메뉴 건너뛰기




Volumn 2, Issue , 2012, Pages

Minimal conformational plasticity enables TCR cross-reactivity to different MHC class II heterodimers

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; HLA DR1 ANTIGEN; HLA DR4 ANTIGEN; LYMPHOCYTE ANTIGEN RECEPTOR;

EID: 84866070726     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep00629     Document Type: Article
Times cited : (26)

References (58)
  • 2
    • 0033615678 scopus 로고    scopus 로고
    • A direct estimate of the human alphabeta T cell receptor diversity
    • Arstila, T. P. et al. A direct estimate of the human alphabeta T cell receptor diversity. Science 286, 958-961 (1999).
    • (1999) Science , vol.286 , pp. 958-961
    • Arstila, T.P.1
  • 3
    • 0032171644 scopus 로고    scopus 로고
    • A very high level of crossreactivity is an essential feature of the T- cell receptor
    • DOI 10.1016/S0167-5699(98)01299-7, PII S0167569998012997
    • Mason, D. A very high level of crossreactivity is an essential feature of the T-cell receptor. Immunol Today 19, 395-404 (1998). (Pubitemid 28392279)
    • (1998) Immunology Today , vol.19 , Issue.9 , pp. 395-404
    • Mason, D.1
  • 4
    • 54049111388 scopus 로고    scopus 로고
    • Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes
    • Armstrong, K. M., Piepenbrink, K. H.Baker, B. M. Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes. Biochem J 415, 183-196 (2008).
    • (2008) Biochem J , vol.415 , pp. 183-196
    • Armstrong, K.M.1    Piepenbrink, K.H.2    Baker, B.M.3
  • 5
    • 47649130715 scopus 로고    scopus 로고
    • Thermodynamics of T-cell receptor-peptide/MHC interactions: Progress and opportunities
    • DOI 10.1002/jmr.896
    • Armstrong, K. M., Insaidoo, F. K.&Baker, B. M. Thermodynamics of T-cell receptor-peptide/MHC interactions: progress and opportunities. J Mol Recognit 21, 275-287 (2008). (Pubitemid 352019057)
    • (2008) Journal of Molecular Recognition , vol.21 , Issue.4 , pp. 275-287
    • Armstrong, K.M.1    Insaidoo, F.K.2    Baker, B.M.3
  • 6
    • 0032549142 scopus 로고    scopus 로고
    • Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen
    • DOI 10.1126/science.279.5354.1166
    • Garcia, K. C. et al. Structural basis of plasticity in T cell receptor recognition of a self peptide-MHC antigen. Science 279, 1166-1172 (1998). (Pubitemid 28164360)
    • (1998) Science , vol.279 , Issue.5354 , pp. 1166-1172
    • Garcia, K.C.1    Degano, M.2    Pease, L.R.3    Huang, M.4    Peterson, P.A.5    Teyton, L.6    Wilson, I.A.7
  • 7
    • 82555168290 scopus 로고    scopus 로고
    • Disparate degrees of hypervariable loop flexibility control T-cell receptor crossreactivity, specificity, and binding mechanism
    • Scott, D. R., Borbulevych, O. Y., Piepenbrink, K. H., Corcelli, S. A.&Baker, B. M. Disparate degrees of hypervariable loop flexibility control T-cell receptor crossreactivity, specificity, and binding mechanism. J Mol Biol 414, 385-400 (2011).
    • (2011) J Mol Biol , vol.414 , pp. 385-400
    • Scott, D.R.1    Borbulevych, O.Y.2    Piepenbrink, K.H.3    Corcelli, S.A.4    Baker, B.M.5
  • 8
    • 0036682133 scopus 로고    scopus 로고
    • Two-step binding mechanism for T-cell receptor recognition of peptide-MHC
    • DOI 10.1038/nature00920
    • Wu, L. C., Tuot, D. S., Lyons, D. S., Garcia, K. C. Davis, M. M. Two-step binding mechanism for T-cell receptor recognition of peptide MHC. Nature 418, 552-556 (2002). (Pubitemid 34851403)
    • (2002) Nature , vol.418 , Issue.6897 , pp. 552-556
    • Wu, L.C.1    Tuot, D.S.2    Lyons, D.S.3    Garcia, C.4    Davis, M.M.5
  • 9
    • 80052677601 scopus 로고    scopus 로고
    • TCRs used in cancer gene therapy cross-react with MART-1/Melan-A tumor antigens via distinct mechanisms
    • Borbulevych, O. Y., Santhanagopolan, S. M., Hossain, M.&Baker, B. M. TCRs used in cancer gene therapy cross-react with MART-1/Melan-A tumor antigens via distinct mechanisms. J Immunol 187, 2453-2463 (2011).
