Cited by 65Virus-based gene therapy researchParvovirus B19 Infection StudiesVirology and Viral Diseases

Adeno-associated virus interactions with B23/Nucleophosmin: Identification of sub-nucleolar virion regions

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Bevington, Joyce M., Needham, Patrick G., Verrill, Kristin C., Collaco, Roy F., Basrur, Venkatesh, Trempe, James P.·2007·Virology

Abstract

Adeno-associated virus (AAV) is a human parvovirus that normally requires a helper virus such as adenovirus (Ad) for replication. The four replication proteins (Rep78, 68, 52 and 40) encoded by AAV are pleiotropic effectors of virus integration, replication, transcription and virion assembly. Using Rep68 column chromatography and mass spectrometry, we have identified the nucleolar, B23/Nucleophosmin (NPM) protein as an Rep-interacting partner. Rep-NPM interactions were verified by co-immunofluorescence and chemical cross-linking studies. We have found that there is demonstrable, but limited co-localization between Rep and NPM in co-infected cells. In contrast, there was significant co-localization between NPM and AAV Cap proteins. In vitro experiments using purified MBPRep78 and NPM show that NPM stimulates MBPRep78 interactions with the AAV ITR as well as endonuclease activity. These studies suggest that NPM plays a role in AAV amplification affecting Rep function and virion assembly.

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Crossref · 10.1016/j.virol.2006.07.050

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  • Nucleolin and nucleophosmin associate with both VPs and assembled capsids in the nucleoli.

    “Additionally, two nuclear proteins, nucleolin and nucleophosmin [43,44], have been shown to associate with both VPs and assembled capsids in the nucleoli.”

    From Understanding Capsid Assembly and Genome Packaging for Adeno-Associated Viruses (2017) · cites this paper as [43]

    The ‘NPM co-localization with Cap and Rep proteins’ section reports that nucleophosmin (NPM) co-localizes with AAV Cap proteins in nucleoli. The Discussion proposes a model in which Cap proteins assemble there and associate with NPM, but the paper does not establish an association with assembled capsids; it also does not address nucleolin. (LLM, conf=0.87)

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  1. Kotin, R.M., Siniscalco, M., Samulski, R.J., Zhu, X.D., Hunter, L., Laughlin, C.A., McLaughlin, S., Muzyczka, N., Rocchi, M., Berns, K.I., 1990. Site- specific integration by adeno-associated virus. Proc. Natl. Acad. Sci. U.S.A. 87 (6), 2211-2215.
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  4. Weger, S., Wendland, M., Kleinschmidt, J.A., Heilbronn, R., 1999. The adeno- associated virus type 2 regulatory proteins rep78 and rep68 interact with the transcriptional coactivator PC4. J. Virol. 73 (1), 260-269.
  5. Yoneda-Kato, N., Look, A.T., Kirstein, M.N., Valentine, M.B., Raimondi, S.C., Cohen, K.J., Carroll, A.J., Morris, S.W., 1996. The t(3;5)(q25.1;q34) of myelodysplastic syndrome and acute myeloid leukemia produces a novel fusion gene, NPM-MLF1. Oncogene 12 (2), 265-275.

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Authors
Bevington, J. M., Needham, P. G., Verrill, K. C., Collaco, R. F., Basrur, V., & Trempe, J. P.
Affiliations
University of Toledo (US)
Corresponding author
Trempe, James P.
Venue
Virology
Publisher
Elsevier BV
Published
2007-01
Volume
357
Issue
1
Pages
102-113
ISSN
0042-6822 (ISSN-L)
OpenAlex
W2070890881
Cited by
65
References
0
Citations by year
2026: 2 · 2025: 1 · 2024: 4 · 2023: 1 · 2022: 2 · 2021: 1 · 2019: 2 · 2018: 5 · 2017: 5 · 2016: 5 · 2015: 3 · 2014: 4 · 2013: 4 · 2012: 3
FWCI
2.09
Type
journal article
Language
en
Open access
Locations
  • Virology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Institute of General Medical Sciences (GM64765, R01GM064765)
  • National Institute of Allergy and Infectious Diseases (R01AI051471, AI 51471)
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, Rep78, Rep68, inverted terminal repeats, endonuclease activity, viral assembly, viral replication, colocalization
MeSH terms
Nucleophosmin, Dependovirus, Cell Nucleolus, DNA-Binding Proteins, Fluorescent Antibody Technique, HeLa Cells, Humans, Nuclear Proteins, Protein Binding, Viral Proteins, Virion, Virus Assembly, Immunoprecipitation

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