메뉴 건너뛰기




Volumn 182, Issue 1, 2009, Pages 446-455

Presentation of cytosolically stable peptides by HLA-B27 is not dependent on the canonic interactions of N-terminal basic residues in the a pocket

Author keywords

[No Author keywords available]

Indexed keywords

HLA B27 ANTIGEN; GLUTAMIC ACID; HLA B 2705 ANTIGEN; HLA B ANTIGEN; HLA-B 2705 ANTIGEN; LIGAND; PEPTIDE FRAGMENT; SERINE; THREONINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 59849128475     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.182.1.446     Document Type: Article
Times cited : (9)

References (44)
  • 3
    • 0025234494 scopus 로고
    • Guilt by association: HLA-B27 and ankylosing spondylitis
    • Benjamin, R., and P. Parham. 1990. Guilt by association: HLA-B27 and ankylosing spondylitis. Immunol. Today 11: 137-142.
    • (1990) Immunol. Today , vol.11 , pp. 137-142
    • Benjamin, R.1    Parham, P.2
  • 4
    • 43849110108 scopus 로고    scopus 로고
    • Peptides: The cornerstone of HLA-B27 biology and pathogenetic role in spondyloarthritis
    • Marcilla, M., and J. A. Lopez de Castro. 2008. Peptides: the cornerstone of HLA-B27 biology and pathogenetic role in spondyloarthritis. Tissue Antigens 71: 495-506.
    • (2008) Tissue Antigens , vol.71 , pp. 495-506
    • Marcilla, M.1    Lopez de Castro, J.A.2
  • 5
    • 0021612264 scopus 로고
    • HLA-B27, a dominant restricting element in antiviral responses?
    • Gomard, E., M. Sitbon, A. Toubert, B. Begue, and J. P. Levy. 1984. HLA-B27, a dominant restricting element in antiviral responses? Immunogenetics 20: 197-204.
    • (1984) Immunogenetics , vol.20 , pp. 197-204
    • Gomard, E.1    Sitbon, M.2    Toubert, A.3    Begue, B.4    Levy, J.P.5
  • 9
    • 43949094512 scopus 로고    scopus 로고
    • Structural and functional constraints limit options for cytotoxic T-lymphocyte escape in the immunodominant HLA-B27-restricted epitope in human immunodeficiency virus type 1 capsid
    • Schneidewind, A., M. A. Brockman, J. Sidney, Y. E. Wang, H. Chen, T. J. Suscovich, B. Li, R. I. Adam, R. L. Allgaier, B. R. Mothe, et al. 2008. Structural and functional constraints limit options for cytotoxic T-lymphocyte escape in the immunodominant HLA-B27-restricted epitope in human immunodeficiency virus type 1 capsid. J. Virol. 82: 5594-5605.
    • (2008) J. Virol , vol.82 , pp. 5594-5605
    • Schneidewind, A.1    Brockman, M.A.2    Sidney, J.3    Wang, Y.E.4    Chen, H.5    Suscovich, T.J.6    Li, B.7    Adam, R.I.8    Allgaier, R.L.9    Mothe, B.R.10
  • 13
    • 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: 1035-1048.
    • (1992) Cell , vol.70 , pp. 1035-1048
    • Madden, D.R.1    Gorga, J.C.2    Strominger, J.L.3    Wiley, D.C.4
  • 14
    • 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: 2370-2377.
    • (1995) Eur. J. Immunol , vol.25 , pp. 2370-2377
    • Villadangos, J.A.1    Galocha, B.2    Garcia, F.3    Albar, J.P.4    Lopez de Castro, J.A.5
  • 15
    • 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: 1975-1985.
    • (1999) Arthritis Rheum , vol.42 , pp. 1975-1985
    • Lamas, J.R.1    Paradela, A.2    Roncal, F.3    Lopez de Castro, J.A.4
  • 17
    • 33644547347 scopus 로고    scopus 로고
    • Cutting edge: HLA-B27 acquires many N-terminal dibasic peptides: coupling cytosolic peptide stability to antigen presentation
    • Herberts, C. A., J. J. Neijssen, J. de Haan, L. Janssen, J. W. Drijfhout, E. A. Reits, and J. J. Neefjes. 2006. Cutting edge: HLA-B27 acquires many N-terminal dibasic peptides: coupling cytosolic peptide stability to antigen presentation. J. Immunol. 176: 2697-2701.
    • (2006) J. Immunol , vol.176 , pp. 2697-2701
