2ian Citations

Structural basis for the recognition of mutant self by a tumor-specific, MHC class II-restricted T cell receptor.

Nat. Immunol. 8 398-408 (2007)
Related entries: 2ial, 2iam

Cited: 44 times
EuropePMC logo PMID: 17334368

Abstract

Structural studies of complexes of T cell receptor (TCR) and peptide-major histocompatibility complex (MHC) have focused on TCRs specific for foreign antigens or native self. An unexplored category of TCRs includes those specific for self determinants bearing alterations resulting from disease, notably cancer. We determined here the structure of a human melanoma-specific TCR (E8) bound to the MHC molecule HLA-DR1 and an epitope from mutant triosephosphate isomerase. The structure had features intermediate between 'anti-foreign' and autoimmune TCR-peptide-MHC class II complexes that may reflect the hybrid nature of altered self. E8 manifested very low affinity for mutant triosephosphate isomerase-HLA-DR1 despite the highly tumor-reactive properties of E8 cells. A second TCR (G4) had even lower affinity but underwent peptide-specific formation of dimers, suggesting this as a mechanism for enhancing low-affinity TCR-peptide-MHC interactions for T cell activation.

Articles - 2ian mentioned but not cited (4)



Reviews citing this publication (20)

  1. Evolutionarily conserved amino acids that control TCR-MHC interaction. Marrack P, Scott-Browne JP, Dai S, Gapin L, Kappler JW. Annu. Rev. Immunol. 26 171-203 (2008)
  2. The fidelity, occasional promiscuity, and versatility of T cell receptor recognition. Godfrey DI, Rossjohn J, McCluskey J. Immunity 28 304-314 (2008)
  3. Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes. Armstrong KM, Piepenbrink KH, Baker BM. Biochem. J. 415 183-196 (2008)
  4. Structural alterations in peptide-MHC recognition by self-reactive T cell receptors. Wucherpfennig KW, Call MJ, Deng L, Mariuzza R. Curr. Opin. Immunol. 21 590-595 (2009)
  5. Common themes in the assembly and architecture of activating immune receptors. Call ME, Wucherpfennig KW. Nat. Rev. Immunol. 7 841-850 (2007)
  6. What guides MHC-restricted TCR recognition? Mazza C, Malissen B. Semin. Immunol. 19 225-235 (2007)
  7. Recognition of self-peptide-MHC complexes by autoimmune T-cell receptors. Deng L, Mariuzza RA. Trends Biochem. Sci. 32 500-508 (2007)
  8. Structural basis for self-recognition by autoimmune T-cell receptors. Yin Y, Li Y, Mariuzza RA. Immunol. Rev. 250 32-48 (2012)
  9. Structural and dynamic control of T-cell receptor specificity, cross-reactivity, and binding mechanism. Baker BM, Scott DR, Blevins SJ, Hawse WF. Immunol. Rev. 250 10-31 (2012)
  10. T cell receptor specificity for major histocompatibility complex proteins. Marrack P, Rubtsova K, Scott-Browne J, Kappler JW. Curr. Opin. Immunol. 20 203-207 (2008)
  11. Structural and dynamic control of T-cell receptor specificity, cross-reactivity, and binding mechanism. Baker BM, Scott DR, Blevins SJ, Hawse WF. Immunol. Rev. 250 10-31 (2012)
  12. Structural basis for self-recognition by autoimmune T-cell receptors. Yin Y, Li Y, Mariuzza RA. Immunol. Rev. 250 32-48 (2012)
  13. Structural alterations in peptide-MHC recognition by self-reactive T cell receptors. Wucherpfennig KW, Call MJ, Deng L, Mariuzza R. Curr. Opin. Immunol. 21 590-595 (2009)
  14. Evolutionarily conserved amino acids that control TCR-MHC interaction. Marrack P, Scott-Browne JP, Dai S, Gapin L, Kappler JW. Annu. Rev. Immunol. 26 171-203 (2008)
  15. Conformational changes and flexibility in T-cell receptor recognition of peptide-MHC complexes. Armstrong KM, Piepenbrink KH, Baker BM. Biochem. J. 415 183-196 (2008)
  16. T cell receptor specificity for major histocompatibility complex proteins. Marrack P, Rubtsova K, Scott-Browne J, Kappler JW. Curr. Opin. Immunol. 20 203-207 (2008)
  17. The fidelity, occasional promiscuity, and versatility of T cell receptor recognition. Godfrey DI, Rossjohn J, McCluskey J. Immunity 28 304-314 (2008)
  18. What guides MHC-restricted TCR recognition? Mazza C, Malissen B. Semin. Immunol. 19 225-235 (2007)
  19. Recognition of self-peptide-MHC complexes by autoimmune T-cell receptors. Deng L, Mariuzza RA. Trends Biochem. Sci. 32 500-508 (2007)
  20. Common themes in the assembly and architecture of activating immune receptors. Call ME, Wucherpfennig KW. Nat. Rev. Immunol. 7 841-850 (2007)

Articles citing this publication (20)

