Crystal structure of the coat protein of the flexible filamentous papaya mosaic virus.

Crystal structure of the coat protein of the flexible filamentous papaya mosaic virus.
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DOI:
10.1016/j.jmb.2012.05.032
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发表时间:
2012-09-14
影响因子:
5.6
通讯作者:
Li, Huilin
Li, Huilin
中科院分区:
生物学2区
文献类型:
--
作者:
Yang, Shaoqing;Wang, Tao;Bohon, Jen;Gagne, Marie-Eve Laliberte;Bolduc, Marilene;Leclerc, Denis;Li, Huilin

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木瓜花叶病毒(PapMV)是一种丝状植物病毒,属于甲花叶病毒科。柔性丝状病毒在纤维衍射方面已经进行了20多年的研究,目前还没有高分辨率的结构可用于甲流病毒科的任何成员。在这里,我们通过x射线晶体学和低温电镜三维重建报告了PapMV的结构特征。我们发现PapMV的直径为135 Å,每转约有10个亚基的螺旋对称。c端截断的PMV外壳蛋白的晶体结构显示出具有7个α-螺旋的新型全螺旋折叠。因此PMV的CP结构不同于烟草花叶病毒(TMV)的四螺旋束折叠,后者的螺旋束在TMV的亚基界面中占主导地位,并向杆状病毒传递刚性。PapMV外壳蛋白结晶为一个不对称的二聚体,其中一个蛋白通过n端肽捆绑另一个蛋白。对亚基间套索相互作用至关重要的残基的突变取消了外壳蛋白聚合。晶体结构表明PMV可能通过连续n端环套链机制进行聚合。研究了PapMV纳米颗粒的结构,为其合理设计和工程制备新型疫苗提供了理论依据。
Papaya Mosaic Virus (PapMV) is a filamentous plant virus that belongs to the Alphaflexiviridae family. Flexible filamentous viruses have defied more than two decades of effort in fiber diffraction, and no high-resolution structure is available for any member of the Alphaflexiviridae family. Here we report our structural characterization of PapMV by X-ray crystallography and cryo-EM 3D reconstruction. We found that PapMV is 135 Å in diameter with a helical symmetry of ~ 10 subunits per turn. Crystal structure of the C-terminal truncated PMV coat protein reveals a novel all helix fold with seven α-helices. Thus the PMV CP structure is different from the four-helix bundle fold of Tobacco Mosaic Virus (TMV) in which helix bundling dominates the subunit interface in TMV and conveys rigidity to the rod virus. PapMV coat protein was crystallized as an asymmetrical dimer in which one protein lassoes the other by the N-terminal peptide. Mutation of residues critical to the inter-subunit lasso interaction abolishes coat protein polymerization. The crystal structure suggests that PMV may polymerize via the consecutive N-terminal loop lassoing mechanism. The structure of PapMV will be useful for rational design and engineering of the PapMV nanoparticles into innovative vaccines.
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