7KGO
Crystal Structure of HLA-A*0201in complex with SARS-CoV-2 N351-359
Summary for 7KGO
| Entry DOI | 10.2210/pdb7kgo/pdb |
| Descriptor | MHC class I antigen, Beta-2-microglobulin, Nucleoprotein, ... (7 entities in total) |
| Functional Keywords | hla-a*0201, t cell, sars-cov-2, covid-19, viral peptide, tcr, immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 45306.72 |
| Authors | Szeto, C.,Chatzileontiadou, D.S.M.,Riboldi-Tunnicliffe, A.,Gras, S. (deposition date: 2020-10-18, release date: 2021-01-20, Last modification date: 2024-11-20) |
| Primary citation | Szeto, C.,Chatzileontiadou, D.S.M.,Nguyen, A.T.,Sloane, H.,Lobos, C.A.,Jayasinghe, D.,Halim, H.,Smith, C.,Riboldi-Tunnicliffe, A.,Grant, E.J.,Gras, S. The presentation of SARS-CoV-2 peptides by the common HLA-A * 02:01 molecule. Iscience, 24:102096-102096, 2021 Cited by PubMed Abstract: CD8+ T cells are crucial for anti-viral immunity; however, understanding T cell responses requires the identification of epitopes presented by human leukocyte antigens (HLA). To date, few SARS-CoV-2-specific CD8+ T cell epitopes have been described. Internal viral proteins are typically more conserved than surface proteins and are often the target of CD8+ T cells. Therefore, we have characterized eight peptides derived from the internal SARS-CoV-2 nucleocapsid protein predicted to bind HLA-A02:01, the most common HLA molecule in the global population. We determined not all peptides could form a complex with HLA-A02:01, and the six crystal structures determined revealed that some peptides adopted a mobile conformation. We therefore provide a molecular understanding of SARS-CoV-2 CD8+ T cell epitopes. Furthermore, we show that there is limited pre-existing CD8+ T cell response toward these epitopes in unexposed individuals. Together, these data show that SARS-CoV-2 nucleocapsid might not contain potent epitopes restricted to HLA-A02:01. PubMed: 33521593DOI: 10.1016/j.isci.2021.102096 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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