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Open data
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Basic information
| Entry | ![]() | |||||||||
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| Title | Structure of AAV8 in the complex of AAV8 with its receptor | |||||||||
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Keywords | AAV8 / virus / complex | |||||||||
| Function / homology | Function and homology informationT=1 icosahedral viral capsid / nucleotide binding / structural molecule activity Similarity search - Function | |||||||||
| Biological species | Adeno-associated virus - 8 / adeno-associated virus 8 | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 2.32 Å | |||||||||
Authors | Xu H / Wang GP / Su XD | |||||||||
| Funding support | China, 1 items
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Citation | Journal: Cell / Year: 2025Title: An alternate receptor for adeno-associated viruses. Authors: Bijay P Dhungel / Hua Xu / Rajini Nagarajah / Joseph Vitale / Alex C H Wong / Divya Gokal / Yue Feng / Mehdi Sharifi Tabar / Cynthia Metierre / Chirag Parsania / Xiaohui Song / Guopeng Wang ...Authors: Bijay P Dhungel / Hua Xu / Rajini Nagarajah / Joseph Vitale / Alex C H Wong / Divya Gokal / Yue Feng / Mehdi Sharifi Tabar / Cynthia Metierre / Chirag Parsania / Xiaohui Song / Guopeng Wang / Xiao-Dong Su / Charles G Bailey / John E J Rasko / ![]() Abstract: Systemic gene therapy using adeno-associated virus (AAV) vectors is approved for the treatment of several genetic disorders, but challenges and toxicities associated with high vector doses remain. We ...Systemic gene therapy using adeno-associated virus (AAV) vectors is approved for the treatment of several genetic disorders, but challenges and toxicities associated with high vector doses remain. We report an alternate receptor for AAV (AAVR2, carboxypeptidase D [CPD]), which is distinct from the multi-serotype AAV receptor (AAVR). AAVR2 enables the transduction of clade E AAVs, including AAV8, and determines an exclusive AAVR-independent transduction pathway for AAV11 and AAV12. We characterized direct binding between the AAV8 capsid and AAVR2 by cryo-electron microscopy (cryo-EM) and identified contact residues. We observed that AAV8 directly binds to the carboxypeptidase-like domain 1 of AAVR2 via its variable region VIII and demonstrated that AAV capsids that lack AAVR2 binding can be bioengineered to engage with AAVR2. Finally, we overexpressed a minimal functional AAVR2 to enhance AAV transduction in vivo. Our study provides insights into AAV biology and clinically deployable solutions to reduce dose-related toxicities associated with AAV vectors. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_61205.map.gz | 58.3 MB | EMDB map data format | |
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| Header (meta data) | emd-61205-v30.xml emd-61205.xml | 16.4 KB 16.4 KB | Display Display | EMDB header |
| Images | emd_61205.png | 79.3 KB | ||
| Filedesc metadata | emd-61205.cif.gz | 5.9 KB | ||
| Others | emd_61205_half_map_1.map.gz emd_61205_half_map_2.map.gz | 296.7 MB 296.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-61205 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-61205 | HTTPS FTP |
-Validation report
| Summary document | emd_61205_validation.pdf.gz | 955.8 KB | Display | EMDB validaton report |
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| Full document | emd_61205_full_validation.pdf.gz | 955.3 KB | Display | |
| Data in XML | emd_61205_validation.xml.gz | 17.2 KB | Display | |
| Data in CIF | emd_61205_validation.cif.gz | 20.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-61205 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-61205 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9j7kMC ![]() 9j6zC ![]() 9j7lC M: atomic model generated by this map C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_61205.map.gz / Format: CCP4 / Size: 371.3 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: 1.07 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #1
| File | emd_61205_half_map_1.map | ||||||||||||
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-Half map: #2
| File | emd_61205_half_map_2.map | ||||||||||||
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Sample components
-Entire : adeno-associated virus 8
| Entire | Name: adeno-associated virus 8 |
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| Components |
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-Supramolecule #1: adeno-associated virus 8
| Supramolecule | Name: adeno-associated virus 8 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 202813 / Sci species name: adeno-associated virus 8 / Virus type: VIRION / Virus isolate: SEROTYPE / Virus enveloped: No / Virus empty: Yes |
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-Macromolecule #1: Capsid protein
| Macromolecule | Name: Capsid protein / type: protein_or_peptide / ID: 1 / Number of copies: 60 / Enantiomer: LEVO |
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| Source (natural) | Organism: Adeno-associated virus - 8 |
| Molecular weight | Theoretical: 81.833047 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: MAADGYLPDW LEDNLSEGIR EWWALKPGAP KPKANQQKQD DGRGLVLPGY KYLGPFNGLD KGEPVNAADA AALEHDKAYD QQLQAGDNP YLRYNHADAE FQERLQEDTS FGGNLGRAVF QAKKRVLEPL GLVEEGAKTA PGKKRPVEPS PQRSPDSSTG I GKKGQQPA ...String: MAADGYLPDW LEDNLSEGIR EWWALKPGAP KPKANQQKQD DGRGLVLPGY KYLGPFNGLD KGEPVNAADA AALEHDKAYD QQLQAGDNP YLRYNHADAE FQERLQEDTS FGGNLGRAVF QAKKRVLEPL GLVEEGAKTA PGKKRPVEPS PQRSPDSSTG I GKKGQQPA RKRLNFGQTG DSESVPDPQP LGEPPAAPSG VGPNTMAAGG GAPMADNNEG ADGVGSSSGN WHCDSTWLGD RV ITTSTRT WALPTYNNHL YKQISNGTSG GATNDNTYFG YSTPWGYFDF NRFHCHFSPR DWQRLINNNW GFRPKRLSFK LFN IQVKEV TQNEGTKTIA NNLTSTIQVF TDSEYQLPYV LGSAHQGCLP PFPADVFMIP QYGYLTLNNG SQAVGRSSFY CLEY FPSQM LRTGNNFQFT YTFEDVPFHS SYAHSQSLDR LMNPLIDQYL YYLSRTQTTG GTANTQTLGF SQGGPNTMAN QAKNW LPGP CYRQQRVSTT TGQNNNSNFA WTAGTKYHLN GRNSLANPGI AMATHKDDEE RFFPSNGILI FGKQNAARDN ADYSDV MLT SEEEIKTTNP VATEEYGIVA DNLQQQNTAP QIGTVNSQGA LPGMVWQNRD VYLQGPIWAK IPHTDGNFHP SPLMGGF GL KHPPPQILIK NTPVPADPPT TFNQSKLNSF ITQYSTGQVS VEIEWELQKE NSKRWNPEIQ YTSNYYKSTS VDFAVNTE G VYSEPRPIGT RYLTRNL UniProtKB: Capsid protein |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.8 mg/mL |
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| Buffer | pH: 7.2 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi




adeno-associated virus 8
Keywords
Authors
China, 1 items
Citation








Z (Sec.)
Y (Row.)
X (Col.)




































Homo sapiens (human)
Processing
FIELD EMISSION GUN
