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A conserved energetic footprint underpins recognition of human leukocyte antigen-E by two distinct αβ T cell receptors.

Sullivan LC, Walpole NG, Farenc C, Pietra G, Sum MJW, Clements CS, Lee EJ, Beddoe T, Falco M, Mingari MC, Moretta L, Gras S, Rossjohn J, Brooks AG
J Biol Chem 292 21149-21158 (2017)
Cited: 15 times
EuropePMC logo PMID: 28972140

Abstract

αβ T cell receptors (TCRs) interact with peptides bound to the polymorphic major histocompatibility complex class Ia (MHC-Ia) and class II (MHC-II) molecules as well as the essentially monomorphic MHC class Ib (MHC-Ib) molecules. Although there is a large amount of information on how TCRs engage with MHC-Ia and MHC-II, our understanding of TCR/MHC-Ib interactions is very limited. Infection with cytomegalovirus (CMV) can elicit a CD8+ T cell response restricted by the human MHC-Ib molecule human leukocyte antigen (HLA)-E and specific for an epitope from UL40 (VMAPRTLIL), which is characterized by biased TRBV14 gene usage. Here we describe an HLA-E-restricted CD8+ T cell able to recognize an allotypic variant of the UL40 peptide with a modification at position 8 (P8) of the peptide (VMAPRTLVL) that uses the TRBV9 gene segment. We report the structures of a TRBV9+ TCR in complex with the HLA-E molecule presenting the two peptides. Our data revealed that the TRBV9+ TCR adopts a different docking mode and molecular footprint atop HLA-E when compared with the TRBV14+ TCR-HLA-E ternary complex. Additionally, despite their differing V gene segment usage and different docking mechanisms, mutational analyses showed that the TCRs shared a conserved energetic footprint on the HLA-E molecule, focused around the peptide-binding groove. Hence, we provide new insights into how monomorphic MHC molecules interact with T cells.

Articles - 5w1w mentioned but not cited (2)

  1. A conserved energetic footprint underpins recognition of human leukocyte antigen-E by two distinct αβ T cell receptors. Sullivan LC, Walpole NG, Farenc C, Pietra G, Sum MJW, Clements CS, Lee EJ, Beddoe T, Falco M, Mingari MC, Moretta L, Gras S, Rossjohn J, Brooks AG. J Biol Chem 292 21149-21158 (2017)
  2. Structure-guided stabilization of pathogen-derived peptide-HLA-E complexes using non-natural amino acids conserves native TCR recognition. Barber C, De Souza VA, Paterson RL, Martin-Urdiroz M, Mulakkal NC, Srikannathasan V, Connolly M, Phillips G, Foong-Leong T, Pengelly R, Karuppiah V, Grant T, Dembek M, Verma A, Gibbs-Howe D, Blicher TH, Knox A, Robinson RA, Cole DK, Leonard S. Eur J Immunol 52 618-632 (2022)


Reviews citing this publication (5)

  1. 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)
  2. Modulation of innate and adaptive immunity by cytomegaloviruses. Berry R, Watson GM, Jonjic S, Degli-Esposti MA, Rossjohn J. Nat Rev Immunol 20 113-127 (2020)
  3. Integrating Experiment and Theory to Understand TCR-pMHC Dynamics. Buckle AM, Borg NA. Front Immunol 9 2898 (2018)
  4. Antigen presentation by MHC-E: a putative target for vaccination? Voogd L, Ruibal P, Ottenhoff THM, Joosten SA. Trends Immunol 43 355-365 (2022)
  5. Evolution and molecular interactions of major histocompatibility complex (MHC)-G, -E and -F genes. Arnaiz-Villena A, Suarez-Trujillo F, Juarez I, Rodríguez-Sainz C, Palacio-Gruber J, Vaquero-Yuste C, Molina-Alejandre M, Fernández-Cruz E, Martin-Villa JM. Cell Mol Life Sci 79 464 (2022)

Articles citing this publication (8)



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