National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
R01 AI056346
United States
National Natural Science Foundation of China (NSFC)
313290002
China
National Institutes of Health/National Center for Research Resources (NIH/NCRR)
1S10RR23057
United States
China Academy of Sciences
XDB02050000
China
National Science Foundation (NSF, United States)
DBI-1338135
United States
Citation
Journal: J Gen Virol / Year: 2017 Title: A pUL25 dimer interfaces the pseudorabies virus capsid and tegument. Authors: Yun-Tao Liu / Jiansen Jiang / Kevin Patrick Bohannon / Xinghong Dai / G W Gant Luxton / Wong Hoi Hui / Guo-Qiang Bi / Gregory Allan Smith / Z Hong Zhou / Abstract: Inside the virions of α-herpesviruses, tegument protein pUL25 anchors the tegument to capsid vertices through direct interactions with tegument proteins pUL17 and pUL36. In addition to promoting ...Inside the virions of α-herpesviruses, tegument protein pUL25 anchors the tegument to capsid vertices through direct interactions with tegument proteins pUL17 and pUL36. In addition to promoting virion assembly, both pUL25 and pUL36 are critical for intracellular microtubule-dependent capsid transport. Despite these essential roles during infection, the stoichiometry and precise organization of pUL25 and pUL36 on the capsid surface remain controversial due to the insufficient resolution of existing reconstructions from cryo-electron microscopy (cryoEM). Here, we report a three-dimensional (3D) icosahedral reconstruction of pseudorabies virus (PRV), a varicellovirus of the α-herpesvirinae subfamily, obtained by electron-counting cryoEM at 4.9 Å resolution. Our reconstruction resolves a dimer of pUL25 forming a capsid-associated tegument complex with pUL36 and pUL17 through a coiled coil helix bundle, thus correcting previous misinterpretations. A comparison between reconstructions of PRV and the γ-herpesvirus Kaposi's sarcoma-associated herpesvirus (KSHV) reinforces their similar architectures and establishes important subfamily differences in the capsid-tegument interface.
History
Deposition
Jun 8, 2017
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Header (metadata) release
Jul 19, 2017
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Map release
Nov 1, 2017
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Update
Dec 25, 2019
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Current status
Dec 25, 2019
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Shell ID: 1 / Name: Capsid / Diameter: 1250.0 Å / T number (triangulation number): 16
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Experimental details
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Structure determination
Method
cryo EM
Processing
single particle reconstruction
Aggregation state
particle
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Sample preparation
Buffer
pH: 7
Vitrification
Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV
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Electron microscopy
Microscope
FEI TITAN KRIOS
Image recording
Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Frames/image: 2-25 / Number real images: 1830 / Average electron dose: 18.0 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Type of model: INSILICO MODEL In silico model: The particles were processed using EMAN for initial 3D reconstruction and refinement with icosahedral symmetry enforced.
Final reconstruction
Applied symmetry - Point group: I (icosahedral) / Resolution.type: BY AUTHOR / Resolution: 4.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 13537
Initial angle assignment
Type: NOT APPLICABLE
Final angle assignment
Type: NOT APPLICABLE
FSC plot (resolution estimation)
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Atomic model buiding 1
Refinement
Protocol: RIGID BODY FIT
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