Hurdiss Daniel L, Morgan Ethan L, Thompson Rebecca F, Prescott Emma L, Panou Margarita M, Macdonald Andrew, Ranson Neil A
Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Structure. 2016 Apr 5;24(4):528-536. doi: 10.1016/j.str.2016.02.008. Epub 2016 Mar 17.
BK polyomavirus is the causative agent of several diseases in transplant patients and the immunosuppressed. In order to better understand the structure and life cycle of BK, we produced infectious virions and VP1-only virus-like particles in cell culture, and determined their three-dimensional structures using cryo-electron microscopy (EM) and single-particle image processing. The resulting 7.6-Å resolution structure of BK and 9.1-Å resolution of the virus-like particles are the highest-resolution cryo-EM structures of any polyomavirus. These structures confirm that the architecture of the major structural protein components of these human polyomaviruses are similar to previous structures from other hosts, but give new insight into the location and role of the enigmatic minor structural proteins, VP2 and VP3. We also observe two shells of electron density, which we attribute to a structurally ordered part of the viral genome, and discrete contacts between this density and both VP1 and the minor capsid proteins.
BK多瘤病毒是移植患者和免疫抑制人群中多种疾病的病原体。为了更好地了解BK病毒的结构和生命周期，我们在细胞培养中产生了感染性病毒粒子和仅含VP1的病毒样颗粒，并使用冷冻电子显微镜（EM）和单颗粒图像处理技术确定了它们的三维结构。由此获得的BK病毒7.6埃分辨率结构和病毒样颗粒9.1埃分辨率结构是任何多瘤病毒的最高分辨率冷冻电镜结构。这些结构证实，这些人类多瘤病毒主要结构蛋白成分的结构与来自其他宿主的先前结构相似，但对神秘的次要结构蛋白VP2和VP3的位置和作用有了新的认识。我们还观察到两层电子密度壳，我们将其归因于病毒基因组的结构有序部分，以及该密度与VP1和次要衣壳蛋白之间的离散接触。
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