ArticleJournal of structural biology2009
Heparin binding induces conformational changes in Adeno-associated virus serotype 2.
Article in Journal of structural biology, 2009. 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.
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Who cites it
71 citing papers in PubMed, 106 citations in OpenAlex.
- AI-engineered AAV capsid enables intravitreal delivery for the treatment of diverse retinal degenerations.Molecular therapy. Advances · 2026Article
- Capsid-engineered AAV vector overcomes a key intracellular barrier and efficiently transduces spiral ganglion neurons in adult mice.Molecular therapy. Advances · 2026Article
- The amazing AAV capsids: Into the structure-verse.Molecular therapy. Methods & clinical development · 2025Review
- 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
- Peptide ligands for the affinity purification of adeno-associated viruses from HEK 293 cell lysates.Biotechnology and bioengineering · 2023Article
- Cryo-electron Microscopy of Adeno-associated Virus.Chemical reviews · 2022Review
- Adeno-associated virus (AAV) cell entry: structural insights.Trends in microbiology · 2022Review
- Human and Insect Cell-Produced Recombinant Adeno-Associated Viruses Show Differences in Genome Heterogeneity.Human gene therapy · 2022Article
- Intracellular trafficking of adeno-associated virus (AAV) vectors: challenges and future directions.Gene therapy · 2021Review
- Adeno-associated Virus 9 Structural Rearrangements Induced by Endosomal Trafficking pH and Glycan Attachment.Journal of virology · 2021Article
- Adeno-Associated Virus (AAV) Gene Delivery: Dissecting Molecular Interactions upon Cell Entry.Viruses · 2021Review
- Structural Insight into Non-Enveloped Virus Binding to Glycosaminoglycan Receptors: A Review.Viruses · 2021Review
- Structural characterization of a bat Adeno-associated virus capsid.Journal of structural biology · 2020Article
- Attenuation of Heparan Sulfate Proteoglycan Binding EnhancesMolecular therapy. Methods & clinical development · 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
- Review
- Capsid Modifications for Targeting and Improving the Efficacy of AAV Vectors.Molecular therapy. Methods & clinical development · 2019Review
- Vector uncoating limits adeno-associated viral vector-mediated transduction of human dendritic cells and vector immunogenicity.Scientific reports · 2019Article
- Longer Inactivating Sequence in Peptide Lock Improves Performance of Synthetic Protease-Activatable Adeno-Associated Virus.ACS synthetic biology · 2019Article
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
11 authors at 3 institutions in 1 country.
Funding
Abstract
Adeno-associated virus serotype 2 (AAV2) uses heparan sulfate proteoglycan as a cell surface-attachment receptor. In this study the structures of AAV2 alone and complexed with heparin were determined to approximately 18A resolution using cryo-electron microscopy and three-dimensional image reconstruction. A difference map showed positive density, modeled as heparin, close to the icosahedral twofold axes and between the protrusions that surround the threefold axes of the capsid. Regions of the model near the threefold place the receptor in close proximity to basic residues previously identified as part of the heparin binding site. The region of the model near the twofold axes identifies a second contact site, not previously characterized but which is also possibly configured by heparin binding. The difference map also revealed two significant conformational changes: (I) at the tops of the threefold protrusions, which have become flattened in the complex, and (II) at the fivefold axes where the top of the channel is widened possibly in response to movement of the HI loops in the capsid proteins. Ordered density in the interior of the capsid in the AAV2-heparin complex was interpreted as nucleic acid, consistent with the presence of non-viral DNA in the expressed capsids.
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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.