7RTR

YLQ-SG3 TCR in complex with SARS-CoV-2 Spike-derived peptide S269-277 (YLQPRTFLL) presented by HLA-A*02:01

Summary for 7RTR

• Entry DOI: 10.2210/pdb7rtr/pdb
• Descriptor: HLA class I antigen, Beta-2-microglobulin, Spike protein S1, ... (7 entities in total)
• Functional Keywords: human leukocyte antigen, major histocompatibility complex, hla-a2, hla-a*02:01, ylqprtfll, t cell receptor, tcr, tcrpmhc, immune system
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 5
• Total formula weight: 104379.03

Authors

Szeto, C.,Gras, S. (deposition date: 2021-08-14, release date: 2021-10-13, Last modification date: 2024-10-16)

Primary citation

Szeto, C.,Nguyen, A.T.,Lobos, C.A.,Chatzileontiadou, D.S.M.,Jayasinghe, D.,Grant, E.J.,Riboldi-Tunnicliffe, A.,Smith, C.,Gras, S.
Molecular Basis of a Dominant SARS-CoV-2 Spike-Derived Epitope Presented by HLA-A*02:01 Recognised by a Public TCR.
Cells, 10:-, 2021

PubMed Abstract: The data currently available on how the immune system recognises the SARS-CoV-2 virus is growing rapidly. While there are structures of some SARS-CoV-2 proteins in complex with antibodies, which helps us understand how the immune system is able to recognise this new virus; however, we lack data on how T cells are able to recognise this virus. T cells, especially the cytotoxic CD8+ T cells, are critical for viral recognition and clearance. Here we report the X-ray crystallography structure of a T cell receptor, shared among unrelated individuals (public TCR) in complex with a dominant spike-derived CD8+ T cell epitope (YLQ peptide). We show that YLQ activates a polyfunctional CD8+ T cell response in COVID-19 recovered patients. We detail the molecular basis for the shared TCR gene usage observed in HLA-A*02:01+ individuals, providing an understanding of TCR recognition towards a SARS-CoV-2 epitope. Interestingly, the YLQ peptide conformation did not change upon TCR binding, facilitating the high-affinity interaction observed.

PubMed: 34685626
DOI: 10.3390/cells10102646

Experimental method

X-RAY DIFFRACTION (2.6 Å)