Departament of Condensed Matter Physics, Universidad Autónoma de Madrid and Institute of Condensed Matter Physics (IFIMAC), 28049 Madrid, Spain.
Department of Molecular Life Sciences, University of Zurich, CH-8057 Zurich, Switzerland.
Sci Adv. 2023 Apr 7;9(14):eade9910. doi: 10.1126/sciadv.ade9910.
Out of the three core proteins in human adenovirus, protein V is believed to connect the inner capsid surface to the outer genome layer. Here, we explored mechanical properties and in vitro disassembly of particles lacking protein V (Ad5-ΔV). Ad5-ΔV particles were softer and less brittle than the wild-type ones (Ad5-wt), but they were more prone to release pentons under mechanical fatigue. In Ad5-ΔV, core components did not readily diffuse out of partially disrupted capsids, and the core appeared more condensed than in Ad5-wt. These observations suggest that instead of condensing the genome, protein V antagonizes the condensing action of the other core proteins. Protein V provides mechanical reinforcement and facilitates genome release by keeping DNA connected to capsid fragments that detach during disruption. This scenario is in line with the location of protein V in the virion and its role in Ad5 cell entry.
在人类腺病毒的三种核心蛋白中，蛋白 V 被认为将内壳表面与外壳层的基因组连接起来。在这里，我们探索了缺乏蛋白 V（Ad5-ΔV）的颗粒的机械性能和体外解体。与野生型（Ad5-wt）相比，Ad5-ΔV 颗粒更柔软，更不易脆，但在机械疲劳下更容易释放五邻体。在 Ad5-ΔV 中，核心成分不易从部分破坏的衣壳中扩散出来，并且核心比 Ad5-wt 更浓缩。这些观察结果表明，蛋白 V 没有使基因组浓缩，而是拮抗了其他核心蛋白的浓缩作用。蛋白 V 通过将 DNA 连接到在破坏过程中分离的衣壳片段上，提供机械加固并促进基因组的释放。这种情况与蛋白 V 在病毒粒子中的位置及其在 Ad5 细胞进入中的作用一致。
