Rashleigh, Liam, Venugopal, Hariprasad, Rice, Michael T., Gunasinghe, Sachith D., Sok, Chhon Ling, Gherardin, Nicholas A., Almeida, Catarina F., Van Rhijn, Ildiko, Moody, D. Branch, Godfrey, Dale I., Rossjohn, Jamie ![]() ![]() |
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Abstract
The antigen recognition principles of B cells and αβ T cells have been well described compared to those of the γδ T cell. By way of their specificity conferring receptor (γδTCR), γδ T cells can directly bind proteinaceous antigens. A known γδ T cell and B cell model antigen is phycoerythrin (PE), a light harvesting protein from rhodophytes and cyanobacteria. Here we probed human γδTCR reactivity to PE, in which a Vδ1Vγ5 TCR bound directly to induce proximal signaling and cellular activation. We determined the cryoelectron microscopy (cryo-EM) structure of the γδTCR-phycoerythrin immune complex. We then determined the cryo-EM structures of an antibody fragment and an αβTCR bound to PE. This revealed convergent use of apical aromatic residues to mediate contacts with a common PE epitope. Comparative analyses of the γδTCR revealed multiple antibody-like characteristics, including an enrichment of apical aromatic residues. Our findings reveal further distinct facets of antigen recognition by the γδTCR.
Item Type: | Article |
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Date Type: | Published Online |
Status: | In Press |
Schools: | Schools > Medicine |
Publisher: | Elsevier |
ISSN: | 0969-2126 |
Date of First Compliant Deposit: | 12 August 2025 |
Date of Acceptance: | 4 July 2025 |
Last Modified: | 12 Aug 2025 12:48 |
URI: | https://orca.cardiff.ac.uk/id/eprint/180372 |
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