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Molecular Basis of a Dominant SARS-CoV-2 Spike-Derived Epitope Presented by HLA-A*02:01 Recognised by a Public TCR
| Content Provider | MDPI |
|---|---|
| Author | Szeto, Christopher Nguyen, Andrea T. Lobos, Christian A. Chatzileontiadou, Demetra S. M. Jayasinghe, Dhilshan Grant, Emma J. Riboldi-Tunnicliffe, Alan Smith, Corey Gras, Stephanie |
| Copyright Year | 2021 |
| Description | 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. |
| Starting Page | 2646 |
| e-ISSN | 20734409 |
| DOI | 10.3390/cells10102646 |
| Journal | Cells |
| Issue Number | 10 |
| Volume Number | 10 |
| Language | English |
| Publisher | MDPI |
| Publisher Date | 2021-10-03 |
| Access Restriction | Open |
| Subject Keyword | Cells Immunology Sars-cov-2 T Cells Epitope Presentation Public Tcr Recognition Ylq Peptide Covid-19 Recovered |
| Content Type | Text |
| Resource Type | Article |
