in the cytosol during recycling. J. Exp. Med. 180:1591
    • (1994) J. Exp. Med. , vol.180 , pp. 1591
    • Roelse, J.1    Gromme, M.2    Momburg, F.3    Hammerling, G.4    Neefjes, J.5
  • 7
    • 0028925556 scopus 로고
    • Processing of major histocompalibility class I-restricted antigens in the endoplasmic reticulum
    • Elliott, T., A. Willis, V. Cerundolo, and A. Townsend. 1995. Processing of major histocompalibility class I-restricted antigens in the endoplasmic reticulum. J. Exp. Med. 181:1481.
    • (1995) J. Exp. Med. , vol.181 , pp. 1481
    • Elliott, T.1    Willis, A.2    Cerundolo, V.3    Townsend, A.4
  • 8
    • 0029965803 scopus 로고    scopus 로고
    • The protease inhibitor. N-acetyl-L-leucyl-L-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum
    • Hughes, E. A., B. Ortmann, M. Surman, and P. Cresswell. 1996. The protease inhibitor. N-acetyl-L-leucyl-L-leucyl-L-norleucinal, decreases the pool of major histocompatibility complex class I-binding peptides and inhibits peptide trimming in the endoplasmic reticulum. J. Exp. Med. 183:1569.
    • (1996) J. Exp. Med. , vol.183 , pp. 1569
    • Hughes, E.A.1    Ortmann, B.2    Surman, M.3    Cresswell, P.4
  • 9
    • 0030886208 scopus 로고    scopus 로고
    • Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide
    • Craiu, A., T. Akopian, A. Goldberg, and K. L. Rock. 1997. Two distinct proteolytic processes in the generation of a major histocompatibility complex class I-presented peptide. Proc. Natl. Acad. Sci. USA 94:10850.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10850
    • Craiu, A.1    Akopian, T.2    Goldberg, A.3    Rock, K.L.4
  • 10
    • 0032563221 scopus 로고    scopus 로고
    • Interferon-gamma can stimulate post-proteasomal trimming of the N-terminus of an antigenic peptide by inducing leucine aminopeptidase
    • Beninga, J., K. L. Rock, and A. L. Goldberg. 1998. Interferon-gamma can stimulate post-proteasomal trimming of the N-terminus of an antigenic peptide by inducing leucine aminopeptidase. J. Biol. Chem. 273:18734.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18734
    • Beninga, J.1    Rock, K.L.2    Goldberg, A.L.3
  • 11
    • 0032555922 scopus 로고    scopus 로고
    • Major histocompalibility complex class I viral antigen processing in the secretory pathway defined by the trans-Golgi network protease furin
    • Gil-Torregrosa, B. C., A. R. Castano, and M. Del Val. 1998. Major histocompalibility complex class I viral antigen processing in the secretory pathway defined by the trans-Golgi network protease furin. J. Exp. Med. 188:1105.
    • (1998) J. Exp. Med. , vol.188 , pp. 1105
    • Gil-Torregrosa, B.C.1    Castano, A.R.2    Del Val, M.3
  • 16
    • 0031895637 scopus 로고    scopus 로고
    • Mechanisms of MHC class I-restricted antigen processing
    • Pamer, E., and P. Cresswell. 1998. Mechanisms of MHC class I-restricted antigen processing. Annu. Rev. Immunol. 16:323.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 323
    • Pamer, E.1    Cresswell, P.2
  • 17
    • 0033001665 scopus 로고    scopus 로고
    • Genes regulating MHC class I processing of antigen
    • Van Endert, P. M. 1999. Genes regulating MHC class I processing of antigen. Curr. Opin. Immunol. 11:82.
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 82
    • Van Endert, P.M.1
  • 18
    • 0032076171 scopus 로고    scopus 로고
    • HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading
    • Peh, C. A., S. R. Burrows, M. Barnden, R. Khanna, P. Cresswell, D. J. Moss, and J. McCluskey. 1998. HLA-B27-restricted antigen presentation in the absence of tapasin reveals polymorphism in mechanisms of HLA class I peptide loading. Immunity 8:531.
