7ZR2
Crystal structure of a chimeric protein mimic of SARS-CoV-2 Spike HR1 in complex with HR2
Summary for 7ZR2
| Entry DOI | 10.2210/pdb7zr2/pdb |
| Descriptor | Spike protein S2',Chimeric protein mimic of SARS-CoV-2 Spike HR1, Spike protein S2' (3 entities in total) |
| Functional Keywords | coiled-coil, antiviral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 More |
| Total number of polymer chains | 2 |
| Total formula weight | 31250.85 |
| Authors | Camara-Artigas, A.,Gavira, J.A.,Cano-Munoz, M.,Polo-Megias, D.,Conejero-Lara, F. (deposition date: 2022-05-03, release date: 2022-11-09, Last modification date: 2024-10-09) |
| Primary citation | Cano-Munoz, M.,Polo-Megias, D.,Camara-Artigas, A.,Gavira, J.A.,Lopez-Rodriguez, M.J.,Laumond, G.,Schmidt, S.,Demiselle, J.,Bahram, S.,Moog, C.,Conejero-Lara, F. Novel chimeric proteins mimicking SARS-CoV-2 spike epitopes with broad inhibitory activity. Int.J.Biol.Macromol., 222:2467-2478, 2022 Cited by PubMed Abstract: SARS-CoV-2 spike (S) protein mediates virus attachment to the cells and fusion between viral and cell membranes. Membrane fusion is driven by mutual interaction between the highly conserved heptad-repeat regions 1 and 2 (HR1 and HR2) of the S2 subunit of the spike. For this reason, these S2 regions are interesting therapeutic targets for COVID-19. Although HR1 and HR2 have been described as transiently exposed during the fusion process, no significant antibody responses against these S2 regions have been reported. Here we designed chimeric proteins that imitate highly stable HR1 helical trimers and strongly bind to HR2. The proteins have broad inhibitory activity against WT B.1 and BA.1 viruses. Sera from COVID-19 convalescent donors showed significant levels of reactive antibodies (IgG and IgA) against the HR1 mimetic proteins, whereas these antibody responses were absent in sera from uninfected donors. Moreover, both inhibitory activity and antigenicity of the proteins correlate positively with their structural stability but not with the number of amino acid changes in their HR1 sequences, indicating a conformational and conserved nature of the involved epitopes. Our results reveal previously undetected spike epitopes that may guide the design of new robust COVID-19 vaccines and therapies. PubMed: 36220405DOI: 10.1016/j.ijbiomac.2022.10.031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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