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10.3390/cells10102646 http://scihub22266oqcxt.onion/10.3390/cells10102646 34685626!8534114!34685626     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34685626&cmd=llinks): Failed to open stream: HTTP request failed! 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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 |pdf=|usr=}}{{34685626}} gab.com Text Molecular Basis of a Dominant SARS-CoV-2 Spike-Derived Epitope Presented by HLA-A*02:01 Recognised by a Public TCR JO: Cells http://www.kidney.de/pget.php?&tw=1&pmid=34685626 #FOAvip 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. Twit Text FOAVip Molecular Basis of a Dominant SARS-CoV-2 Spike-Derived Epitope Presented by HLA-A*02:01 Recognised by a Public TCR ????Cells http://www.kidney.de/pget.php?&tw=1&pmid=34685626 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34685626 #FOAvip English Wikipedia <ref>{{Cite pmid|34685626}}</ref> Molecular Basis of a Dominant SARS-CoV-2 Spike-Derived Epitope Presented by HLA-A*02:01 Recognised by a Public TCR #MMPMID34685626 Szeto C; Nguyen AT; Lobos CA; Chatzileontiadou DSM; Jayasinghe D; Grant EJ; Riboldi-Tunnicliffe A; Smith C; Gras S Cells 2021[Oct]; 10 (10): ä PMID34685626show ga 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. |*SARS-CoV-2[MESH] |CD8-Positive T-Lymphocytes/cytology[MESH] |COVID-19/*immunology/*virology[MESH] |Crystallography, X-Ray[MESH] |Cytokines/metabolism[MESH] |Epitopes, T-Lymphocyte/*chemistry[MESH] |Epitopes/chemistry[MESH] |HLA-A2 Antigen/chemistry/*immunology[MESH] |Humans[MESH] |Mutation[MESH] |Peptides/chemistry[MESH] |Protein Binding[MESH] |Protein Denaturation[MESH] |Protein Folding[MESH] |Receptors, Antigen, T-Cell/*immunology[MESH] |Spike Glycoprotein, Coronavirus/*chemistry[MESH] |Surface Plasmon Resonance[MESH]Molecular Basis of a Dominant SARS-CoV-2 Spike-Derived Epitope Present(epmc).pdf DeepDyve Pubget Overpricing