T=7 icosahedral viral capsid / endocytosis involved in viral entry into host cell / host cell nucleus / virion attachment to host cell / structural molecule activity Similarity search - Function
Major capsid L1 (late) protein, Papillomavirus / Major capsid L1 (late) superfamily, Papillomavirus / L1 (late) protein / Double-stranded DNA virus, group I, capsid Similarity search - Domain/homology
National Institutes of Health/Office of the Director
S10 OD026822-01
United States
National Institutes of Health/Office of the Director
Al134910-01A1
United States
Citation
Journal: Viruses / Year: 2021 Title: Cryo EM Analysis Reveals Inherent Flexibility of Authentic Murine Papillomavirus Capsids. Authors: Samantha R Hartmann / Daniel J Goetschius / Jiafen Hu / Joshua J Graff / Carol M Bator / Neil D Christensen / Susan L Hafenstein / Abstract: Human papillomavirus (HPV) is a significant health burden and leading cause of virus-induced cancers. However, studies have been hampered due to restricted tropism that makes production and ...Human papillomavirus (HPV) is a significant health burden and leading cause of virus-induced cancers. However, studies have been hampered due to restricted tropism that makes production and purification of high titer virus problematic. This issue has been overcome by developing alternative HPV production methods such as virus-like particles (VLPs), which are devoid of a native viral genome. Structural studies have been limited in resolution due to the heterogeneity, fragility, and stability of the VLP capsids. The mouse papillomavirus (MmuPV1) presented here has provided the opportunity to study a native papillomavirus in the context of a common laboratory animal. Using cryo EM to solve the structure of MmuPV1, we achieved 3.3 Å resolution with a local symmetry refinement method that defined smaller, symmetry related subparticles. The resulting high-resolution structure allowed us to build the MmuPV1 asymmetric unit for the first time and identify putative L2 density. We also used our program ISECC to quantify capsid flexibility, which revealed that capsomers move as rigid bodies connected by flexible linkers. The MmuPV1 flexibility was comparable to that of a HPV VLP previously characterized. The resulting MmuPV1 structure is a promising step forward in the study of papillomavirus and will provide a framework for continuing biochemical, genetic, and biophysical research for papillomaviruses.
#200 - Aug 2016 Quasisymmetry in Icosahedral Viruses similarity (2)
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Assembly
Deposited unit
A: Major capsid protein L1 B: Major capsid protein L1 C: Major capsid protein L1 D: Major capsid protein L1 E: Major capsid protein L1 F: Major capsid protein L1
A: Major capsid protein L1 B: Major capsid protein L1 C: Major capsid protein L1 D: Major capsid protein L1 E: Major capsid protein L1 F: Major capsid protein L1
A: Major capsid protein L1 B: Major capsid protein L1 C: Major capsid protein L1 D: Major capsid protein L1 E: Major capsid protein L1 F: Major capsid protein L1
x 5
icosahedral pentamer
1.73 MDa, 30 polymers
Theoretical mass
Number of molelcules
Total (without water)
1,728,706
30
Polymers
1,728,706
30
Non-polymers
0
0
Water
0
Type
Name
Symmetry operation
Number
identity operation
1_555
x,y,z
1
point symmetry operation
4
4
A: Major capsid protein L1 B: Major capsid protein L1 C: Major capsid protein L1 D: Major capsid protein L1 E: Major capsid protein L1 F: Major capsid protein L1
x 6
icosahedral 23 hexamer
2.07 MDa, 36 polymers
Theoretical mass
Number of molelcules
Total (without water)
2,074,448
36
Polymers
2,074,448
36
Non-polymers
0
0
Water
0
Type
Name
Symmetry operation
Number
identity operation
1_555
x,y,z
1
point symmetry operation
5
5
Idetical with deposited unit
icosahedral asymmetric unit, std point frame
Type
Name
Symmetry operation
Number
identity operation
1_555
x,y,z
1
Symmetry
Point symmetry: (Schoenflies symbol: I (icosahedral))
-
Components
#1: Protein
MajorcapsidproteinL1
Mass: 57623.543 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) Mus musculus papillomavirus type 1 / References: UniProt: A0A2D3I4N0
-
Experimental details
-
Experiment
Experiment
Method: ELECTRON MICROSCOPY
EM experiment
Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction
Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K
-
Electron microscopy imaging
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
Microscopy
Model: FEI TITAN KRIOS
Electron gun
Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lens
Mode: BRIGHT FIELD / Cs: 0.01 mm
Specimen holder
Cryogen: NITROGEN
Image recording
Electron dose: 45 e/Å2 / Detector mode: COUNTING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 2859
-
Processing
EM software
ID
Name
Version
Category
Details
1
cryoSPARC
2.8.3
particleselection
Templatepickerfrommanualpicks
4
cryoSPARC
2.8.3
CTFcorrection
CTFFIND4
CTF correction
Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Particle selection
Num. of particles selected: 10181
Symmetry
Point symmetry: I (icosahedral)
3D reconstruction
Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 10181 / Symmetry type: POINT
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