CPV 的原子模型揭示了这种单壳病毒在经济上执行多壳呼肠孤病毒中保守功能的机制。
Atomic model of CPV reveals the mechanism used by this single-shelled virus to economically carry out functions conserved in multishelled reoviruses.
机构信息
Department of Microbiology, Immunology and Molecular Genetics, University of California, Los Angeles, Los Angeles, CA 90095-7364, USA.
出版信息
Structure. 2011 May 11;19(5):652-61. doi: 10.1016/j.str.2011.03.003.
Unlike the multishelled viruses in the Reoviridae, cytoplasmic polyhedrosis virus (CPV) is single shelled, yet stable and fully capable of carrying out functions conserved within Reoviridae. Here, we report a 3.1 Å resolution cryo electron microscopy structure of CPV and derive its atomic model, consisting of 60 turret proteins (TPs), 120 each of capsid shell proteins (CSPs) and large protrusion proteins (LPPs). Two unique segments of CSP contribute to CPV's stability: an inserted protrusion domain interacting with neighboring proteins, and an N-anchor tying up CSPs together through strong interactions such as β sheet augmentation. Without the need to interact with outer shell proteins, LPP retains only the N-terminal two-third region containing a conserved helix-barrel core and interacts exclusively with CSP. TP is also simplified, containing only domains involved in RNA capping. Our results illustrate how CPV proteins have evolved in a coordinative manner to economically carry out their conserved functions.
不同于呼肠孤病毒科的多壳病毒，质型多角体病毒（CPV）为单壳结构，但却稳定且完全能够行使呼肠孤病毒科所保守的功能。在此，我们报道了 CPV 的 3.1 Å 分辨率冷冻电镜结构，并推导出其原子模型，由 60 个转塔蛋白（TP）、120 个衣壳壳蛋白（CSP）和 120 个大突起蛋白（LPP）组成。CSP 的两个独特片段有助于 CPV 的稳定性：插入的突起结构域与相邻蛋白相互作用，N-锚通过β片层增强等强相互作用将 CSP 系在一起。LPP 无需与外壳蛋白相互作用，仅保留含有保守螺旋-桶核心的 N 端三分之二区域，并与 CSP 特异性相互作用。TP 也被简化，仅包含涉及 RNA 加帽的结构域。我们的结果说明了 CPV 蛋白如何以协调的方式进化，以经济有效地行使其保守功能。
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