Summary for 8TEX
| Entry DOI | 10.2210/pdb8tex/pdb |
| EMDB information | 41208 |
| Descriptor | Capsid protein (1 entity in total) |
| Functional Keywords | adeno-associated virus, capsid, quail bronchitis, avianaav, aaav, virus |
| Biological source | Avian adeno-associated virus |
| Total number of polymer chains | 60 |
| Total formula weight | 3614250.00 |
| Authors | Hsi, J.,Mietzsch, M.,Chipman, P.,Afione, S.,Zeher, A.,Huang, R.,Chiorini, J.,McKenna, R. (deposition date: 2023-07-07, release date: 2023-08-30, Last modification date: 2025-05-28) |
| Primary citation | Hsi, J.,Mietzsch, M.,Chipman, P.,Afione, S.,Zeher, A.,Huang, R.,Chiorini, J.,McKenna, R. Structural and antigenic characterization of the avian adeno-associated virus capsid. J.Virol., 97:e0078023-e0078023, 2023 Cited by PubMed Abstract: AAVs are extensively studied as promising therapeutic gene delivery vectors. In order to circumvent pre-existing antibodies targeting primate-based AAV capsids, the AAAV capsid was evaluated as an alternative to primate-based therapeutic vectors. Despite the high sequence diversity, the AAAV capsid was found to bind to a common glycan receptor, terminal galactose, which is also utilized by other AAVs already being utilized in gene therapy trials. However, contrary to the initial hypothesis, AAAV was recognized by approximately 30% of human sera tested. Structural and sequence comparisons point to conserved epitopes in the fivefold region of the capsid as the reason determinant for the observed cross-reactivity. PubMed: 37702486DOI: 10.1128/jvi.00780-23 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.54 Å) |
Structure validation
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