    • Herberts, C.A.1    Neijssen, J.J.2    de Haan, J.3    Janssen, L.4    Drijfhout, J.W.5    Reits, E.A.6    Neefjes, J.J.7
  • 18
    • 0026521967 scopus 로고
    • The HLA-A,B "negative" mutant cell line C1R expresses a novel HLA-B35 allele, which also has a point mutation in the translation initiation codon
    • Zemmour, J., A. M. Little, D. J. Schendel, and P. Parham. 1992. The HLA-A,B "negative" mutant cell line C1R expresses a novel HLA-B35 allele, which also has a point mutation in the translation initiation codon. J. Immunol. 148: 1941-1948.
    • (1992) J. Immunol , vol.148 , pp. 1941-1948
    • Zemmour, J.1    Little, A.M.2    Schendel, D.J.3    Parham, P.4
  • 19
    • 0025335830 scopus 로고
    • Structure and diversity of HLA-B27-specific T cell epitopes: Analysis with site-directed mutants mimicking HLA-B27 subtype polymorphism
    • Calvo, V., S. Rojo, D. Lopez, B. Galocha, and J. A. Lopez de Castro. 1990. Structure and diversity of HLA-B27-specific T cell epitopes: analysis with site-directed mutants mimicking HLA-B27 subtype polymorphism. J. Immunol. 144: 4038-4045.
    • (1990) J. Immunol , vol.144 , pp. 4038-4045
    • Calvo, V.1    Rojo, S.2    Lopez, D.3    Galocha, B.4    Lopez de Castro, J.A.5
  • 20
    • 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: 505-510.
    • (1992) J. Immunol , vol.149 , pp. 505-510
    • Villadangos, J.A.1    Galocha, B.2    Lopez, D.3    Calvo, V.4    Lopez de Castro, J.A.5
  • 21
    • 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. 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 for genetic analysis. Cell 14: 9-20.
    • (1978) Cell , vol.14 , pp. 9-20
    • Barnstable, C.J.1    Bodmer, W.F.2    Brown, G.3    Galfre, G.4    Milstein, C.5    Williams, A.F.6    Ziegler, A.7
  • 22
    • 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: 49-59.
    • (1982) Hum. Immunol , vol.5 , pp. 49-59
    • Ellis, S.A.1    Taylor, C.2    McMichael, A.3
  • 23
    • 0022533999 scopus 로고
    • Monoclonal antibodies raised against denatured HLA-B locus heavy chains permit biochemical characterization of certain HLA-C locus products
    • Stam, N. J., H. Spits, and H. L. Ploegh. 1986. Monoclonal antibodies raised against denatured HLA-B locus heavy chains permit biochemical characterization of certain HLA-C locus products. J. Immunol. 137: 2299-2306.
    • (1986) J. Immunol , vol.137 , pp. 2299-2306
    • Stam, N.J.1    Spits, H.2    Ploegh, H.L.3
  • 24
    • 26844446015 scopus 로고    scopus 로고
    • 2-microglobulin-free heavy chains by HLA-B27 subtypes differentially associated with ankylosing spondylitis
    • 2-microglobulin-free heavy chains by HLA-B27 subtypes differentially associated with ankylosing spondylitis. Arthritis Rheum. 52: 3290-3299.
    • (2005) Arthritis Rheum , vol.52 , pp. 3290-3299
    • Vázquez, M.N.1    Lopez de Castro, J.A.2
  • 25
    • 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: 5481-5490.
    • (1998) J. Immunol , vol.161 , pp. 5481-5490
    • Paradela, A.1    Garcia-Peydro, M.2    Vazquez, J.3    Rognan, D.4    Lopez de Castro, J.A.5
  • 26
    • 0033961477 scopus 로고    scopus 로고
    • 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
    • Paradela, A., I. Alvarez, M. Garcia-Peydro, L. Sesma, M. Ramos, J. Vazquez, and J. A. Lopez de Castro. 2000. 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. J. Immunol. 164: 329-337.
    • (2000) J. Immunol , vol.164 , pp. 329-337
    • Paradela, A.1    Alvarez, I.2    Garcia-Peydro, M.3    Sesma, L.4    Ramos, M.5    Vazquez, J.6    Lopez de Castro, J.A.7
  • 27
    • 0032969777 scopus 로고    scopus 로고
