ArticleVirology
Structure of adeno-associated virus-2 in complex with neutralizing monoclonal antibody A20.
Article in Virology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 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
71 citing papers in PubMed, 83 citations in OpenAlex.
- The amazing AAV capsids: Into the structure-verse.Molecular therapy. Methods & clinical development · 2025Review
- Graphene-Enhanced Plasmonic Interfaces: A General Strategy for Highly Sensitive Detection of Biomolecular Interactions.Advanced healthcare materials · 2025Article
- Structural characterization of antibody-responses following Zolgensma treatment for AAV capsid engineering to expand patient cohorts.Nature communications · 2025Article
- Structural studies of Parvoviridae capsid assembly and evolution: implications for novel AAV vector design.Frontiers in artificial intelligence · 2025Review
- An investigation of the immune epitopes of adeno-associated virus capsid-derived peptides among hemophilia patients.Molecular therapy. Methods & clinical development · 2024Article
- Dissecting positive selection events and immunological drives during the evolution of adeno-associated virus lineages.PLoS pathogens · 2024Article
- TRIM21 and Fc-engineered antibodies: decoding its complex antibody binding mode with implications for viral neutralization.Frontiers in immunology · 2024Article
- Novel rAAV vector mediated intrathecal HGF delivery has an impact on neuroimmune modulation in the ALS motor cortex with TDP-43 pathology.Gene therapy · 2023Article
- The Structures and Functions of Parvovirus Capsids and Missing Pieces: the Viral DNA and Its Packaging, Asymmetrical Features, Nonprotein Components, and Receptor or Antibody Binding and Interactions.Journal of virology · 2023Review
- Biophysical characterization of adeno-associated virus capsid through the viral transduction life cycle.Journal, genetic engineering & biotechnology · 2023Review
- Review
- Adeno-associated virus receptor complexes and implications for adeno-associated virus immune neutralization.Frontiers in microbiology · 2023Article
- Cryo-electron Microscopy of Adeno-associated Virus.Chemical reviews · 2022Review
- Article
- Adeno-associated virus (AAV) cell entry: structural insights.Trends in microbiology · 2022Review
- Structurally Mapping Antigenic Epitopes of Adeno-associated Virus 9: Development of Antibody Escape Variants.Journal of virology · 2022Article
- Enhanced Transduction of P2X7-Expressing Cells with Recombinant rAAV Vectors.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Comparative structural, biophysical, and receptor binding study of true type and wild type AAV2.Journal of structural biology · 2021Article
- Structural Study of Aavrh.10 Receptor and Antibody Interactions.Journal of virology · 2021Article
- Adeno-Associated Virus (AAV) Gene Delivery: Dissecting Molecular Interactions upon Cell Entry.Viruses · 2021Review
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The use of adeno-associated virus (AAV) as a gene therapy vector is limited by the host neutralizing immune response. The cryo-electron microscopy (EM) structure at 8.5Å resolution is determined for a complex of AAV-2 with the Fab' fragment of monoclonal antibody (MAb) A20, the most extensively characterized AAV MAb. The binding footprint is determined through fitting the cryo-EM reconstruction with a homology model following sequencing of the variable domain, and provides a structural basis for integrating diverse prior epitope mappings. The footprint extends from the previously implicated plateau to the side of the spike, and into the conserved canyon, covering a larger area than anticipated. Comparison with structures of binding and non-binding serotypes indicates that recognition depends on a combination of subtle serotype-specific features. Separation of the neutralizing epitope from the heparan sulfate cell attachment site encourages attempts to develop immune-resistant vectors that can still bind to target cells.
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What OpenQuestion holds
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.