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Home / Equine Research Bank / J Virol / Late domain-dependent inhibition of equine infectious anemia...
Journal of virology2003; 78(2); 724-732; doi: 10.1128/jvi.78.2.724-732.2004

Late domain-dependent inhibition of equine infectious anemia virus budding.

Abstract: The Gag proteins of a number of different retroviruses contain late or L domains that promote the release of virions from the plasma membrane. Three types of L domains have been identified to date: Pro-Thr-Ala-Pro (PTAP), Pro-Pro-X-Tyr, and Tyr-Pro-Asp-Leu. It has previously been demonstrated that overexpression of the N-terminal, E2-like domain of the endosomal sorting factor TSG101 (TSG-5') inhibits human immunodeficiency virus type 1 (HIV-1) release but does not affect the release of the PPPY-containing retrovirus murine leukemia virus (MLV), whereas overexpression of the C-terminal portion of TSG101 (TSG-3') potently disrupts both HIV-1 and MLV budding. In addition, it has been reported that, while the release of a number of retroviruses is disrupted by proteasome inhibitors, equine infectious anemia virus (EIAV) budding is not affected by these agents. In this study, we tested the ability of TSG-5', TSG-3', and full-length TSG101 (TSG-F) overexpression, a dominant negative form of the AAA ATPase Vps4, and proteasome inhibitors to disrupt the budding of EIAV particles bearing each of the three types of L domain. The results indicate that (i) inhibition by TSG-5' correlates with dependence on PTAP; (ii) the release of wild-type EIAV (EIAV/WT) is insensitive to TSG-3', whereas this C-terminal TSG101 fragment potently impairs the budding of EIAV when it is rendered PTAP or PPPY dependent; (iii) budding of all EIAV clones is blocked by dominant negative Vps4; and (iv) EIAV/WT release is not impaired by proteasome inhibitors, while EIAV/PTAP and EIAV/PPPY release is strongly disrupted by these compounds. These findings highlight intriguing similarities and differences in host factor utilization by retroviral L domains and suggest that the insensitivity of EIAV to proteasome inhibitors is conferred by the L domain itself and not by determinants in Gag outside the L domain.
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Publication Date: 2003-12-25 PubMed ID: 14694104PubMed Central: PMC368837DOI: 10.1128/jvi.78.2.724-732.2004Google 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.

This research investigates the impacts of certain endosomal sorting factors and proteasome inhibitors on the release or “budding” of the equine infectious anemia virus (EIAV). The study draws a comparison between the effects on different isolates of EIAV and other retroviruses, shedding light on their similarities and differences.

Understanding L Domains and Retroviruses

  • Gag proteins of varying retroviruses contain what are known as late or L domains. These L domains aid the release of virus particles, or virions, from the host cell’s plasma membrane.
  • Three types of L domains, Pro-Thr-Ala-Pro (PTAP), Pro-Pro-X-Tyr, and Tyr-Pro-Asp-Leu, have been identified in different breakthrough studies and research.

Role and Impact of TSG101

  • The endosomal sorting factor TSG101 plays an essential role in regulating the exit of certain retroviruses, such as the human immunodeficiency virus type 1 (HIV-1). However, it does not affect the release of others like the murine leukemia virus (MLV).
  • In the case of EIAV, various TSG101 isoforms (TSG-5′, TSG-3′, and full-length TSG101) expressed in excess displayed varying effects on the budding of EIAV particles depending on the type of L domain present.
  • It is noteworthy that inhibition by TSG-5′ correlates strongly with an L domain that exhibits a PTAP pattern. Similarly, while the release of wild-type EIAV is unaffected by TSG-3′, this isoform of TSG101 essentially disrupts the budding process when PTAP or Pro-Pro-X-Tyr L domain is present in EIAV.

Effects of ATPase Vps4 and Proteasome Inhibitors

  • The AAA ATPase Vps4, a critical agent in the mechanisms of membrane fusion and fission, has shown strong blocking effects on budding in all EIAV clones.
  • While proteasome inhibitors, a significant class of anti-cancer agents, do not impair the release of wild type EIAV, they have strong disruptive effects on the release of EIAV showcasing PTAP and Pro-Pro-X-Tyr L domains.
  • These observations suggest that insensitivity of EIAV to proteasome inhibitors is primarily a feature of the L domain itself rather than other factors in Gag outside the L domain.

Summary of the Findings

  • The results indicate a peculiar interplay of host factors and L domains in retroviral release and how understanding these relations can help manipulate or disrupt virus budding processes. This discovery opens pathways for effective antiviral therapeutic strategies.
  • The data also reminds researchers of the intriguing similarities and differences in L domain and host factor usage across different retroviruses, warranting further exploration.

Cite This Article

APA
Shehu-Xhilaga M, Ablan S, Demirov DG, Chen C, Montelaro RC, Freed EO. (2003). Late domain-dependent inhibition of equine infectious anemia virus budding. J Virol, 78(2), 724-732. https://doi.org/10.1128/jvi.78.2.724-732.2004

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 78
Issue: 2
Pages: 724-732

Researcher Affiliations

Shehu-Xhilaga, Miranda
  • Laboratory of Molecular Microbiology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-0460, USA.
Ablan, Sherimay
    Demirov, Dimiter G
      Chen, Chaoping
        Montelaro, Ronald C
          Freed, Eric O

            MeSH Terms

            • Adenosine Triphosphatases / antagonists & inhibitors
            • Amino Acid Motifs
            • Animals
            • Cell Line
            • Cysteine Endopeptidases
            • Gene Expression Regulation, Viral
            • Gene Products, gag / chemistry
            • Gene Products, gag / genetics
            • Gene Products, gag / metabolism
            • Humans
            • Infectious Anemia Virus, Equine / chemistry
            • Infectious Anemia Virus, Equine / growth & development
            • Infectious Anemia Virus, Equine / pathogenicity
            • Multienzyme Complexes / antagonists & inhibitors
            • Protease Inhibitors / pharmacology
            • Proteasome Endopeptidase Complex
            • Transfection
            • Virion / genetics
            • Virion / metabolism

            Grant Funding

            • R01 CA049296 / NCI NIH HHS
            • T32 AI049820 / NIAID NIH HHS
            • 2R01 CA49296 / NCI NIH HHS
            • T32 AI49820 / NIAID NIH HHS

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