Structure of adeno-associated virus-2 in complex with neutralizing monoclonal antibody A20
Open accessAbstract
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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A20's epitope runs from the 2/5-fold wall toward the 5-fold axes and does not share residues with the peptide.
“While the A20 epitope is positioned from the 2/5-fold wall towards the 5-fold axes and shares no residues with the peptide (McCraw et al., 2012), the C37-B epitope is significantly overlapped by the position of the inserted peptide (Fig. 8B).”
From Structure comparison of the chimeric AAV2.7m8 vector with parental AAV2 (2020) · cites this paper as McCraw et al., 2012
The Results and Discussion sections on the binding site and epitope place A20’s footprint across the plateau, wall, and canyon, supporting its general location. They do not establish that it extends toward the fivefold axes or compare its residues with the specific inserted peptide in the citing sentence; the paper discusses other peptide-insertion sites instead. Page numbers were not available in our copy. (LLM, conf=0.82)
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“The wall of the 2-fold depression is formed by VR-VI, the 2/5-fold wall is formed by VR-I, VR-III, and VR-IX, the top of the 5-fold channel is formed by VR-II, and the protrusions surrounding the 3-fold axis is composed of VR-IV, J Struct Biol.”
BackgroundInfluential
- Authors
- McCraw, D. M., O’Donnell, J. K., Taylor, K. A., Stagg, S. M., & Chapman, M. S.
- Affiliations
- Oregon Health & Science University (US)
- Florida State University (US)
- Corresponding author
- Chapman, Michael S.
- Venue
- Virology
- Publisher
- Elsevier BV
- Published
- 2012-09
- Volume
- 431
- Issue
- 1-2
- Pages
- 40-49
- ISSN
- 0042-6822 (ISSN-L)
- PMC
- PMC3383000
- OpenAlex
- W2054723576
- Cited by
- 84
- References
- 76
- Citations by year
- 2025: 5 · 2024: 5 · 2023: 6 · 2022: 3 · 2021: 6 · 2020: 8 · 2019: 7 · 2018: 8 · 2017: 4 · 2016: 8 · 2015: 8 · 2014: 6 · 2013: 8 · 2012: 2
- FWCI
- 4.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Virology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (R01GM66875, R01GM78538)
- Office of Naval Research (N000141010082)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Keywords
- adeno-associated virus type 2, AAV2, Fab fragment, virus-antibody complexes, capsid structure, neutralizing epitopes, heparan sulfate binding, gene therapy vectors, immune resistance, epitope mapping
- MeSH terms
- Dependovirus, Amino Acid Sequence, Antibodies, Monoclonal, Antibodies, Viral, Humans, Immunoglobulin Fab Fragments, Molecular Sequence Data, Molecular Structure, Epitope Mapping, Cryoelectron Microscopy, Protein Structure, Quaternary, Macromolecular Substances
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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