Cited by 292Ubiquitin and proteasome pathwaysHIV Research and TreatmentT-cell and Retrovirus Studies

Ubiquitin is part of the retrovirus budding machinery

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Patnaik, Akash, Chau, Vincent, Wills, John W.·2000·Proceedings of the National Academy of Sciences

Abstract

Retroviruses contain relatively large amounts of ubiquitin, but the significance of this finding has been unknown. Here, we show that drugs that are known to reduce the level of free ubiquitin in the cell dramatically reduced the release of Rous sarcoma virus, an avian retrovirus. This effect was suppressed by overexpressing ubiquitin and also by directly fusing ubiquitin to the C terminus of Gag, the viral protein that directs budding and particle release. The block to budding was found to be at the plasma membrane, and electron microscopy revealed that the reduced level of ubiquitin results in a failure of mature virus particles to separate from each other and from the plasma membrane during budding. These data indicate that ubiquitin is actually part of the budding machinery.

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Crossref · 10.1073/pnas.97.24.13069

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46 of 46 references verified0 citation errors · 0 not checkable

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  • HIV Gag and other retroviruses are modified with ubiquitin in their p6 domains, and a C-terminal ubiquitin-Gag fusion can stimulate and rescue defective virus release.

    “HIV Gag and other retroviruses are modified with ubiquitin in their p6 domains, and a C-terminal ubiquitin-Gag fusion construct mimicking a true p6 domain modification, can stimulate and rescue defective virus release [22,23].”

    From Budding of a Retrovirus: Some Assemblies Required (2020) · cites this paper as [22]

  • Ubiquitination of Gag is a common feature among retroviruses, intricately associated with retroviral budding/release.

    “ubiquitination of Gag is a common feature among retroviruses, intricately associated with retroviral budding/release”

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Authors
Patnaik, A., Chau, V., & Wills, J. W.
Affiliations
Pennsylvania State University (US)
Venue
Proceedings of the National Academy of Sciences
Published
2000-11-21
Volume
97
Issue
24
Pages
13069-13074
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2060316418
Cited by
292
References
46
Citations by year
2026: 1 · 2025: 4 · 2024: 4 · 2023: 5 · 2022: 7 · 2021: 5 · 2020: 6 · 2019: 7 · 2018: 7 · 2017: 6 · 2016: 4 · 2015: 7 · 2014: 9 · 2013: 8 · 2012: 6
FWCI
11.58
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health
  • National Cancer Institute (R01CA047482, CA-47482, R37CA047482)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Keywords
ubiquitin, Rous sarcoma virus, Gag protein, viral particle release, plasma membrane, viral assembly, avian retroviruses
MeSH terms
Acetylcysteine, Animals, Avian Sarcoma Viruses, Cell Line, Cell Membrane, Cysteine Endopeptidases, Endocytosis, Leupeptins, Multienzyme Complexes, Oligopeptides, Protease Inhibitors, Quail, Recombinant Fusion Proteins, Ubiquitins, Virus Replication, Gene Products, gag, Proteasome Endopeptidase Complex

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