    • High-sensitivity analysis and sequencing of peptides and proteins by quadrupole ion trap mass spectrometry
    • Marina, A., M. A. Garcia, J. P. Albar, J. Yague, J. A. Lopez de Castro, and J. Vazquez. 1999. High-sensitivity analysis and sequencing of peptides and proteins by quadrupole ion trap mass spectrometry. J. Mass Spectrom. 34: 17-27.
    • (1999) J. Mass Spectrom , vol.34 , pp. 17-27
    • Marina, A.1    Garcia, M.A.2    Albar, J.P.3    Yague, J.4    Lopez de Castro, J.A.5    Vazquez, J.6
  • 28
    • 57549095623 scopus 로고    scopus 로고
    • Disparate folding and stability of the ankylosing spondylitis-associated HLA-B*1403 and B*2705 proteins
    • Merino, E., B. Galocha, M. Vázquez, and J. A. López de Castro. 2008. Disparate folding and stability of the ankylosing spondylitis-associated HLA-B*1403 and B*2705 proteins. Arthritis. Rheum. 58: 3693-3703.
    • (2008) Arthritis. Rheum , vol.58 , pp. 3693-3703
    • Merino, E.1    Galocha, B.2    Vázquez, M.3    López de Castro, J.A.4
  • 29
    • 0037053328 scopus 로고    scopus 로고
    • The peptide repertoires of HLA-B27 subtypes differentially associated to spondyloarthropathy (B*2704 and B*2706) differ by specific changes at three anchor positions
    • Sesma, L., V. Montserrat, J. R. Lamas, A. Marina, J. Vazquez, and J. A. Lopez de Castro. 2002. The peptide repertoires of HLA-B27 subtypes differentially associated to spondyloarthropathy (B*2704 and B*2706) differ by specific changes at three anchor positions. J. Biol. Chem. 277: 16744-16749.
    • (2002) J. Biol. Chem , vol.277 , pp. 16744-16749
    • Sesma, L.1    Montserrat, V.2    Lamas, J.R.3    Marina, A.4    Vazquez, J.5    Lopez de Castro, J.A.6
  • 30
    • 0037047424 scopus 로고    scopus 로고
    • Differential association of HLA-B*2705 and B*2709 to ankylosing spondylitis correlates with limited peptide subsets but not with altered cell surface stability
    • Ramos, M., A. Paradela, M. Vazquez, A. Marina, J. Vazquez, and J. A. Lopez de Castro. 2002. Differential association of HLA-B*2705 and B*2709 to ankylosing spondylitis correlates with limited peptide subsets but not with altered cell surface stability. J. Biol. Chem. 277: 28749-28756.
    • (2002) J. Biol. Chem , vol.277 , pp. 28749-28756
    • Ramos, M.1    Paradela, A.2    Vazquez, M.3    Marina, A.4    Vazquez, J.5    Lopez de Castro, J.A.6
  • 31
    • 33746217869 scopus 로고    scopus 로고
    • B*2707 differs in peptide specificity from B*2705 and B*2704 as much as from HLA-B27 subtypes not associated to spondyloarthritis
    • Gomez, P., V. Montserrat, M. Marcilla, A. Paradela, and J. A. López de Castro. 2006. B*2707 differs in peptide specificity from B*2705 and B*2704 as much as from HLA-B27 subtypes not associated to spondyloarthritis. Eur. J. Immunol. 36: 1867-1881.
    • (2006) Eur. J. Immunol , vol.36 , pp. 1867-1881
    • Gomez, P.1    Montserrat, V.2    Marcilla, M.3    Paradela, A.4    López de Castro, J.A.5
  • 32
    • 27744561683 scopus 로고    scopus 로고
    • Two HLA-B14 subtypes (B*1402 and B*1403) differentially associated with ankylosing spondylitis differ substantially in peptide specificity, but have limited peptide and T-cell epitope sharing with HLA-B27
    • Merino, E., V. Montserrat, A. Paradela, and J. A. Lopez de Castro. 2005. Two HLA-B14 subtypes (B*1402 and B*1403) differentially associated with ankylosing spondylitis differ substantially in peptide specificity, but have limited peptide and T-cell epitope sharing with HLA-B27. J. Biol. Chem. 280: 35868-35880.
    • (2005) J. Biol. Chem , vol.280 , pp. 35868-35880
    • Merino, E.1    Montserrat, V.2    Paradela, A.3    Lopez de Castro, J.A.4
  • 33