    • (1998) Immunity , vol.8 , pp. 531
    • Peh, C.A.1    Burrows, S.R.2    Barnden, M.3    Khanna, R.4    Cresswell, P.5    Moss, D.J.6    McCluskey, J.7
  • 19
    • 0028943275 scopus 로고
    • The three-dimensional structure of peptide-MHC complexes
    • Madden, D. R. 1995. The three-dimensional structure of peptide-MHC complexes. Annu. Rev. Immunol. 13:587.
    • (1995) Annu. Rev. Immunol. , vol.13 , pp. 587
    • Madden, D.R.1
  • 20
    • 0032533487 scopus 로고    scopus 로고
    • The same natural ligand is involved in allorecognition of multiple HLA-B27 subtypes by a single T cell clone: Role of peptide and the MHC molecule in alloreactivity
    • Paradela, A., M. Garcia-Peydro, J. Vazquez, D. Rognan, and J. A. Lopez de Castro. 1998. The same natural ligand is involved in allorecognition of multiple HLA-B27 subtypes by a single T cell clone: role of peptide and the MHC molecule in alloreactivity. J. Immunol. 161:5481.
    • (1998) J. Immunol. , vol.161 , pp. 5481
    • Paradela, A.1    Garcia-Peydro, M.2    Vazquez, J.3    Rognan, D.4    Lopez De Castro, J.A.5
  • 21
    • 0028200021 scopus 로고
    • Clonal analysis of alloreactive T cell responses against the closely related B*2705 and B*2703 subtypes: Implications for HLA-B27 association to spondyloarthropathy
    • 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: implications for HLA-B27 association to spondyloarthropathy. J. Immunol. 152:5557.
    • (1994) J. Immunol. , vol.152 , pp. 5557
    • Lopez, D.1    Garcia Hoyo, R.2    Lopez De Castro, J.A.3
  • 22
    • 0022317963 scopus 로고
    • Host resistance directed selectively against H-2-deficient lymphoma variants. Analysis of the mechanism
    • Ljunggren, H. G., and K. Karre. 1985. Host resistance directed selectively against H-2-deficient lymphoma variants. Analysis of the mechanism. J. Exp. Med. 162: 1745.
    • (1985) J. Exp. Med. , vol.162 , pp. 1745
    • Ljunggren, H.G.1    Karre, K.2
  • 23
    • 0024324442 scopus 로고
    • Association of class I major histocompatibility heavy and light chains induced by viral peptides
    • Townsend, A., C. Ohlen, J. Bastin, H. G. Ljunggren, L. Foster, and K. Karre. 1989. Association of class I major histocompatibility heavy and light chains induced by viral peptides. Nature 340:443.
    • (1989) Nature , vol.340 , pp. 443
    • Townsend, A.1    Ohlen, C.2    Bastin, J.3    Ljunggren, H.G.4    Foster, L.5    Karre, K.6
  • 24
    • 0018154865 scopus 로고
    • Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens: New tools tor genetic analysis
    • Barnstable, C. J., W. F. Bodmer, G, Brown, G. Galfre, C. Milstein, A. F. Williams, and A. Ziegler. 1978. Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens: new tools tor genetic analysis. Cell 14:9
    • (1978) Cell , vol.14 , pp. 9
    • Barnstable, C.J.1    Bodmer, W.F.2    Brown, G.3    Galfre, G.4    Milstein, C.5    Williams, A.F.6    Ziegler, A.7
  • 25
    • 0030475570 scopus 로고    scopus 로고
    • Binding of peptides naturally presented by HLA-B27 to the differentially disease-associated B*2704 and B*2706 subtypes, and to mutants mimicking their polymorphism
    • Galocha, B., J. R. Lamas, J. A. Villadangos, J. P. Albar, and J. A. Lopez de Castro. 1996. Binding of peptides naturally presented by HLA-B27 to the differentially disease-associated B*2704 and B*2706 subtypes, and to mutants mimicking their polymorphism. Tissue Antigens 48:509.
    • (1996) Tissue Antigens , vol.48 , pp. 509
    • Galocha, B.1    Lamas, J.R.2    Villadangos, J.A.3    Albar, J.P.4    Lopez De Castro, J.A.5
  • 26
    • 0020300724 scopus 로고
    • Recognition of HLA-B27 and related antigens by a monoclonal antibody
    • Ellis, S. A., C. Taylor, and A. McMichael. 1982. Recognition of HLA-B27 and related antigens by a monoclonal antibody. Hum. Immunol. 5:-49.
