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-Structure paper
タイトル | A tradeoff between enterovirus A71 particle stability and cell entry. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 7450, Year 2023 |
掲載日 | 2023年11月17日 |
著者 | Adam Catching / Ming Te Yeh / Simone Bianco / Sara Capponi / Raul Andino / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:37978288 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.1 - 14.0 Å |
構造データ | EMDB-27850, PDB-8e2x: EMDB-27851, PDB-8e2y: EMDB-27853, PDB-8e31: EMDB-27859, PDB-8e38: EMDB-27860, PDB-8e39: EMDB-27861, PDB-8e3a: EMDB-27862, PDB-8e3b: EMDB-27863, PDB-8e3c: |
化合物 | ChemComp-SPH: |
由来 |
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キーワード | VIRUS / enterovirus / thermostability / capsid |