    • 34249706374 scopus 로고    scopus 로고
    • Proteasome-independent HLA-B27 ligands arise mainly from small basic proteins
    • Marcilla, M., J. J. Cragnolini, and J. A. Lopez de Castro. 2007. Proteasome-independent HLA-B27 ligands arise mainly from small basic proteins. Mol. Cell. Proteomics 6: 923-938.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 923-938
    • Marcilla, M.1    Cragnolini, J.J.2    Lopez de Castro, J.A.3
  • 34
    • 0024345149 scopus 로고
    • Specificity pockets for the side chains of peptide antigens in HLA-Aw68
    • Garrett, T. P., M. A. Saper, P. J. Bjorkman, J. L. Strominger, and D. C. Wiley. 1989. Specificity pockets for the side chains of peptide antigens in HLA-Aw68. Nature 342: 692-696.
    • (1989) Nature , vol.342 , pp. 692-696
    • Garrett, T.P.1    Saper, M.A.2    Bjorkman, P.J.3    Strominger, J.L.4    Wiley, D.C.5
  • 35
    • 0346521283 scopus 로고    scopus 로고
    • Making sense of mass destruction: Quantitating MHC class I antigen presentation
    • Yewdell, J. W., E. Reits, and J. Neefjes. 2003. Making sense of mass destruction: quantitating MHC class I antigen presentation. Nat. Rev. Immunol. 3: 952-961.
    • (2003) Nat. Rev. Immunol , vol.3 , pp. 952-961
    • Yewdell, J.W.1    Reits, E.2    Neefjes, J.3
  • 38
    • 0033029388 scopus 로고    scopus 로고
    • The South Amerindian allotype HLA-B*3909 has the largest known similarity in peptide specificity and common natural ligands with HLA- B27
    • Yague, J., M. Ramos, J. Vazquez, A. Marina, J. P. Albar, and J. A. Lopez de Castro. 1999. The South Amerindian allotype HLA-B*3909 has the largest known similarity in peptide specificity and common natural ligands with HLA- B27. Tissue Antigens 53: 227-236.
    • (1999) Tissue Antigens , vol.53 , pp. 227-236
    • Yague, J.1    Ramos, M.2    Vazquez, J.3    Marina, A.4    Albar, J.P.5    Lopez de Castro, J.A.6
  • 40
    • 0026673724 scopus 로고
    • Crystal structures of two viral peptides in complex with murine MHC class I H-2Kb
    • Fremont, D. H., M. Matsumura, 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: 919-927.
    • (1992) Science , vol.257 , pp. 919-927
    • Fremont, D.H.1    Matsumura, M.2    Stura, E.A.3    Peterson, P.A.4    Wilson, I.A.5
  • 41
    • 34447503697 scopus 로고    scopus 로고
    • Conformational entropy in molecular recognition by proteins
    • Frederick, K. K., M. S. Marlow, K. G. Valentine, and A. J. Wand. 2007. Conformational entropy in molecular recognition by proteins. Nature 448: 325-329.
    • (2007) Nature , vol.448 , pp. 325-329
    • Frederick, K.K.1    Marlow, M.S.2    Valentine, K.G.3    Wand, A.J.4
  • 42
    • 59749104185 scopus 로고    scopus 로고
    • Side-chain conformational space analysis (SCSA): A multi conformation-based QSAR approach for modeling and prediction of protein-peptide binding affinities
    • In press
    • Zhou, P., X. Chen, and Z. Shang. 2009. Side-chain conformational space analysis (SCSA): a multi conformation-based QSAR approach for modeling and prediction of protein-peptide binding affinities. J. Comput. Aided Mol. Des. In press.
    • (2009) J. Comput. Aided Mol. Des
    • Zhou, P.1    Chen, X.2    Shang, Z.3
  • 44
    • 0036230677 scopus 로고    scopus 로고
    • Optimization of the MHC class I peptide cargo is dependent on tapasin
    • Williams, A. P., C. A. Peh, A. W. Purcell, J. McCluskey, and T. Elliott. 2002. Optimization of the MHC class I peptide cargo is dependent on tapasin. Immunity 16: 509-520.
    • (2002) Immunity , vol.16 , pp. 509-520
    • Williams, A.P.1    Peh, C.A.2    Purcell, A.W.3    McCluskey, J.4    Elliott, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.