Electron cryo‐microscopy and image reconstruction of adeno‐associated virus type 2 empty capsids
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Adeno-associated virus type 2 empty capsids are composed of three proteins, VP1, VP2 and VP3, which have relative molecular masses of 87, 72 and 62 kDa, respectively, and differ in their N-terminal amino acid sequences. They have a likely molar ratio of 1:1:8 and occupy symmetrical equivalent positions in an icosahedrally arranged protein shell. We have investigated empty capsids of adeno-associated virus type 2 by electron cryo-microscopy and icosahedral image reconstruction. The three-dimensional map at 1.05 nm resolution showed sets of three elongated spikes surrounding the three-fold symmetry axes and narrow empty channels at the five-fold axes. The inside of the capsid superimposed with the previously determined structure of the canine parvovirus (Q. Xie and M.S. Chapman, 1996, J. Mol. Biol., 264, 497-520), whereas the outer surface showed clear discrepancies. Globular structures at the inner surface of the capsid at the two-fold symmetry axes were identified as possible positions for the N-terminal extensions of VP1 and VP2.
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In contrast to MVM and B19, the N termini of Vp1 and Vp2 of AAV are located within the virion.
“In contrast, the N termini of Vp1 and Vp2 of AAV are located within the virion (27, 46, 48).”
From Packaging Capacity of Adeno-Associated Virus Serotypes: Impact of Larger Genomes on Infectivity and Postentry Steps (2005) · cites this paper as [27]
The Results (page not provided) conclude that VP1 and VP2 N-terminal extensions are likely inside AAV2 empty capsids, in contrast to evidence of outward extension in MVM and B19. The source presents the AAV2 location as an inference, not a directly determined fact, and does not establish it for AAV virions generally. (LLM, conf=0.88)
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“This conclusion is supported by the reaction of capsids with two monoclonal antibodies having VP1- and VP1/VP2-specific epitopes (Wobus et al., 2000).”
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Background
- Authors
- Kronenberg, S., Kleinschmidt, J. A., & Böttcher, B.
- Affiliations
- German Cancer Research Center (DE)
- European Molecular Biology Laboratory (DE)
- Corresponding author
- Böttcher, Bettina
- ORCID
- Böttcher, Bettina
- Venue
- The EMBO Reports
- Published
- 2001-11-01
- Volume
- 2
- Issue
- 11
- Pages
- 997-1002
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC1084133
- OpenAlex
- W2101428586
- Cited by
- 161
- References
- 2
- Citations by year
- 2026: 1 · 2025: 8 · 2024: 4 · 2023: 8 · 2022: 6 · 2021: 8 · 2020: 7 · 2019: 11 · 2018: 2 · 2017: 4 · 2016: 1 · 2015: 5 · 2014: 5 · 2013: 4 · 2012: 7
- FWCI
- 7.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- EMBO Reports (publishedVersion)
- PubMed Central (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- adeno-associated virus type 2, empty capsids, viral capsid structure, VP1, VP2, VP3, capsid symmetry, N-terminal extension
- MeSH terms
- Dependovirus, Capsid, Image Processing, Computer-Assisted, Microscopy, Electron, Models, Molecular, Blotting, Western, Protein Structure, Tertiary, Cryoelectron Microscopy
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