Cited by 161Advanced Electron Microscopy Techniques and ApplicationsVirus-based gene therapy researchEnzyme Structure and Function

Electron cryo‐microscopy and image reconstruction of adeno‐associated virus type 2 empty capsids

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Kronenberg, Stephanie, Kleinschmidt, Jürgen A, Böttcher, Bettina·2001·The EMBO Reports

Abstract

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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Crossref · 10.1093/embo-reports/kve234

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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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Research works printed but not linked: 7

  1. Chipman, P.R., Agbandje-McKenna, M., Kajigaya, S., Brown, K.E., Young, N.S., Baker, T.S. and Rossmann, M.G. (1996) Cryo-electron microscopy studies of empty capsids of human parvovirus B19 complexed with its cellular receptor. Proc. Natl Acad. Sci. USA, 93, 7502-7506.
  2. Crowther, R.A. (1971) Procedures for three-dimensional reconstruction of spherical viruses by Fourier synthesis from electron micrographs. Phil. Trans. R. Soc. Lond. B. Biol. Sci., 261, 221-230.
  3. Harlow, E. and Lane, F. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
  4. Reimer, L. (1993) Transmission Electron Microscopy. Physics of Image Formation and Microanalysis. Springer, Berlin, Heidelberg.
  5. Samulski, R.J., Sally, M. and Muzcyzka, N. (1999) Adeno-associated viral vectors. In Friedman, T. (ed.) The Development of Human Gene Therapy. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, pp. 131-172.
  6. Thomas, J.O. and Kornberg, R.D. (1975) An octamer of histones in chromatin and free in solution. Proc. Natl Acad. Sci. USA, 72, 2626-2630.
  7. Xie, Q. and Chapman, M.S. (1996) Canine parvovirus capsid structure, analyzed at 2.9 Å resolution. J. Mol. Biol., 264, 497-520. DOI: 10.1093/embo-reports/kve234 14693178, 2001, 11, Downloaded from https://www.embopress.org/doi/10.1093/embo-reports/kve234 by Readcube (Labtiva Inc.), Wiley Online Library on [29/08/2023]. See the Terms and Conditions (https://onlinelibrary.wiley.com/terms-and-conditions) on Wiley Online Library for rules of use; OA articles are governed by the applicable Creative Commons License · DOI

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Authors
Kronenberg, S., Kleinschmidt, J. A., & Böttcher, B.
Affiliations
  • German Cancer Research Center (DE)
  • European Molecular Biology Laboratory (DE)
Corresponding author
Böttcher, Bettina
Venue
The EMBO Reports
Published
2001-11-01
Volume
2
Issue
11
Pages
997-1002
ISSN
  • 1469-221X (ISSN-L)
  • 1469-3178
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
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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