    • (2011) J Immunol , vol.187 , pp. 2453-2463
    • Borbulevych, O.Y.1    Santhanagopolan, S.M.2    Hossain, M.3    Baker, B.M.4
  • 10
    • 84857189975 scopus 로고    scopus 로고
    • Structural basis for the killing of human beta cells by CD8(1) T cells in type 1 diabetes
    • Bulek, A. M. et al. Structural basis for the killing of human beta cells by CD8(1) T cells in type 1 diabetes. Nat Immunol 13, 283-289 (2012).
    • (2012) Nat Immunol , vol.13 , pp. 283-289
    • Bulek, A.M.1
  • 11
    • 20944450033 scopus 로고    scopus 로고
    • Structural and kinetic basis for heightened immunogenicity of T cell vaccines
    • Chen, J. L. et al. Structural and kinetic basis for heightened immunogenicity of T cell vaccines. J Exp Med 201, 1243-1255 (2005).
    • (2005) J Exp Med , vol.201 , pp. 1243-1255
    • Chen, J.L.1
  • 12
    • 68949108186 scopus 로고    scopus 로고
    • Structural bases for the affinity-driven selection of a public TCR against a dominant human cytomegalovirus epitope
    • Gras, S. et al. Structural bases for the affinity-driven selection of a public TCR against a dominant human cytomegalovirus epitope. J Immunol 183, 430-437 (2009).
    • (2009) J Immunol , vol.183 , pp. 430-437
    • Gras, S.1
  • 14
    • 71749112218 scopus 로고    scopus 로고
    • T cell receptor cross-reactivity directed by antigendependent tuning of peptide-MHC molecular flexibility
    • Borbulevych, O. Y. et al. T cell receptor cross-reactivity directed by antigendependent tuning of peptide-MHC molecular flexibility. Immunity 31, 885-896 (2009).
    • (2009) Immunity , vol.31 , pp. 885-896
    • Borbulevych, O.Y.1
  • 16
    • 0020078842 scopus 로고
    • Antigen-specific human T lymphocyte clones: Induction, antigen specificity, and MHC restriction of influenza virus-immune clones
    • Lamb, J. R. et al. Antigen-specific human T lymphocyte clones: induction, antigen specificity, and MHC restriction of influenza virus-immune clones. J Immunol 128, 233-238 (1982). (Pubitemid 12207447)
    • (1982) Journal of Immunology , vol.128 , Issue.1 , pp. 233-238
    • Lamb, J.R.1    Eckels, D.D.2    Lake, P.3
  • 17
    • 0025793243 scopus 로고
    • Single amino acid changes in DR and antigen define residues critical for peptide-MHC binding and T cell recognition
    • Krieger, J. I. et al. Single amino acid changes in DR and antigen define residues critical for peptide-MHC binding and T cell recognition. J Immunol 146, 2331-2340 (1991).
    • (1991) J Immunol , vol.146 , pp. 2331-2340
    • Krieger, J.I.1
  • 18
    • 0025323546 scopus 로고
    • High-affinity binding of an influenza hemagglutinin-derived peptide to purified HLA-DR
    • Roche, P. A.&Cresswell, P. High-affinity binding of an influenza hemagglutininderived peptide to purified HLA-DR. J Immunol 144, 1849-1856 (1990). (Pubitemid 20094019)
    • (1990) Journal of Immunology , vol.144 , Issue.5 , pp. 1849-1856
    • Roche, P.A.1    Cresswell, P.2
  • 19
    • 0029155735 scopus 로고
    • The effects of changes at peptide residues contactingMHCclass II T-cell receptor on antigen recognition and human Th0 cell effector function
    • Lamb, J. R. et al. The effects of changes at peptide residues contactingMHCclass II T-cell receptor on antigen recognition and human Th0 cell effector function. Immunology 85, 447-454 (1995).