  1. T cell-mediated autoimmune disease due to low-affinity crossreactivity to common microbial peptides. Harkiolaki M, Holmes SL, Svendsen P, Gregersen JW, Jensen LT, McMahon R, Friese MA, van Boxel G, Etzensperger R, Tzartos JS, Kranc K, Sainsbury S, Harlos K, Mellins ED, Palace J, Esiri MM, van der Merwe PA, Jones EY, Fugger L. Immunity 30 348-357 (2009)
  2. Vgamma2Vdelta2 T Cell Receptor recognition of prenyl pyrophosphates is dependent on all CDRs. Wang H, Fang Z, Morita CT. J. Immunol. 184 6209-6222 (2010)
  3. Antigen ligation triggers a conformational change within the constant domain of the alphabeta T cell receptor. Beddoe T, Chen Z, Clements CS, Ely LK, Bushell SR, Vivian JP, Kjer-Nielsen L, Pang SS, Dunstone MA, Liu YC, Macdonald WA, Perugini MA, Wilce MC, Burrows SR, Purcell AW, Tiganis T, Bottomley SP, McCluskey J, Rossjohn J. Immunity 30 777-788 (2009)
  4. Cutting edge: Evidence for a dynamically driven T cell signaling mechanism. Hawse WF, Champion MM, Joyce MV, Hellman LM, Hossain M, Ryan V, Pierce BG, Weng Z, Baker BM. J. Immunol. 188 5819-5823 (2012)
  5. Structural basis for the presentation of tumor-associated MHC class II-restricted phosphopeptides to CD4+ T cells. Li Y, Depontieu FR, Sidney J, Salay TM, Engelhard VH, Hunt DF, Sette A, Topalian SL, Mariuzza RA. J. Mol. Biol. 399 596-603 (2010)
  6. On computational approaches for size-and-shape distributions from sedimentation velocity analytical ultracentrifugation. Schuck P. Eur. Biophys. J. 39 1261-1275 (2010)
  7. High-affinity T cell receptor differentiates cognate peptide-MHC and altered peptide ligands with distinct kinetics and thermodynamics. Persaud SP, Donermeyer DL, Weber KS, Kranz DM, Allen PM. Mol. Immunol. 47 1793-1801 (2010)
  8. Minimal conformational plasticity enables TCR cross-reactivity to different MHC class II heterodimers. Holland CJ, Rizkallah PJ, Vollers S, Calvo-Calle JM, Madura F, Fuller A, Sewell AK, Stern LJ, Godkin A, Cole DK. Sci Rep 2 629 (2012)
  9. Efficient induction of CD25- iTreg by co-immunization requires strongly antigenic epitopes for T cells. Geng S, Yu Y, Kang Y, Pavlakis G, Jin H, Li J, Hu Y, Hu W, Wang S, Wang B. BMC Immunol. 12 27 (2011)
  10. Re-Directing CD4(+) T Cell Responses with the Flanking Residues of MHC Class II-Bound Peptides: The Core is Not Enough. Holland CJ, Cole DK, Godkin A. Front Immunol 4 172 (2013)
  11. Structural insights into the editing of germ-line-encoded interactions between T-cell receptor and MHC class II by Vα CDR3. Deng L, Langley RJ, Wang Q, Topalian SL, Mariuzza RA. Proc. Natl. Acad. Sci. U.S.A. 109 14960-14965 (2012)
  12. Physical and functional bivalency observed among TCR/CD3 complexes isolated from primary T cells. Schrum AG, Gil D, Turka LA, Palmer E. J. Immunol. 187 870-878 (2011)
  13. The SCHOOL of nature: I. Transmembrane signaling. Sigalov AB. Self Nonself 1 4-39 (2010)
  14. Understanding TR binding to pMHC complexes: how does a TR scan many pMHC complexes yet preferentially bind to one. Khan JM, Ranganathan S. PLoS ONE 6 e17194 (2011)
  15. Glutamic acid decarboxylase-derived epitopes with specific domains expand CD4(+)CD25(+) regulatory T cells. Chen G, Han G, Feng J, Wang J, Wang R, Xu R, Shen B, Qian J, Li Y. PLoS ONE 4 e7034 (2009)
  16. "Monovalent" ligands that trigger TLR-4 and TCR are not necessarily truly monovalent. Sigalov AB. Mol. Immunol. 51 356-362 (2012)
  17. The SCHOOL of nature: III. From mechanistic understanding to novel therapies. Sigalov AB. Self Nonself 1 192-224 (2010)
  18. Gauche(+) side-chain orientation as a key factor in the search for an immunogenic peptide mixture leading to a complete fully protective vaccine. Bermúdez A, Calderon D, Moreno-Vranich A, Almonacid H, Patarroyo MA, Poloche A, Patarroyo ME. Vaccine 32 2117-2126 (2014)
  19. Binding of TCR multimers and a TCR-like antibody with distinct fine-specificities is dependent on the surface density of HLA complexes. Low JL, Naidoo A, Yeo G, Gehring AJ, Ho ZZ, Yau YH, Shochat SG, Kranz DM, Bertoletti A, Grotenbreg GM. PLoS ONE 7 e51397 (2012)
  20. Structure-based design of altered MHC class II-restricted peptide ligands with heterogeneous immunogenicity. Chen S, Li Y, Depontieu FR, McMiller TL, English AM, Shabanowitz J, Kos F, Sidney J, Sette A, Rosenberg SA, Hunt DF, Mariuzza RA, Topalian SL. J. Immunol. 191 5097-5106 (2013)