Integrin and Defensin Modulate the Mechanical Properties of Adenovirus
Integrin and Defensin Modulate the Mechanical Properties of Adenovirus
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DOI：
10.1128/jvi.02516-12
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发表时间：
2013-03-01
影响因子：
5.4
通讯作者：
Wuite, Gijs J. L.
中科院分区：
文献类型：
--
作者：
Snijder, Joost;Reddy, Vijay S.;Wuite, Gijs J. L.
人腺病毒衣壳解体和脱壳的倾向通过与宿主细胞分子如整合素和α防御素的相互作用来调节。在这里，我们使用原子力显微镜（AFM）纳米压痕来阐明，在单颗粒水平上，这些宿主分子的结合影响病毒颗粒弹性的机制。我们的研究结果表明，整合素或防御素的结合和病毒的机械性能之间的直接联系。我们发现，腺病毒的结构和几何形状的结果在一个各向异性的弹性响应，涉及到二十面体对称。这种弹性响应在结合宿主分子时发生变化。尽管整合素结合软化顶点区域，但人α防御素的结合具有完全相反的效果。我们的研究结果表明，这些宿主分子的能力，影响腺病毒拆卸相关的五邻体区域的弹性强度的直接影响。因此，影响腺病毒感染性的宿主因素调节衣壳的弹性。我们的发现揭示了病毒-宿主相互作用和衣壳机制之间的直接联系。
The propensity for capsid disassembly and uncoating of human adenovirus is modulated by interactions with host cell molecules like integrins and alpha defensins. Here, we use atomic force microscopy (AFM) nanoindentation to elucidate, at the single-particle level, the mechanism by which binding of these host molecules affects virus particle elasticity. Our results demonstrate the direct link between integrin or defensin binding and the mechanical properties of the virus. We show that the structure and geometry of adenovirus result in an anisotropic elastic response that relates to icosahedral symmetry. This elastic response changes upon binding host molecules. Whereas integrin binding softens the vertex regions, binding of a human alpha defensin has exactly the opposite effect. Our results reveal that the ability of these host molecules to influence adenovirus disassembly correlates with a direct effect on the elastic strength of the penton region. Host factors that influence adenovirus infectivity thus modulate the elastic properties of the capsid. Our findings reveal a direct link between virus-host interactions and capsid mechanics.