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- PDB-43mi: Yeast-expressed polio type 3 stabilized virus-like particles -

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Basic information

Entry
Database: PDB / ID: 43mi
TitleYeast-expressed polio type 3 stabilized virus-like particles
Components
  • VP1
  • VP2
  • VP3
KeywordsVIRUS LIKE PARTICLE / Poliovirus type 3 / virus-like particles / stabilized state
Function / homology
Function and homology information


symbiont genome entry into host cell via pore formation in plasma membrane / viral capsid / host cell cytoplasm / symbiont-mediated suppression of host gene expression / virion attachment to host cell / structural molecule activity
Similarity search - Function
Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) / Picornavirus capsid / picornavirus capsid protein / Picornavirus/Calicivirus coat protein / Viral coat protein subunit
Similarity search - Domain/homology
Biological speciesPoliovirus 3
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.87 Å
AuthorsHong, Q. / Cong, Y.
Funding support China, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32130056 China
National Natural Science Foundation of China (NSFC)32570924 China
CitationJournal: Antiviral Res / Year: 2026
Title: High-yield production of immunogenic PV3 virus-like particle in yeast.
Authors: Tian Chen / Qin Hong / Wenyu Han / Shuxia Wang / Cheng Lin / Jiaqi Yao / Chaoyang Lian / Qingwei Liu / Xiaoli Wang / Yanqiu Zhou / Yao Cong / Zhong Huang /
Abstract: The identification of thermally stabilized mutants of all three poliovirus serotypes (PV1, PV2, and PV3) has enabled the development of virus-like particle (VLP)-based next-generation poliovirus ...The identification of thermally stabilized mutants of all three poliovirus serotypes (PV1, PV2, and PV3) has enabled the development of virus-like particle (VLP)-based next-generation poliovirus vaccines. PV3 stabilized mutant-derived VLPs (sVLPs) have been produced in several recombinant systems through co-expression of mutant P1 polyprotein with native or uncleavable viral protease 3CD, and have shown immunogenicity in animal models. However, their yields remain suboptimal, likely because of intrinsic 3CD toxicity and/or inefficient 3CD-mediated cleavage of P1 into capsid subunits VP0, VP3, and VP1, creating a bottleneck for cost-effective product development. In this study, we designed a protease-independent expression strategy based on simultaneous co-expression of VP0, VP3, and VP1 capsid subunit (VP0/VP3/VP1) and compared it with the conventional P1/3CD co-expression approach for production of PV3 sVLP and wildtype VLP (wtVLP) in Pichia pastoris. For each VLP type, the VP0/VP3/VP1 strategy in general enhances target protein expression and D-antigen formation compared with P1/3CD co-expression. The PV3 sVLP produced by the VP0/VP3/VP1 strategy possesses higher levels of D-antigen and significantly enhanced thermostability than the corresponding wtVLP. Moreover, structural and immunological analyses reveal that PV3 sVLP, but not wtVLP, adopts a native conformation and potently elicits neutralizing antibodies in a mouse model. These findings not only confirm yeast-produced PV3 sVLP as a promising vaccine candidate, but also establish a high-yield and scalable expression strategy amenable to further development and industrial-level production of sVLP-based next-generation polio vaccines.
History
DepositionJul 8, 2026Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Sep 16, 2026Provider: repository / Type: Initial release
Revision 1.0Sep 16, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: VP1
C: VP2
D: VP3


Theoretical massNumber of molelcules
Total (without water)90,0673
Polymers90,0673
Non-polymers00
Water00
1
A: VP1
C: VP2
D: VP3
x 60


Theoretical massNumber of molelcules
Total (without water)5,404,012180
Polymers5,404,012180
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation59
MethodUCSF CHIMERA

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Components

#1: Protein VP1


Mass: 33562.785 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Poliovirus 3 / Production host: Komagataella pastoris (fungus) / References: UniProt: Q84895
#2: Protein VP2


Mass: 30188.982 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Poliovirus 3 / Production host: Komagataella pastoris (fungus) / References: UniProt: Q84895
#3: Protein VP3


Mass: 26315.100 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Poliovirus 3 / Production host: Komagataella pastoris (fungus) / References: UniProt: Q84895
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: Poliovirus 3 / Type: VIRUS / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Poliovirus 3
Source (recombinant)Organism: Komagataella pastoris (fungus)
Details of virusEmpty: YES / Enveloped: NO / Isolate: STRAIN / Type: VIRUS-LIKE PARTICLE
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

MicroscopyModel: TFS TALOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k)

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Processing

EM software
IDNameVersionCategory
1crYOLOparticle selection
2PHENIXmodel refinement
13RELION43D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 2.87 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 50980 / Symmetry type: POINT

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