EMD-41209

Single-particle
3.06 Å
EMD-41209 Deposition: 07/07/2023
Map released: 30/08/2023
Last modified: 29/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-41209

Avian Adeno-associated virus - empty capsid

EMD-41209

Single-particle
3.06 Å
EMD-41209 Deposition: 07/07/2023
Map released: 30/08/2023
Last modified: 29/05/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Avian adeno-associated virus
Sample: Avian adeno-associated virus
Fitted models: 8tey (Avg. Q-score: 0.591)

Deposition Authors: 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.
Hsi J , Mietzsch M , Chipman P , Afione S, Zeher A, Huang R, Chiorini J, McKenna R
(2023) J Virol , 97 , e0078023 - e0078023
PUBMED: 37702486
DOI: doi:10.1128/jvi.00780-23
ISSN: 1098-5514
ASTM: JOVIAM
Abstract:
Importance
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.