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- PDB-7zq8: VelcroVax tandem HBcAg with SUMO-Affimer inserted at MIR (T=4 VLP) -

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Entry
Database: PDB / ID: 7zq8
TitleVelcroVax tandem HBcAg with SUMO-Affimer inserted at MIR (T=4 VLP)
ComponentsVelcroVax tandem HBcAg with SUMO-Affimer inserted at MIR
KeywordsVIRUS LIKE PARTICLE / VelcroVax / Hepatitis B virus / Hepatitis B core antigen / Affimer / Vaccine / Recombinant / VLP / Antigen display
Biological speciessynthetic construct (others)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsKingston, N.J. / Grehan, K. / Snowden, J.S. / Alzahrani, J. / Ranson, N.A. / Rowlands, D.J. / Stonehouse, N.J.
Funding support United Kingdom, United States, 4items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MR/P022626/1 United Kingdom
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI 169457-0 United States
Wellcome Trust204825/Z/16/Z United Kingdom
Wellcome Trust102174/B/13/Z United Kingdom
CitationJournal: mSphere / Year: 2023
Title: VelcroVax: a "Bolt-On" Vaccine Platform for Glycoprotein Display.
Authors: Natalie J Kingston / Keith Grehan / Joseph S Snowden / Mark Hassall / Jehad Alzahrani / Guido C Paesen / Lee Sherry / Connor Hayward / Amy Roe / Sam Stephen / Darren Tomlinson / Antra ...Authors: Natalie J Kingston / Keith Grehan / Joseph S Snowden / Mark Hassall / Jehad Alzahrani / Guido C Paesen / Lee Sherry / Connor Hayward / Amy Roe / Sam Stephen / Darren Tomlinson / Antra Zeltina / Katie J Doores / Neil A Ranson / Martin Stacey / Mark Page / Nicola J Rose / Thomas A Bowden / David J Rowlands / Nicola J Stonehouse /
Abstract: Having varied approaches to the design and manufacture of vaccines is critical in being able to respond to worldwide needs and newly emerging pathogens. Virus-like particles (VLPs) form the basis of ...Having varied approaches to the design and manufacture of vaccines is critical in being able to respond to worldwide needs and newly emerging pathogens. Virus-like particles (VLPs) form the basis of two of the most successful licensed vaccines (against hepatitis B virus [HBV] and human papillomavirus). They are produced by recombinant expression of viral structural proteins, which assemble into immunogenic nanoparticles. VLPs can be modified to present unrelated antigens, and here we describe a universal "bolt-on" platform (termed VelcroVax) where the capturing VLP and the target antigen are produced separately. We utilize a modified HBV core (HBcAg) VLP with surface expression of a high-affinity binding sequence (Affimer) directed against a SUMO tag and use this to capture SUMO-tagged gp1 glycoprotein from the arenavirus Junín virus (JUNV). Using this model system, we have solved the first high-resolution structures of VelcroVax VLPs and shown that the VelcroVax-JUNV gp1 complex induces superior humoral immune responses compared to the noncomplexed viral protein. We propose that this system could be modified to present a range of antigens and therefore form the foundation of future rapid-response vaccination strategies. The hepatitis B core protein (HBc) forms noninfectious virus-like particles, which can be modified to present a capturing molecule, allowing suitably tagged antigens to be bound on their surface. This system can be adapted and provides the foundation for a universal "bolt-on" vaccine platform (termed VelcroVax) that can be easily and rapidly modified to generate nanoparticle vaccine candidates.
History
DepositionApr 29, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 18, 2023Provider: repository / Type: Initial release
Revision 1.1Aug 9, 2023Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.2Oct 9, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / em_admin / pdbx_entry_details / pdbx_modification_feature
Item: _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: VelcroVax tandem HBcAg with SUMO-Affimer inserted at MIR
B: VelcroVax tandem HBcAg with SUMO-Affimer inserted at MIR


Theoretical massNumber of molelcules
Total (without water)105,5862
Polymers105,5862
Non-polymers00
Water00
1
A: VelcroVax tandem HBcAg with SUMO-Affimer inserted at MIR
B: VelcroVax tandem HBcAg with SUMO-Affimer inserted at MIR
x 60


Theoretical massNumber of molelcules
Total (without water)6,335,132120
Polymers6,335,132120
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation59

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Components

#1: Protein VelcroVax tandem HBcAg with SUMO-Affimer inserted at MIR


Mass: 52792.770 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: Komagataella phaffii (fungus)
Has protein modificationY

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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: T=4 virus-like particle for VelcroVax tandem HBcAg with SUMO-Affimer inserted at MIR
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: synthetic construct (others)
Source (recombinant)Organism: Komagataella phaffii (fungus)
Buffer solutionpH: 7.4
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen 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 defocus max: 3000 nm / Nominal defocus min: 800 nm
Image recordingElectron dose: 60.1 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: I (icosahedral)
3D reconstructionResolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 49489 / Symmetry type: POINT

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