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Highly divergent T-cell receptor binding modes underlie specific recognition of a bulged viral peptide bound to a human leukocyte antigen class I molecule.

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Liu YC, Miles JJ, Neller MA, Gostick E, Price DA, Purcell AW, McCluskey J, Burrows SR, Rossjohn J, Gras S
OpenAccess logo J Biol Chem 288 15442-54 (2013)
Cited: 36 times
EuropePMC logo PMID: 23569211

Abstract

Human leukocyte antigen (HLA)-I molecules can present long peptides, yet the mechanisms by which T-cell receptors (TCRs) recognize featured pHLA-I landscapes are unclear. We compared the binding modes of three distinct human TCRs, CA5, SB27, and SB47, complexed with a "super-bulged" viral peptide (LPEPLPQGQLTAY) restricted by HLA-B*35:08. The CA5 and SB27 TCRs engaged HLA-B*35:08(LPEP) similarly, straddling the central region of the peptide but making limited contacts with HLA-B*35:08. Remarkably, the CA5 TCR did not contact the α1-helix of HLA-B*35:08. Differences in the CDR3β loop between the CA5 and SB27 TCRs caused altered fine specificities. Surprisingly, the SB47 TCR engaged HLA-B*35:08(LPEP) using a completely distinct binding mechanism, namely "bypassing" the bulged peptide and making extensive contacts with the extreme N-terminal end of HLA-B*35:08. This docking footprint included HLA-I residues not observed previously as TCR contact sites. The three TCRs exhibited differing patterns of alloreactivity toward closely related or distinct HLA-I allotypes. Thus, the human T-cell repertoire comprises a range of TCRs that can interact with "bulged" pHLA-I epitopes using unpredictable strategies, including the adoption of atypical footprints on the MHC-I.

Reviews - 4jrx mentioned but not cited (2)

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  2. T cell receptor bias for MHC: co-evolution or co-receptors? Rangarajan S, Mariuzza RA. Cell Mol Life Sci 71 3059-3068 (2014)

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Reviews citing this publication (7)

  1. T cell antigen receptor recognition of antigen-presenting molecules. Rossjohn J, Gras S, Miles JJ, Turner SJ, Godfrey DI, McCluskey J. Annu Rev Immunol 33 169-200 (2015)
  2. Using T Cell Receptor Repertoires to Understand the Principles of Adaptive Immune Recognition. Bradley P, Thomas PG. Annu Rev Immunol 37 547-570 (2019)
  3. TCR Recognition of Peptide-MHC-I: Rule Makers and Breakers. Szeto C, Lobos CA, Nguyen AT, Gras S. Int J Mol Sci 22 E68 (2020)
  4. Understanding the complexity and malleability of T-cell recognition. Miles JJ, McCluskey J, Rossjohn J, Gras S. Immunol Cell Biol 93 433-441 (2015)
  5. Targeting the MHC Ligandome by Use of TCR-Like Antibodies. Høydahl LS, Frick R, Sandlie I, Løset GÅ. Antibodies (Basel) 8 E32 (2019)
  6. Predisposed αβ T cell antigen receptor recognition of MHC and MHC-I like molecules? Eckle SB, Turner SJ, Rossjohn J, McCluskey J. Curr Opin Immunol 25 653-659 (2013)
  7. Specificity, promiscuity, and precursor frequency in immunoreceptors. Venturi V, Rudd BD, Davenport MP. Curr Opin Immunol 25 639-645 (2013)

Articles citing this publication (18)



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