7EJN
Complex Structure of HLA-A*2402 with the Peptide from HCoV(CoV-HKU1) spike protein
Summary for 7EJN
Entry DOI | 10.2210/pdb7ejn/pdb |
Descriptor | MHC class I antigen, Beta-2-microglobulin, 9-mer peptide from the HCoV spike protein, ... (4 entities in total) |
Functional Keywords | hla-a*2402, mhc class i, immune system, coronavirus |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 3 |
Total formula weight | 45611.52 |
Authors | Murayama, K.,Kato-Murayama, M.,Shirouzu, M. (deposition date: 2021-04-02, release date: 2022-01-26, Last modification date: 2023-11-29) |
Primary citation | Shimizu, K.,Iyoda, T.,Sanpei, A.,Nakazato, H.,Okada, M.,Ueda, S.,Kato-Murayama, M.,Murayama, K.,Shirouzu, M.,Harada, N.,Hidaka, M.,Fujii, S.I. Identification of TCR repertoires in functionally competent cytotoxic T cells cross-reactive to SARS-CoV-2. Commun Biol, 4:1365-1365, 2021 Cited by PubMed Abstract: SARS-CoV-2-specific CD8 T cells are scarce but detectable in unexposed healthy donors (UHDs). It remains unclear whether pre-existing human coronavirus (HCoV)-specific CD8 T cells are converted to functionally competent T cells cross-reactive to SARS-CoV-2. Here, we identified the HLA-A24-high binding, immunodominant epitopes in SARS-CoV-2 spike region that can be recognized by seasonal coronavirus-specific CD8 T cells from HLA-A24 UHDs. Cross-reactive CD8 T cells were clearly reduced in patients with hematological malignancy, who are usually immunosuppressed, compared to those in UHDs. Furthermore, we showed that CD8 T cells in response to a selected dominant epitope display multifunctionality and cross-functionality across HCoVs in HLA-A24 donors. Cross-reactivity of T-cell receptors isolated from them exhibited selective diversity at the single-cell level. Taken together, when stimulated well by immunodominant epitopes, selective pre-existing CD8 T cells with high functional avidity may be cross-reactive against SARS-CoV-2. PubMed: 34857854DOI: 10.1038/s42003-021-02885-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.11 Å) |
Structure validation
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