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Journal of virology2002; 76(6); 3038-3044; doi: 10.1128/jvi.76.6.3038-3044.2002

Equine infectious anemia virus and the ubiquitin-proteasome system.

Abstract: Some retroviruses contain monoubiquitinated Gag and do not bud efficiently from cells treated with proteasome inhibitors, suggesting an interaction between the ubiquitin-proteasome system and retrovirus assembly. We examined equine infectious anemia virus (EIAV) particles and found that approximately 2% of the p9(Gag) proteins are monoubiquitinated, demonstrating that this Gag protein interacts with an ubiquitinating activity. Different types of proteasome inhibitors were used to determine if proteasome inactivation affects EIAV release from chronically infected cells. Pulse-chase immunoprecipitation and time course immunoblot analyses showed that proteasome inactivation slightly decreased virus release (at most a twofold effect), while it did not affect Gag processing. These results contrast with those obtained with other viruses which are sensitive to these inhibitors. This suggests that, although its Gag is monoubiquitinated, the requirements for EIAV release are somewhat different from those for retroviruses that are sensitive to proteasome inhibitors.
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Publication Date: 2002-02-28 PubMed ID: 11861870PubMed Central: PMC135975DOI: 10.1128/jvi.76.6.3038-3044.2002Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article investigates the relationship between the equine infectious anemia virus (EIAV) and the ubiquitin-proteasome system, a critical part of cellular function and virus assembly. The study found that EIAV reacts differently than other viruses to proteasome inhibitors, indicating distinctive mechanisms in the EIAV release process.

Interaction of EIAV Gag Proteins and Ubiquitin

  • The researchers first looked at the EIAV particles and found that approximately 2% of the p9(Gag) proteins in them are monoubiquitinated. This indicates that this particular protein interacts with ubiquitinating activity.
  • Ubiquitination is a process that tags proteins for degradation or to alter their cellular functions. In this case, the p9(Gag) proteins being monoubiquitinated suggests that there is an interaction between the virus and the ubiquitin-proteasome system, which is involved in the degradation of unnecessary or damaged proteins in the cell.

Impact of Proteasome Inhibition on EIAV

  • Different types of proteasome inhibitors were used to evaluate if there is a relationship between proteasome activity and the release of the EIAV from cells.
  • Proteasome inhibitors are compounds that disrupt the proteasome’s function, potentially impacting the virus’s life cycle. These compounds were used based on previously observed behavior in other retroviruses that did not bud efficiently when cells were treated with proteasomes inhibitors.
  • After applying proteasome inhibitors, the study found that virus release slightly decreased while the processing of Gag proteins remained unaffected. The decrease in virus release was minimal, showing at most a twofold effect.

Comparison with Other Retroviruses

  • The results obtained from this study contrasted with those obtained with other viruses which were more sensitive to proteasome inhibitors.
  • Despite the Gag protein of EIAV being monoubiquitinated (similar to some other retroviruses), the release process of EIAV behaved differently under proteasome inhibition. This suggests that the requirements for the release of EIAV are not exactly the same as for other retroviruses that are more sensitive to the effects of proteasome inhibitors.

Cite This Article

APA
Ott DE, Coren LV, Sowder RC, Adams J, Nagashima K, Schubert U. (2002). Equine infectious anemia virus and the ubiquitin-proteasome system. J Virol, 76(6), 3038-3044. https://doi.org/10.1128/jvi.76.6.3038-3044.2002

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 76
Issue: 6
Pages: 3038-3044

Researcher Affiliations

Ott, David E
  • AIDS Vaccine Program, SAIC Frederick, National Cancer Institute at Frederick, National Institutes of Health, Frederick, Maryland 21702, USA. ott@ncifcrf.gov
Coren, Lori V
    Sowder, Raymond C
      Adams, Julian
        Nagashima, Kunio
          Schubert, Ulrich

            MeSH Terms

            • Animals
            • Cell Line
            • Cysteine Endopeptidases / metabolism
            • Enzyme Inhibitors / pharmacology
            • Equine Infectious Anemia / virology
            • Gene Products, gag / metabolism
            • Infectious Anemia Virus, Equine / drug effects
            • Infectious Anemia Virus, Equine / physiology
            • Multienzyme Complexes / antagonists & inhibitors
            • Multienzyme Complexes / metabolism
            • Proteasome Endopeptidase Complex
            • Ubiquitin / metabolism
            • Virus Assembly

            Grant Funding

            • N01-CO-56000 / NCI NIH HHS

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