8E3A

Purification of Enterovirus A71, strain 4643, WT capsid

Summary for 8E3A

• Entry DOI: 10.2210/pdb8e3a/pdb
• EMDB information: 27861
• Descriptor: VP1, VP2, VP3, ... (4 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: 94461.37

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

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: 37978288
DOI: 10.1038/s41467-023-43029-0

Experimental method

ELECTRON MICROSCOPY (7.4 Å)