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Open data
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Basic information
| Entry | Database: EMDB / ID: EMD-6798 | |||||||||
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| Title | CryoEM structure of HPV11 L1-only VLP | |||||||||
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Sample |
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| Biological species | Human papillomavirus type 11 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 20.0 Å | |||||||||
Authors | Li SW | |||||||||
Citation | Journal: Vaccine / Year: 2017Title: Bacterially expressed human papillomavirus type 6 and 11 bivalent vaccine: Characterization, antigenicity and immunogenicity. Authors: Huirong Pan / Zhihai Li / Jin Wang / Shuo Song / Daning Wang / Minxi Wei / Ying Gu / Jun Zhang / Shaowei Li / Ningshao Xia / ![]() Abstract: Human papillomavirus (HPV)-6 and HPV11 are the major etiological causes of condylomata acuminate. HPV neutralization by vaccine-elicited neutralizing antibodies can block viral infection and prevent ...Human papillomavirus (HPV)-6 and HPV11 are the major etiological causes of condylomata acuminate. HPV neutralization by vaccine-elicited neutralizing antibodies can block viral infection and prevent subsequent disease. Currently, two commercially available HPV vaccines cover these two genotypes, expressed by Saccharomyces cerevisiae. Here we describe another HPV6/11 bivalent vaccine candidate derived from Escherichia coli. The soluble expression of N-terminally truncated L1 proteins was optimized to generate HPV6- and HPV11 L1-only virus-like particles (VLPs) as a scalable process. In a pilot scale, we used various biochemical, biophysical and immunochemical approaches to comprehensively characterize the scale and lot consistency of the vaccine candidate at 30L and 100L. Cryo-EM structure analysis showed that these VLPs form a T=7 icosahedral lattice, imitating the L1 capsid of the authentic HPV virion. This HPV6/11 bivalent vaccine confers a neutralization titer and antibody production profile in monkey that is comparable with the quadrivalent vaccine, Gardasil. This study demonstrates the robustness and scalability of a potential HPV6/11 bivalent vaccine using a prokaryotic system for vaccine production. | |||||||||
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Structure visualization
| Movie |
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| Structure viewer | EM map: SurfView Molmil Jmol/JSmol |
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_6798.map.gz | 12.2 MB | EMDB map data format | |
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| Header (meta data) | emd-6798-v30.xml emd-6798.xml | 7.3 KB 7.3 KB | Display Display | EMDB header |
| Images | emd_6798.png | 120.6 KB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-6798 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-6798 | HTTPS FTP |
-Validation report
| Summary document | emd_6798_validation.pdf.gz | 77.2 KB | Display | EMDB validaton report |
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| Full document | emd_6798_full_validation.pdf.gz | 76.3 KB | Display | |
| Data in XML | emd_6798_validation.xml.gz | 494 B | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6798 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6798 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_6798.map.gz / Format: CCP4 / Size: 22.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 4.44 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Human papillomavirus type 11
| Entire | Name: Human papillomavirus type 11 |
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| Components |
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-Supramolecule #1: Human papillomavirus type 11
| Supramolecule | Name: Human papillomavirus type 11 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 10580 / Sci species name: Human papillomavirus type 11 / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: OTHER / Virus enveloped: No / Virus empty: Yes |
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| Host system | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 6.5 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TECNAI F30 |
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| Image recording | Film or detector model: FEI FALCON I (4k x 4k) / Average electron dose: 25.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
| Experimental equipment | ![]() Model: Tecnai F30 / Image courtesy: FEI Company |
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Image processing
| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 20.0 Å / Resolution method: FSC 0.5 CUT-OFF / Number images used: 536 |
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| Initial angle assignment | Type: COMMON LINE |
| Final angle assignment | Type: COMMON LINE |
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