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- PDB-8ach: Nudaurelia capensis omega virus maturation intermediate captured ... -

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Basic information

Entry
Database: PDB / ID: 8ach
TitleNudaurelia capensis omega virus maturation intermediate captured at pH5.6 (insect cell expressed VLPs): large class from symmetry expansion
Componentsp70
KeywordsVIRUS LIKE PARTICLE / ICOSAHEDRAL VIRUS / AUTO-CATALYTIC CLEAVAGE / VIRUS MATURATION / VIRUS-LIKE PARTICLE
Function / homologyPeptidase N2 / Peptidase family A21 / virion component / Viral coat protein subunit / p70
Function and homology information
Biological speciesNudaurelia capensis omega virus
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.91 Å
AuthorsCastells-Graells, R. / Hesketh, E.L. / Johnson, J.E. / Ranson, N.A. / Lawson, D.M. / Lomonossoff, G.P.
Funding support United Kingdom, 3items
OrganizationGrant numberCountry
Biotechnology and Biological Sciences Research Council (BBSRC)BB/L014130/1 United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)BBS/E/J/000PR9794 United Kingdom
Wellcome Trust108466/Z/15/Z United Kingdom
CitationJournal: Proc Natl Acad Sci U S A / Year: 2026
Title: Unraveling the maturation pathway of a eukaryotic virus through cryo-EM.
Authors: Roger Castells-Graells / Emma L Hesketh / Tsutomu Matsui / John E Johnson / Neil A Ranson / David M Lawson / George P Lomonossoff /
Abstract: Virus maturation is a fundamental biological process involving large-scale structural reorganizations that drive functional activation and lead to infectivity. Understanding the steps from the ...Virus maturation is a fundamental biological process involving large-scale structural reorganizations that drive functional activation and lead to infectivity. Understanding the steps from the initial procapsid assembly to mature virions is essential, both for comprehending viral life cycles and for developing antiviral therapies. However, capturing these steps has been challenging due to the transient and elusive nature of intermediate states. The nonenveloped, T = 4, ssRNA-containing, omega virus (NωV) is a highly accessible model system that exemplifies the maturation process of a eukaryotic virus. During maturation, the particle shrinks in outer diameter from 482 Å (pH 7.6) to 428 Å (pH 5.0). It is possible to mimic the maturation process in vitro by lowering the pH of a population of procapsids produced in heterologous systems. Indeed, by controlling the pH in vitro, it is possible to produce homogenous populations of intermediate NωV virus-like particles (VLPs) that occur too fleetingly to be observed in vivo. Here, we report structural models, based on cryoelectron microscopy (cryo-EM), of five intermediates in the NωV maturation process. The structures of the intermediate particles reveal unique, quaternary position-dependent trajectories and refolding of subunit N and C-terminal regions, including the formation of the autocatalytic cleavage site at N570. The detailed structures reported here, coupled with previously determined structures of the procapsids and mature particles, allow the maturation pathway to be described in detail for a eukaryotic virus.
History
DepositionJul 5, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 28, 2022Provider: repository / Type: Initial release
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Revision 1.0Dec 28, 2022Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
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Revision 1.1Jul 24, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / em_3d_fitting_list / em_admin
Item: _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id ..._em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type / _em_admin.last_update
Revision 1.2Mar 18, 2026Group: Data collection / Database references / Structure summary
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Revision 1.1Mar 18, 2026Data content type: EM metadata / Data content type: EM metadata / EM metadata / Group: Database references / Experimental summary / Data content type: EM metadata / EM metadata / EM metadata / Category: citation / citation_author / em_admin
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: p70
B: p70
C: p70
D: p70


Theoretical massNumber of molelcules
Total (without water)279,5684
Polymers279,5684
Non-polymers00
Water00
1
A: p70
B: p70
C: p70
D: p70
x 60


Theoretical massNumber of molelcules
Total (without water)16,774,069240
Polymers16,774,069240
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_5551
point symmetry operation59

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Components

#1: Protein
p70


Mass: 69891.953 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Nudaurelia capensis omega virus / Cell (production host): Sf21 cell line / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q4TVS9
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Nudaurelia capensis omega virus / Type: VIRUS / Details: expressed in Spodoptera frugiperda Sf21 cells / Entity ID: all / Source: RECOMBINANT
Molecular weightValue: 16.76 MDa / Experimental value: NO
Source (natural)Organism: Nudaurelia capensis omega virus
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm) / Cell: Sf21
Details of virusEmpty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRUS-LIKE PARTICLE
Natural hostOrganism: Gonimbrasia cytherea
Virus shellName: coat / Diameter: 430 nm / Triangulation number (T number): 4
Buffer solutionpH: 5.6 / Details: NULL
SpecimenConc.: 0.3 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES / Details: NULL
Specimen supportGrid material: COPPER / Grid mesh size: 400 divisions/in.
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 75000 X / Nominal defocus max: 2500 nm / Nominal defocus min: 800 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm
Specimen holderCryogen: NITROGEN
Image recordingAverage exposure time: 1 sec. / Electron dose: 49.1 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) / Num. of grids imaged: 2 / Num. of real images: 16478
Details: Reconstructed from 2 datasets collected at doses of 48.7 and 50.4 electrons per Angstrom squared, respectively. The average of these two values is given.

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Processing

EM software
IDNameVersionCategory
1RELION3.0.3particle selection
2EPUimage acquisition
4Gctf1.06CTF correction
7UCSF Chimera1.14model fitting
8Coot0.9model fitting
10RELION3.0.3initial Euler assignment
11RELION3.0.3final Euler assignment
12RELION3.0.3classification
13RELION3.0.33D reconstruction
14PHENIX1.20rc4model refinement
Image processingDetails: NULL
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C1 (asymmetric)
3D reconstructionResolution: 3.91 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 96960
Details: Particles from an I1 icosahedral consensus map (EMD-15266) were symmetry expanded to C1 and further 3D classified without alignment using a soft mask covering the icosahedral asymmetric unit. ...Details: Particles from an I1 icosahedral consensus map (EMD-15266) were symmetry expanded to C1 and further 3D classified without alignment using a soft mask covering the icosahedral asymmetric unit. The particles for this class were randomly split into half sets for the subsequent reconstruction and postprocessing steps. Note that the symmetry expansion step generates a 60-fold larger particle stack.
Symmetry type: POINT
Atomic model buildingB value: 161 / Protocol: OTHER / Space: REAL / Target criteria: Correlation coefficient
Atomic model buildingPDB-ID: 8AC6

8ac6


Accession code: 8AC6 / Source name: PDB / Type: experimental model

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