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Yorodumi- PDB-9wmq: The cryo-electron microscopy complex structure of PCV3 VLPs and a... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9wmq | ||||||||||||||||||||||||
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| Title | The cryo-electron microscopy complex structure of PCV3 VLPs and antibody 2B5 | ||||||||||||||||||||||||
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Keywords | VIRUS LIKE PARTICLE/IMMUNE SYSTEM / Porcine circovirus 3 / Cryo-EM / PCV3 VLP / Immunocomplexes / VIRUS LIKE PARTICLE-IMMUNE SYSTEM complex | ||||||||||||||||||||||||
| Function / homology | Function and homology informationviral capsid assembly / T=1 icosahedral viral capsid / viral penetration into host nucleus / host cell / endocytosis involved in viral entry into host cell / virion attachment to host cell / host cell nucleus / DNA binding Similarity search - Function | ||||||||||||||||||||||||
| Biological species | Porcine circovirus 3![]() | ||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 1.73 Å | ||||||||||||||||||||||||
Authors | Su, J. / Jiang, Y. / Li, S. / Zheng, Q. | ||||||||||||||||||||||||
| Funding support | 1items
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Citation | Journal: Nat Commun / Year: 2026Title: Structural basis and immunogenic efficacy of porcine circovirus type 3 virus-like particle. Authors: Jinfu Su / Xiaodan Tong / Yanan Jiang / Yu Li / He Yan / Yan Liu / Yanwei Wang / Xiaorui Su / Zhe Sun / Mengyue Wang / Ningshao Xia / Mihnea Bostina / Shaowei Li / Wenqiang Pang / Qingbing ...Authors: Jinfu Su / Xiaodan Tong / Yanan Jiang / Yu Li / He Yan / Yan Liu / Yanwei Wang / Xiaorui Su / Zhe Sun / Mengyue Wang / Ningshao Xia / Mihnea Bostina / Shaowei Li / Wenqiang Pang / Qingbing Zheng / Kegong Tian / ![]() Abstract: Porcine circovirus type 3 (PCV3) is an emerging swine pathogen associated with reproductive failure and systemic inflammation, but vaccines for related PCV2 provide limited cross-protection. Here, we ...Porcine circovirus type 3 (PCV3) is an emerging swine pathogen associated with reproductive failure and systemic inflammation, but vaccines for related PCV2 provide limited cross-protection. Here, we determine high-resolution cryo-EM structures of PCV3 capsid protein assembled into virus-like particles (VLPs) and of PCV3 VLPs bound to the PCV3-specific antibody 2B5. The structures reveal differences from PCV2 in surface loops and define a conserved 2B5 epitope mainly involving the BC, EF and HI loops, providing a structural basis for PCV3-specific recognition. PCV3 VLPs induce sustained antibody responses in mice and pigs. In a pig challenge model, VLP immunization prevents viremia and viral replication in lungs and lymph nodes, as measured by quantitative PCR and in situ hybridization, with protection maintained for at least five months after boosting. These findings support PCV3 VLPs as a vaccine candidate against PCV3 infection. | ||||||||||||||||||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9wmq.cif.gz | 53.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9wmq.ent.gz | 35.8 KB | Display | PDB format |
| PDBx/mmJSON format | 9wmq.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wm/9wmq ftp://data.pdbj.org/pub/pdb/validation_reports/wm/9wmq | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 66101MC ![]() 9wmrC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 21000.908 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Porcine circovirus 3 / Gene: ORF2 / Production host: Baculovirus expression vector pFastBac1-HM / References: UniProt: A0A6B9EZK0 |
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| #2: Antibody | Mass: 13576.949 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Due to patent protection, we only provide the CDR regions of the antibody that are involved in key interactions. Source: (natural) ![]() |
| #3: Antibody | Mass: 11364.478 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: Due to patent protection, we only provide the CDR regions of the antibody that are involved in key interactions. Source: (natural) ![]() |
| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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| Source (natural) |
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| Source (recombinant) | Organism: Baculovirus expression vector pFastBac1-HM | ||||||||||||||||||||||||
| Buffer solution | pH: 7 | ||||||||||||||||||||||||
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: OTHER / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1568 nm / Nominal defocus min: 300 nm |
| Image recording | Electron dose: 48 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||
| 3D reconstruction | Resolution: 1.73 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 197071 / Symmetry type: POINT |
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Porcine circovirus 3

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