Journal
CELLS
Volume 10, Issue 10, Pages -Publisher
MDPI
DOI: 10.3390/cells10102646
Keywords
SARS-CoV-2; T cells; epitope presentation; public TCR recognition; YLQ peptide; COVID-19 recovered
Categories
Funding
- Monash University
- La Trobe University
- Australian Nuclear Science and Technology Organisation (ANSTO)
- Australian Nuclear Science and Technology Organisation (AINSE ECR grants)
- Australian Nuclear Science and Technology Organisation (AINSE PGRA)
- Australian Research Council (ARC)
- National Health and Medical Research Council (NHMRC)
- Medical Research Future Fund (MRFF)
- Monash Biomedicine Institute PhD scholarship
- AINSE Ltd. Postgraduate Research Award (PGRA)
- NHMRC CJ Martin Fellowship [1110429]
- Australian Research Council DECRA [DE210101479]
- NHMRC SRF [1159272]
- National Health and Medical Research Council of Australia [1159272, 1110429] Funding Source: NHMRC
- Australian Research Council [DE210101479] Funding Source: Australian Research Council
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The study presents the crystallography structure of T cell receptor binding with a SARS-CoV-2 epitope, demonstrating the activation of CD8+ T cell response in COVID-19 patients and providing insights into TCR recognition mechanisms.
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.
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