8E39
Purification of Enterovirus A71, strain 4643, WT capsid
Summary for 8E39
| Entry DOI | 10.2210/pdb8e39/pdb |
| EMDB information | 27860 |
| Descriptor | VP1, VP2, VP3, ... (5 entities in total) |
| Functional Keywords | enterovirus, thermostability, capsid, virus |
| Biological source | Human enterovirus 71 (EV71, EV-71) More |
| Total number of polymer chains | 4 |
| Total formula weight | 94760.86 |
| Authors | Catching, A.,Capponi, S.,Andino, R. (deposition date: 2022-08-16, release date: 2023-08-30, Last modification date: 2023-12-06) |
| Primary citation | Catching, A.,Te Yeh, M.,Bianco, S.,Capponi, S.,Andino, R. A tradeoff between enterovirus A71 particle stability and cell entry. Nat Commun, 14:7450-7450, 2023 Cited by PubMed Abstract: A central role of viral capsids is to protect the viral genome from the harsh extracellular environment while facilitating initiation of infection when the virus encounters a target cell. Viruses are thought to have evolved an optimal equilibrium between particle stability and efficiency of cell entry. In this study, we genetically perturb this equilibrium in a non-enveloped virus, enterovirus A71 to determine its structural basis. We isolate a single-point mutation variant with increased particle thermotolerance and decreased efficiency of cell entry. Using cryo-electron microscopy and molecular dynamics simulations, we determine that the thermostable native particles have acquired an expanded conformation that results in a significant increase in protein dynamics. Examining the intermediate states of the thermostable variant reveals a potential pathway for uncoating. We propose a sequential release of the lipid pocket factor, followed by internal VP4 and ultimately the viral RNA. PubMed: 37978288DOI: 10.1038/s41467-023-43029-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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