+Open data
-Basic information
Entry | Database: PDB / ID: 7rwl | ||||||
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Title | Envelope-associated Adeno-associated virus serotype 2 | ||||||
Components | Capsid protein VP1 | ||||||
Keywords | VIRUS / exo-AAV / exosome-associated adeno-associated virus / EA-AAV / Envelope-associated adeno-associated virus | ||||||
Function / homology | Function and homology information permeabilization of host organelle membrane involved in viral entry into host cell / symbiont entry into host cell via permeabilization of inner membrane / host cell nucleolus / T=1 icosahedral viral capsid / clathrin-dependent endocytosis of virus by host cell / virion attachment to host cell / structural molecule activity Similarity search - Function | ||||||
Biological species | Adeno-associated dependoparvovirus A | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.14 Å | ||||||
Authors | Hull, J.A. / Mietzsch, M. / Chipman, P. / Strugatsky, D. / McKenna, R. | ||||||
Funding support | United States, 1items
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Citation | Journal: Virology / Year: 2022 Title: Structural characterization of an envelope-associated adeno-associated virus type 2 capsid. Authors: Joshua A Hull / Mario Mietzsch / Paul Chipman / David Strugatsky / Robert McKenna / Abstract: Adeno-associated virus (AAV) are classified as non-enveloped ssDNA viruses. However, AAV capsids embedded within exosomes have been observed, and it has been suggested that the AAV membrane ...Adeno-associated virus (AAV) are classified as non-enveloped ssDNA viruses. However, AAV capsids embedded within exosomes have been observed, and it has been suggested that the AAV membrane associated accessory protein (MAAP) may play a role in envelope-associated AAV (EA-AAV) capsid formation. Here, we observed and selected sufficient homogeneous EA-AAV capsids of AAV2, produced using the Sf9 baculoviral expression system, to determine the cryo-electron microscopy (cryo-EM) structure at 3.14 Å resolution. The reconstructed map confirmed that the EA-AAV capsid, showed no significant structural variation compared to the non-envelope capsid. In addition, the Sf9 expression system used implies the notion that MAAP may enhance exosome AAV encapsulation. Furthermore, we speculate that these EA-AAV capsids may have therapeutic benefits over the currently used non-envelope AAV capsids, with advantages in immune evasion and/or improved infectivity. | ||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7rwl.cif.gz | 5.7 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7rwl.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 7rwl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7rwl_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 7rwl_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 7rwl_validation.xml.gz | 663.4 KB | Display | |
Data in CIF | 7rwl_validation.cif.gz | 1 MB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rw/7rwl ftp://data.pdbj.org/pub/pdb/validation_reports/rw/7rwl | HTTPS FTP |
-Related structure data
Related structure data | 24718MC 7rwtC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 82031.352 Da / Num. of mol.: 60 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Adeno-associated dependoparvovirus A / Gene: VP1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P03135 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Adeno-associated virus - 2 / Type: VIRUS / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: Adeno-associated virus - 2 |
Source (recombinant) | Organism: Spodoptera frugiperda (fall armyworm) |
Details of virus | Empty: YES / Enveloped: YES / Isolate: SEROTYPE / Type: VIRUS-LIKE PARTICLE |
Virus shell | Triangulation number (T number): 1 |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD |
Image recording | Electron dose: 34 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.16_3549: / Classification: refinement |
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EM software | Name: cisTEM / Version: 1.0.0 / Category: 3D reconstruction |
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
3D reconstruction | Resolution: 3.14 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 291 / Symmetry type: POINT |