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Direct recognition of an intact foreign protein by an αβ T cell receptor. | LitMetric

AI Article Synopsis

  • αβ T cell receptors (αβTCRs) usually recognize antigens in the presence of Major Histocompatibility Complex (MHC) molecules, but some can also bind directly to non-MHC molecules.
  • This study identifies a unique αβ T cell clone that can directly recognize the intact foreign protein R-phycoerythrin (PE) without needing MHC, activating T cells with a strong affinity similar to typical TCR-MHC interactions.
  • The crystal structure analysis shows how multiple αβTCR molecules bind to the PE protein, suggesting that αβTCRs can act similarly to antibodies by recognizing complete proteins rather than just peptide fragments.

Article Abstract

αβ T cell receptors (αβTCRs) co-recognise antigens when bound to Major Histocompatibility Complex (MHC) or MHC class I-like molecules. Additionally, some αβTCRs can bind non-MHC molecules, but how much intact antigen reactivities are achieved remains unknown. Here, we identify an αβ T cell clone that directly recognises the intact foreign protein, R-phycoerythrin (PE), a multimeric (αβ)γ protein complex. This direct αβTCR-PE interaction occurs in an MHC-independent manner, yet triggers T cell activation and bound PE with an affinity comparable to αβTCR-peptide-MHC interactions. The crystal structure reveals how six αβTCR molecules simultaneously engage the PE hexamer, mediated by the complementarity-determining regions (CDRs) of the αβTCR. Here, the αβTCR mainly binds to two α-helices of the globin fold in the PE α-subunit, which is analogous to the antigen-binding platform of the MHC molecule. Using retrogenic mice expressing this TCR, we show that it supports intrathymic T cell development, maturation, and exit into the periphery as mature CD4/CD8 double negative (DN) T cells with TCR-mediated functional capacity. Accordingly, we show how an αβTCR can recognise an intact foreign protein in an antibody-like manner.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11470135PMC
http://dx.doi.org/10.1038/s41467-024-51897-3DOI Listing

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