    • (1995) Immunology , vol.85 , pp. 447-454
    • Lamb, J.R.1
  • 20
    • 0028909789 scopus 로고
    • Pocket 4 of the HLA-DR(alpha,beta 1 0401) molecule is a major determinant of T cells recognition of peptide
    • Fu, X. T. et al. Pocket 4 of the HLA-DR(alpha,beta 1 0401) molecule is a major determinant of T cells recognition of peptide. J Exp Med 181, 915-926 (1995).
    • (1995) J Exp Med , vol.181 , pp. 915-926
    • Fu, X.T.1
  • 21
    • 0034662985 scopus 로고    scopus 로고
    • Identification of T cell ligands in a library of peptides covalently attached to HLA-DR4
    • Boen, E.,Crownover, A. R.,McIlhaney, M.,Korman,A. J.Bill, J. Identification of T cell ligands in a library of peptides covalently attached to HLA-DR4. J Immunol 165, 2040-2047 (2000). (Pubitemid 30648749)
    • (2000) Journal of Immunology , vol.165 , Issue.4 , pp. 2040-2047
    • Boen, E.1    Crownover, A.R.2    McIlhaney, M.3    Korman, A.J.4    Bill, J.5
  • 22
    • 0031665410 scopus 로고    scopus 로고
    • Altered peptide ligands and wild-type peptide induce indistinguishable responses of a human Th0 clone
    • DOI 10.1002/(SICI)1521-4141(199 809)28:09<2801::AID-IMMU2801>3.0. CO;2-N
    • van Bergen, J.&Koning, F. Altered peptide ligands and wild-type peptide induce indistinguishable responses of a human Th0 clone. Eur J Immunol 28, 2801-2808 (1998). (Pubitemid 28425238)
    • (1998) European Journal of Immunology , vol.28 , Issue.9 , pp. 2801-2808
    • Van Bergen, J.1    Koning, F.2
  • 24
    • 0033084056 scopus 로고    scopus 로고
    • Empty and peptide-loaded class II major histocompatibility complex proteins produced by expression in Escherichia coli and folding in vitro
    • DOI 10.1006/prep.1998.0987
    • Frayser, M., Sato, A. K., Xu, L.&Stern, L. J. Empty and peptide-loaded class II major histocompatibility complex proteins produced by expression in Escherichia coli and folding in vitro. Protein Expr Purif 15, 105-114 (1999). (Pubitemid 29321476)
    • (1999) Protein Expression and Purification , vol.15 , Issue.1 , pp. 105-114
    • Frayser, M.1    Sato, A.K.2    Xu, L.3    Stern, L.J.4
  • 26
    • 40849095843 scopus 로고    scopus 로고
    • T cell receptor engagement of peptide-major histocompatibility complex class i does not modify CD8 binding
    • Cole, D. K. et al. T cell receptor engagement of peptide-major histocompatibility complex class I does not modify CD8 binding. Mol Immunol 45, 2700-2709 (2008).
    • (2008) Mol Immunol , vol.45 , pp. 2700-2709
    • Cole, D.K.1
  • 28
    • 0019916069 scopus 로고
    • Human T-cell clones recognize chemically synthesized peptides of influenza haemagglutinin
    • DOI 10.1038/300066a0
    • Lamb, J. R., Eckels, D. D., Lake, P., Woody, J. N.&Green, N. Human T-cell clones recognize chemically synthesized peptides of influenza haemagglutinin. Nature 300, 66-69 (1982). (Pubitemid 12005056)
    • (1982) Nature , vol.300 , Issue.5887 , pp. 66-69
    • Lamb, J.R.1    Eckels, D.D.2    Lake, P.3
  • 29
    • 0033710093 scopus 로고    scopus 로고
    • The relationship of MHC-peptide binding and T cell activation probed using chemically defined MHC class II oligomers
    • Cochran, J. R., Cameron, T. O.&Stern, L. J. The relationship of MHC-peptide binding and T cell activation probed using chemically defined MHC class II oligomers. Immunity 12, 241-250 (2000).
