+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-6795 | |||||||||
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Title | CryoEM structure of HPV16 L1-only VLP | |||||||||
Map data | ||||||||||
Sample |
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Biological species | Alphapapillomavirus 9 | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 30.0 Å | |||||||||
Authors | Li ZH / Yan XD / Zheng QB / Gu Y / Li SW | |||||||||
Citation | Journal: Vaccine / Year: 2017 Title: Characterization of an Escherichia coli-derived human papillomavirus type 16 and 18 bivalent vaccine. Authors: Ying Gu / Minxi Wei / Daning Wang / Zhihai Li / Minghui Xie / Huirong Pan / Ting Wu / Jun Zhang / Shaowei Li / Ningshao Xia / Abstract: Human papillomavirus (HPV) types 16 and 18 account for approximately 70% of cervical cancer worldwide. Neutralizing HPV prophylactic vaccines offer significant benefit, as they block HPV infection ...Human papillomavirus (HPV) types 16 and 18 account for approximately 70% of cervical cancer worldwide. Neutralizing HPV prophylactic vaccines offer significant benefit, as they block HPV infection and prevent subsequent disease. However, the three licensed HPV vaccines that cover these two genotypes were produced in eukaryotic cells, which is expensive, particularly for low-income countries where HPV is highest. Here, we report a new HPV16 and -18 bivalent candidate vaccine produced from Escherichia coli. We used two strategies of N-terminal truncation of HPV L1 proteins and soluble non-fusion expression to generate HPV16 and HPV18 L1-only virus-like particles (VLPs) in a scalable process. Through comprehensive characterization of the bivalent candidate vaccine, we confirm lot consistency in a pilot scale-up of 30L, 100L and 500L. Using cryo-EM 3D reconstruction, we found that HPV16 and -18VLPs present in a T=7 icosahedral arrangement, similar in shape and size to that of the native virions. This HPV16/18 bivalent vaccine shares comparable immunogenicity with the licensed vaccines. Overall, we show that the production of a HPV16/18 bivalent vaccine from an E. coli expression system is robust and scalable, with potentially good accessibility worldwide as a population-based immunization strategy. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_6795.map.gz | 9 MB | EMDB map data format | |
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Header (meta data) | emd-6795-v30.xml emd-6795.xml | 7.7 KB 7.7 KB | Display Display | EMDB header |
Images | emd_6795.png | 69.6 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-6795 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-6795 | HTTPS FTP |
-Validation report
Summary document | emd_6795_validation.pdf.gz | 78.5 KB | Display | EMDB validaton report |
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Full document | emd_6795_full_validation.pdf.gz | 77.7 KB | Display | |
Data in XML | emd_6795_validation.xml.gz | 494 B | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6795 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-6795 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_6795.map.gz / Format: CCP4 / Size: 22.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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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
-Sample components
-Entire : Alphapapillomavirus 9
Entire | Name: Alphapapillomavirus 9 |
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Components |
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-Supramolecule #1: Alphapapillomavirus 9
Supramolecule | Name: Alphapapillomavirus 9 / type: virus / ID: 1 / Parent: 0 / NCBI-ID: 337041 / Sci species name: Alphapapillomavirus 9 / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: OTHER / Virus enveloped: No / Virus empty: Yes |
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Host system | Organism: Escherichia coli (E. coli) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.3 |
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Vitrification | Cryogen name: ETHANE |
-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: OTHER / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Tecnai F30 / Image courtesy: FEI Company |
-Image processing
CTF correction | Software - Name: RELION (ver. 1.4) |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 30.0 Å / Resolution method: FSC 0.5 CUT-OFF / Number images used: 400 |
Initial angle assignment | Type: COMMON LINE |
Final angle assignment | Type: COMMON LINE |