    • (1982) Hum. Immunol. , vol.5 , pp. 49
    • Ellis, S.A.1    Taylor, C.2    McMichael, A.3
  • 27
    • 0032533802 scopus 로고    scopus 로고
    • HLA-B27 subtype polymorphism and CTL epitope choice: Studies with EBV peptides link immunogenicity with stability of the B27:Peptide complex
    • Brooks, J. M., R. A. Colbert, J. P. Mear, A. M. Leese, and A. B. Rickinson. 1998. HLA-B27 subtype polymorphism and CTL epitope choice: studies with EBV peptides link immunogenicity with stability of the B27:peptide complex. J. Immunol. 161:5252.
    • (1998) J. Immunol. , vol.161 , pp. 5252
    • Brooks, J.M.1    Colbert, R.A.2    Mear, J.P.3    Leese, A.M.4    Rickinson, A.B.5
  • 28
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • Rock, K. L., C. Gramm, L. Rothstein, K. Clark, R. Stein, L. Dick, D. Hwang, and A. L. Golderg. 1994, Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78:761.
    • (1994) Cell , vol.78 , pp. 761
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Golderg, A.L.8
  • 29
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee, D. H., and A. L. Goldberg. 1998. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8:397.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397
    • Lee, D.H.1    Goldberg, A.L.2
  • 30
    • 0030926777 scopus 로고    scopus 로고
    • Lactacystin and clasto-lactacystin β-lactone modify multiple proteasome β-subunits and inhibit intracellular proltin degradation and major histocompatibilily complex class I antigen presentation
    • Craiu, A., M. Gaczynska, T. Akopian, C. F. Gramm, G. Fenteany, A. L. Goldberg, and K. L. Rock. 1997. Lactacystin and clasto-lactacystin β-lactone modify multiple proteasome β-subunits and inhibit intracellular proltin degradation and major histocompatibilily complex class I antigen presentation. J. Biol. Chem. 272:13437.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13437
    • Craiu, A.1    Gaczynska, M.2    Akopian, T.3    Gramm, C.F.4    Fenteany, G.5    Goldberg, A.L.6    Rock, K.L.7
  • 31
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and S. L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726.
    • (1995) Science , vol.268 , pp. 726
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 32
    • 18744428952 scopus 로고    scopus 로고
    • Lactacystin, a specific inhibitor of ihe proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme
    • Ostrowska, H., C. Wojcik, S. Omura, and K. Worowski. 1997. Lactacystin, a specific inhibitor of ihe proteasome, inhibits human platelet lysosomal cathepsin A-like enzyme. Biochem. Biophys. Res. Commun. 234:729.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 729
    • Ostrowska, H.1    Wojcik, C.2    Omura, S.3    Worowski, K.4
  • 33
    • 0028287522 scopus 로고
    • Antibodies against the C2 COOH terminal region discriminate the active and latent forms of the multicatalytic proteinase complex
    • Arribas, J. P. Arizti, and J. G. Castano. 1994. Antibodies against the C2 COOH terminal region discriminate the active and latent forms of the multicatalytic proteinase complex. J. Biol. Chem. 269:12858.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12858
    • Arribas, J.1    Arizti, P.2    Castano, J.G.3
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 35
  • 36
    • 0033495770 scopus 로고    scopus 로고
    • Modulation at multiple anchor positions of the peptide specificity of HLA-B27 subtypes differentially associated with ankylosing spondylitis
    • Lamas, J. R., A. Paradela, F. Roncal, and J. A. Lopez de Castro 1999. Modulation at multiple anchor positions of the peptide specificity of HLA-B27 subtypes differentially associated with ankylosing spondylitis. Arthritis Rheum. 42:1975
    • (1999) Arthritis Rheum. , vol.42 , pp. 1975
    • Lamas, J.R.1    Paradela, A.2    Roncal, F.3    Lopez De Castro, J.A.4
  • 38
    • 0026733449 scopus 로고
    • Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size
    • Chicz, R, M., R. G. Urban, W. S. Lane, J. C. Gorga, L. J. Stern, D. A. Vignali. and J. L. Strominger. 1992. Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in size. Nature 358:764.
    • (1992) Nature , vol.358 , pp. 764
    • Chicz, R.M.1    Urban, R.G.2    Lane, W.S.3    Gorga, J.C.4    Stern, L.J.5    Vignali, D.A.6    Strominger, J.L.7


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