    • (2000) Immunity , vol.12 , pp. 241-250
    • Cochran, J.R.1    Cameron, T.O.2    Stern, L.J.3
  • 30
    • 0027171406 scopus 로고
    • + T cell clones obtained from Plasmodium falciparum sporozoite- immunized volunteers recognize polymorphic sequences of the circumsporozoite protein
    • Moreno, A. et al. CD41 T cell clones obtained from Plasmodium falciparum sporozoite-immunized volunteers recognize polymorphic sequences of the circumsporozoite protein. J Immunol 151, 489-499 (1993). (Pubitemid 23207014)
    • (1993) Journal of Immunology , vol.151 , Issue.1 , pp. 489-499
    • Moreno, A.1    Clavijo, P.2    Edelman, R.3    Davis, J.4    Sztein, M.5    Sinigaglia, F.6    Nardin, E.7
  • 32
    • 84866111244 scopus 로고
    • MOSFILM jnt cCP4 and eSF-eACMB
    • Leslie, A. MOSFILM. Jnt CCP4 and ESF-EACMB Newslett. (1992).
    • (1992) Newslett
    • Leslie, A.1
  • 33
    • 0028103275 scopus 로고
    • Collaborative Computational Project N the CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, N. The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760-763 (1994).
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 38
    • 79251518600 scopus 로고    scopus 로고
    • Genetic and structural basis for selection of a ubiquitous T cell receptor deployed in epstein-barr virus infection
    • Miles, J. J. et al. Genetic and structural basis for selection of a ubiquitous T cell receptor deployed in epstein-barr virus infection. PLoS Pathog 6, e1001198 (2010).
    • (2010) PLoS Pathog , vol.6
    • Miles, J.J.1
  • 39
    • 0034329441 scopus 로고    scopus 로고
    • Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1
    • Hennecke, J., Carfi, A.&Wiley, D. C. Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1. Embo J 19, 5611-5624 (2000).
    • (2000) Embo J , vol.19 , pp. 5611-5624
    • Hennecke, J.1    Carfi, A.2    Wiley, D.C.3
  • 40
    • 0037018102 scopus 로고    scopus 로고
    • Structure of a complex of the human α/β T cell receptor (TCR) HA1.7, Influenza hemagglutinin peptide, and major histocompatibility complex class II molecule, HLA-DR4 (DRA 0101 and DRBI 0401): Insight into TCR cross-restriction and alloreactivity
    • DOI 10.1084/jem.20011194
    • Hennecke, J. Wiley, D. C. Structure of a complex of the human alpha/beta T cell receptor (TCR) HA1.7, influenza hemagglutinin peptide, and major histocompatibility complex class II molecule, HLA-DR4 (DRA 0101 and DRB1 0401): insight into TCR cross-restriction and alloreactivity. J Exp Med 195, 571-581 (2002). (Pubitemid 34461502)
    • (2002) Journal of Experimental Medicine , vol.195 , Issue.5 , pp. 571-581
    • Hennecke, J.1    Wiley, D.C.2
  • 41
    • 0034057892 scopus 로고    scopus 로고
    • R(free) and the R(free) ratio. II. Calculation of the expected values and variances of cross-validation statistics in macromolecular least-squares refinement
    • DOI 10.1107/S0907444999016868
    • Tickle, I. J., Laskowski, R. A. Moss, D. S. Rfree and the rfree ratio. II. Calculation Of the expected values and variances of cross-validation statistics in macromolecular least-squares refinement. Acta Crystallogr D Biol Crystallogr 56, 442-450 (2000). (Pubitemid 30231224)
    • (2000) Acta Crystallographica Section D: Biological Crystallography , vol.56 , Issue.4 , pp. 442-450
    • Tickle, I.J.1    Laskowski, R.A.2    Moss, D.S.3
  • 43
    • 0029027698 scopus 로고
    • Mapping T cell recognition: The identification of a T cell receptor residue critical to the specific interaction with an influenza hemagglutinin peptide
    • Wedderburn, L. R., Searle, S. J., Rees, A. R., Lamb, J. R.&Owen, M. J. Mapping T cell recognition: the identification of a T cell receptor residue critical to the specific interaction with an influenza hemagglutinin peptide. Eur J Immunol 25, 1654-1662 (1995).
