衣壳
基因组
生物物理学
核心蛋白
体外
DNA
乳腺腺病毒
细胞生物学
化学
腺病毒科
生物
分子生物学
病毒
病毒学
遗传学
基因
重组DNA
作者
Natalia Martín-González,Alfonso Gómez-González,Mercedes Hernando‐Pérez,Michael Bauer,Urs F. Greber,Carmen San Martı́n,Pedro Pablo
出处
期刊:Science Advances
[American Association for the Advancement of Science (AAAS)]
日期:2023-04-07
卷期号:9 (14): eade9910-eade9910
被引量:20
标识
DOI:10.1126/sciadv.ade9910
摘要
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.
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