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Cited by 147Virus-based gene therapy researchParvovirus B19 Infection StudiesVirology and Viral Diseases

The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.

Intermediates of adeno-associated virus type 2 assembly: identification of soluble complexes containing Rep and Cap proteins

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Wistuba, A, Weger, S, Kern, A, Kleinschmidt, J A·1995·Journal of Virology
DOI 10.1128/jvi.69.9.5311-5319.1995PMC PMC189369
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Abstract

The proteins encoded by the adeno-associated virus type 2 (AAV-2) rep and cap genes obtained during a productive infection of HeLa cells with AAV-2 and adenovirus type 2 were fractionated according to solubility, cellular localization, and sedimentation properties. The majority of Rep and Cap proteins accumulated in the nucleus, where they distributed into a soluble and an insoluble fraction. Analysis of the soluble nuclear fraction of capsid proteins by sucrose density gradients showed that they formed at least three steady-state pools: a monomer pool sedimenting at about 6S, a pool of oligomeric intermediates sedimenting between 10 and 15S, and a broad pool of assembly products with a peak between 60 and 110S, the known sedimentation positions of empty and full capsids. While the soluble nuclear monomer and oligomer pool contained predominantly only two capsid proteins, the 30 to 180S assembly products contained VP1, VP2, and VP3 in a stoichiometry similar to that of purified virions. They probably represent different intermediates in capsid assembly, DNA encapsidation, and capsid maturation. In contrast, the cytoplasmic fraction of capsid proteins showed a pattern of oligomers continuously increasing in size without a defined peak, suggesting that assembly of 60S particles occurs in the nucleus. Soluble nuclear Rep proteins were distributed over the whole sedimentation range, probably as a result of association with AAV DNA. Subfractions of the Rep proteins with defined sedimentation values were obtained in the soluble nuclear and cytoplasmic fractions. We were able to coimmunoprecipitate capsid proteins sedimenting between 60 and 110S with antibodies against Rep proteins, suggesting that they exist in common complexes possibly involved in AAV DNA packaging. Antibodies against the capsid proteins, however, precipitated Rep78 and Rep68 predominantly with a peak around 30S representing a second complex containing Rep and Cap proteins.

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Metadata

Authors
Wistuba, A., Weger, S., Kern, A., & Kleinschmidt, J. A.
Affiliations
German Cancer Research Center (DE)
ORCID
Weger, S
Venue
Journal of Virology
Publisher
American Society for Microbiology
Published
1995-09
Volume
69
Issue
9
Pages
5311-5319
ISSN
  • 0022-538X (ISSN-L)
  • 1098-5514
DOI
10.1128/jvi.69.9.5311-5319.1995
PMC
PMC189369
OpenAlex
W2172045470
Cited by
147
References
44
Citations by year
2026: 3 · 2025: 4 · 2024: 5 · 2023: 6 · 2022: 2 · 2021: 3 · 2020: 3 · 2019: 3 · 2018: 6 · 2017: 4 · 2016: 2 · 2015: 1 · 2014: 3 · 2013: 2 · 2012: 7
FWCI
3.75
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Journal of Virology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
  • Health Sciences › Medicine › Infectious Diseases › Parvovirus B19 Infection Studies
  • Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
Keywords
adeno-associated virus type 2, capsid assembly, Rep protein, capsid protein, capsid maturation, DNA encapsidation, Rep78, Rep68, co-immunoprecipitation, sedimentation analysis
MeSH terms
Dependovirus, Capsid, Cell Fractionation, Cell Nucleus, Cytoplasm, Electrophoresis, Polyacrylamide Gel, Genes, Viral, HeLa Cells, Humans, Virus Replication, Immunoblotting, Viral Nonstructural Proteins

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