ArticleJournal of structural biology2015
Structure of neurotropic adeno-associated virus AAVrh.8.
Article in Journal of structural biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 60 citations in OpenAlex.
- Distinct YY dinucleotide periodicity in adeno-associated virus DNA.Molecular therapy : the journal of the American Society of Gene Therapy · 2026Article
- The amazing AAV capsids: Into the structure-verse.Molecular therapy. Methods & clinical development · 2025Review
- Protein Carrier Adeno-Associated Virus.ACS nano · 2025Article
- Biophysical and structural insights into AAV genome ejection.Journal of virology · 2025Article
- Artificial Intelligence-Based Approaches for AAV Vector Engineering.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Structural studies of Parvoviridae capsid assembly and evolution: implications for novel AAV vector design.Frontiers in artificial intelligence · 2025Review
- Article
- Quantification of full and empty particles of adeno-associated virus vectors via a novel dual fluorescence-linked immunosorbent assay.Molecular therapy. Methods & clinical development · 2024Article
- Protein Carrier AAV.bioRxiv : the preprint server for biology · 2024Article
- Probe capsid structure stability and dynamics of adeno-associated virus as an important viral vector for gene therapy by hydrogen-deuterium exchange-mass spectrometry.Protein science : a publication of the Protein Society · 2024Article
- Gene therapy for the leukodystrophies: From preclinical animal studies to clinical trials.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2024Review
- Structural and antigenic characterization of the avian adeno-associated virus capsid.Journal of virology · 2023Article
- Structural and Biophysical Analysis of Adeno-Associated Virus Serotype 2 Capsid Assembly Variants.Journal of virology · 2023Article
- Bipartite genome and structural organization of the parvovirus Acheta domesticus segmented densovirus.Nature communications · 2023Article
- Production and characterization of an AAV1-VP3-only capsid: An analytical benchmark standard.Molecular therapy. Methods & clinical development · 2023Article
- Gene Therapy of Sphingolipid Metabolic Disorders.International journal of molecular sciences · 2023Review
- Systemic gene therapy for methylmalonic acidemia using the novel adeno-associated viral vector 44.9.Molecular therapy. Methods & clinical development · 2022Article
- Ancestral library identifies conserved reprogrammable liver motif on AAV capsid.Cell reports. Medicine · 2022Article
- Cryo-electron Microscopy of Adeno-associated Virus.Chemical reviews · 2022Review
- Characterization of the Serpentine Adeno-Associated Virus (SAAV) Capsid Structure: Receptor Interactions and Antigenicity.Journal of virology · 2022Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Adeno-associated virus rhesus isolate 8 (AAVrh.8) is a leading vector for the treatment of neurological diseases due to its efficient transduction of neuronal cells and reduced peripheral tissue tropism. Toward identification of the capsid determinants for these properties, the structure of AAVrh.8 was determined by X-ray crystallography to 3.5 Å resolution and compared to those of other AAV isolates. The capsid viral protein (VP) structure consists of an αA helix and an eight-stranded anti-parallel β-barrel core conserved in parvoviruses, and large insertion loop regions between the β-strands form the capsid surface topology. The AAVrh.8 capsid exhibits the surface topology conserved in all AAVs: depressions at the icosahedral twofold axis and surrounding the cylindrical channel at the fivefold axis, and three protrusions around the threefold axis. A structural comparison to serotypes AAV2, AAV8, and AAV9, to which AAVrh.8 shares ∼ 84%, ∼ 91%, and ∼ 87% VP sequence identity, respectively, revealed differences in the surface loops known to affect receptor binding, transduction efficiency, and antigenicity. Consistent with this observation, biochemical assays showed that AAVrh.8 is unable to bind heparin and does not cross-react with conformational monoclonal antibodies and human donor serum directed against the other AAVs compared. This structure of AAVrh.8 thus identified capsid surface differences which can serve as template regions for rational design of vectors with enhanced transduction for specific tissues and escape pre-existing antibody recognition. These features are essential for the creation of an AAV vector toolkit that is amenable to personalized disease treatment.
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