New Structural Insights into the Genome and Minor Capsid Proteins of BK Polyomavirus using Cryo-Electron Microscopy.
New Structural Insights into the Genome and Minor Capsid Proteins of BK Polyomavirus using Cryo-Electron Microscopy.
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DOI:
10.1016/j.str.2016.02.008
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发表时间:
2016-04-05
期刊:
影响因子:
--
通讯作者:
Ranson NA
中科院分区:
文献类型:
--
作者:
Hurdiss DL;Morgan EL;Thompson RF;Prescott EL;Panou MM;Macdonald A;Ranson NA
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. The first 3D structure of native, infectious, human BK polyomavirus Show the location and extent of the minor capsid proteins Identify contacts between all three structural proteins and the packaged genome Describe structural organization within the viral minichromosome Hurdiss et al. present the first structure of human BK polyomavirus at 7.6 Å and compare it with a VP1-only VLP at similar resolution, providing new insights into the location of minor capsid proteins, genome recognition, and organization of the viral minichromosome.