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2016 ; 24
(4
): 528-536
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New Structural Insights into the Genome and Minor Capsid Proteins of BK
Polyomavirus using Cryo-Electron Microscopy
#MMPMID26996963
Hurdiss DL
; Morgan EL
; Thompson RF
; Prescott EL
; Panou MM
; Macdonald A
; Ranson NA
Structure
2016[Apr]; 24
(4
): 528-536
PMID26996963
show ga
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.