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.
【저자키워드】 SARS-CoV-2, T cells, epitope presentation, public TCR recognition, YLQ peptide, COVID-19 recovered, 【초록키워드】 Structure, antibodies, T cells, peptide, CD8+ T cells, SARS-CoV-2 virus, X-ray crystallography, immune system, virus, T cell, Viral, epitope, TCR, T cell receptor, Critical, CD8+ T cell, binding, HLA-A*02:01, Interaction, structures, SARS-CoV-2 proteins, HLA-A, individual, complex, help, molecular basis, SARS-CoV-2 protein, clearance, while, dominant, lack, activate, individuals, COVID-19 recovered patients, the SARS-CoV-2 virus, 【제목키워드】 TCR, Public, Basis,