    • (1995) Eur J Immunol , vol.25 , pp. 1654-1662
    • Wedderburn, L.R.1    Searle, S.J.2    Rees, A.R.3    Lamb, J.R.4    Owen, M.J.5
  • 47
    • 70350438026 scopus 로고    scopus 로고
    • Germ line-governed recognition of a cancer epitope by an immunodominant human T-cell receptor
    • Cole, D. K. et al. Germ line-governed recognition of a cancer epitope by an immunodominant human T-cell receptor. J Biol Chem 284, 27281-27289 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 27281-27289
    • Cole, D.K.1
  • 48
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • DOI 10.1016/0022-2836(84)90309-7
    • Eisenberg, D., Schwarz, E., Komaromy, M. Wall, R. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol 179, 125-142 (1984). (Pubitemid 16223392)
    • (1984) Journal of Molecular Biology , vol.179 , Issue.1 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 49
    • 12544253697 scopus 로고    scopus 로고
    • Two different T cell receptors use different thermodynamic strategies to recognize the same peptide/ MHC ligand
    • Davis-Harrison, R. L., Armstrong, K. M.&Baker, B. M. Two different T cell receptors use different thermodynamic strategies to recognize the same peptide/ MHC ligand. J Mol Biol 346, 533-550 (2005).
    • (2005) J Mol Biol , vol.346 , pp. 533-550
    • Davis-Harrison, R.L.1    Armstrong, K.M.2    Baker, B.M.3
  • 50
    • 33646240071 scopus 로고    scopus 로고
    • Disparate thermodynamics governing T cell receptor-MHC-I interactions implicate extrinsic factors in guiding MHC restriction
    • U S A
    • Ely, L. K. et al. Disparate thermodynamics governing T cell receptor-MHC-I interactions implicate extrinsic factors in guiding MHC restriction. Proc Natl Acad Sci U S A 103, 6641-6646 (2006).
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 6641-6646
    • Ely, L.K.1
  • 51
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • DOI 10.1038/384134a0
    • Garboczi, D. N. et al. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. Nature 384, 134-141 (1996). (Pubitemid 26386462)
    • (1996) Nature , vol.384 , Issue.6605 , 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
  • 53
    • 0038300653 scopus 로고    scopus 로고
    • A structural basis for immunodominant human T cell receptor recognition
    • DOI 10.1038/ni942
    • Stewart-Jones, G. B., McMichael, A. J., Bell, J. I., Stuart, D. I.&Jones, E. Y. A structural basis for immunodominant human T cell receptor recognition. Nat Immunol 4, 657-663 (2003). (Pubitemid 36874442)
    • (2003) Nature Immunology , vol.4 , Issue.7 , pp. 657-663
    • Stewart-Jones, G.B.E.1    McMichael, A.J.2    Bell, J.I.3    Stuart, D.I.4    Jones, E.Y.5
  • 55
    • 0036849685 scopus 로고    scopus 로고
    • The 1.5 A crystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance
    • DOI 10.1016/S0969-2126(02)00878-X, PII S096921260200878X
    • Kjer-Nielsen, L. et al. The 1.5 Acrystal structure of a highly selected antiviral T cell receptor provides evidence for a structural basis of immunodominance. Structure (Camb) 10, 1521-1532 (2002). (Pubitemid 35351492)
    • (2002) Structure , vol.10 , Issue.11 , pp. 1521-1532
    • Kjer-Nielsen, L.1    Clements, C.S.2    Brooks, A.G.3    Purcell, A.W.4    McCluskey, J.5    Rossjohn, J.6
  • 56
    • 71749097993 scopus 로고    scopus 로고
    • T cell allorecognition via molecular mimicry
    • Macdonald, W. A. et al. T cell allorecognition via molecular mimicry. Immunity 31, 897-908 (2009).
    • (2009) Immunity , vol.31 , pp. 897-908
    • MacDonald, W.A.1
  • 57
    • 79952743743 scopus 로고    scopus 로고
    • Conformational melding permits a conserved binding geometry in TCR recognition of foreign and self molecular mimics
    • Borbulevych, O. Y., Piepenbrink, K. H.&Baker, B. M. Conformational melding permits a conserved binding geometry in TCR recognition of foreign and self molecular mimics. J Immunol 186, 2950-2958 (2011).
    • (2011) J Immunol , vol.186 , pp. 2950-2958
    • Borbulevych, O.Y.1    Piepenbrink, K.H.2    Baker, B.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.