Structural highlights
Function
Q7TG43_9VIRU
Publication Abstract from PubMed
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.
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 J Virol. 2023 Oct 31;97(10):e0078023. doi: 10.1128/jvi.00780-23. Epub 2023 Sep , 13. PMID:37702486[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2023 Oct 31;97(10):e0078023. PMID:37702486 doi:10.1128/jvi.00780-23