ArticleJournal of structural biology2018
Atomic structure of a rationally engineered gene delivery vector, AAV2.5.
Article in Journal of structural biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
24 citing papers in PubMed.
- Role of viral protein ratio in the structure and separation of empty and full adeno-associated virus capsids: A molecular dynamics study.Molecular therapy. Advances · 2026Article
- The amazing AAV capsids: Into the structure-verse.Molecular therapy. Methods & clinical development · 2025Review
- AAV vector development, back to the future.Molecular therapy : the journal of the American Society of Gene Therapy · 2025Review
- Review
- Structural studies of Parvoviridae capsid assembly and evolution: implications for novel AAV vector design.Frontiers in artificial intelligence · 2025Review
- Prevalence of AAV2.5 neutralizing antibodies in synovial fluid and serum of patients with osteoarthritis.Gene therapy · 2023Article
- Semirational bioengineering of AAV vectors with increased potency and specificity for systemic gene therapy of muscle disorders.Science advances · 2022Article
- Cryo-electron Microscopy of Adeno-associated Virus.Chemical reviews · 2022Review
- Red Blood Cell Anchoring Enables Targeted Transduction and Re-Administration of AAV-Mediated Gene Therapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Characterization of the Serpentine Adeno-Associated Virus (SAAV) Capsid Structure: Receptor Interactions and Antigenicity.Journal of virology · 2022Article
- A versatile toolkit for overcoming AAV immunity.Frontiers in immunology · 2022Review
- Adeno-associated Virus (AAV) Capsid Chimeras with Enhanced Infectivity Reveal a Core Element in the AAV Genome Critical for both Cell Transduction and Capsid Assembly.Journal of virology · 2021Article
- Completion of the AAV Structural Atlas: Serotype Capsid Structures Reveals Clade-Specific Features.Viruses · 2021Article
- Adeno-Associated Viruses (AAV) and Host Immunity - A Race Between the Hare and the Hedgehog.Frontiers in immunology · 2021Review
- Characterization of AAV-Specific Affinity Ligands: Consequences for Vector Purification and Development Strategies.Molecular therapy. Methods & clinical development · 2020Article
- Structural characterization of a bat Adeno-associated virus capsid.Journal of structural biology · 2020Article
- Structural Characterization of Cuta- and Tusavirus: Insight into Protoparvoviruses Capsid Morphology.Viruses · 2020Article
- Comparative Analysis of the Capsid Structures of AAVrh.10, AAVrh.39, and AAV8.Journal of virology · 2020Article
- Structure comparison of the chimeric AAV2.7m8 vector with parental AAV2.Journal of structural biology · 2020Article
- Engineering the AAV capsid to evade immune responses.Current opinion in biotechnology · 2019Review
Corrections and comments
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Authors and funding
12 authors.
Funding
Abstract
AAV2.5 represents the first structure-guided in-silico designed Adeno-associated virus (AAV) gene delivery vector. This engineered vector combined the receptor attachment properties of AAV serotype 2 (AAV2) with the muscle tropic properties of AAV1, and exhibited an antibody escape phenotype because of a modified antigenic epitope. To confirm the design, the structure of the vector was determined to a resolution of 2.78 Å using cryo-electron microscopy and image reconstruction. The structure of the major viral protein (VP), VP3, was ordered from residue 219 to 736, as reported for other AAV structures, and the five AAV2.5 residues exchanged from AAV2 to AAV1, Q263A, T265 (insertion), N706A, V709A, and T717N, were readily interpretable. Significantly, the surface loops containing these residues adopt the AAV1 conformation indicating the importance of amino acid residues in dictating VP structure.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.