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Home / Equine Research Bank / Traffic / Phosphoinositides direct equine infectious anemia virus gag ...
Traffic (Copenhagen, Denmark)2011; 12(4); 438-451; doi: 10.1111/j.1600-0854.2010.01153.x

Phosphoinositides direct equine infectious anemia virus gag trafficking and release.

Abstract: Phosphatidylinositol 4,5-biphosphate [PI(4,5)P(2) ], the predominant phosphoinositide (PI) on the plasma membrane, binds the matrix (MA) protein of human immunodeficiency virus type 1 (HIV-1) and equine infectious anemia virus (EIAV) with similar affinities in vitro. Interaction with PI(4,5)P(2) is critical for HIV-1 assembly on the plasma membrane. EIAV has been shown to localize in internal compartments; hence, the significance of its interaction with PI(4,5)P(2) is unclear. We therefore investigated the binding in vitro of other PIs to EIAV MA and whether intracellular association with compartments bearing these PIs was important for assembly and release of virus-like particles (VLPs) formed by Gag. In vitro, EIAV MA bound phosphatidylinositol 3-phosphate [PI(3)P] with higher affinity than PI(4,5)P(2) as revealed by nuclear magnetic resonance (NMR) spectra upon lipid titration. Gag was detected on the plasma membrane and in compartments enriched in phosphatidylinositol 3,5-biphosphate [PI(3,5)P(2) ]. Treatment of cells with YM201636, a kinase inhibitor that blocks production of PI(3,5)P(2) from PI(3)P, caused Gag to colocalize with aberrant compartments and inhibited VLP release. In contrast to HIV-1, release of EIAV VLPs was not significantly diminished by coexpression with 5-phosphatase IV, an enzyme that specifically depletes PI(4,5)P(2) from the plasma membrane. However, coexpression with synaptojanin 2, a phosphatase with broader specificity, diminished VLP production. PI-binding pocket mutations caused striking budding defects, as revealed by electron microscopy. One of the mutations also modified Gag-Gag interaction, as suggested by altered bimolecular fluorescence complementation. We conclude that PI-mediated targeting to peripheral and internal membranes is a critical factor in EIAV assembly and release.
© 2011 John Wiley & Sons A/S.
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Publication Date: 2011-02-01 PubMed ID: 21176037PubMed Central: PMC3064743DOI: 10.1111/j.1600-0854.2010.01153.xGoogle 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 study investigates the role of phosphoinositides in directing the trafficking and release of proteins in equine infectious anemia virus (EIAV), highlighting their significant role in the virus assembly and release.

Key Findings

  • The study emphasizes on two phosphoinositides, phosphatidylinositol 4,5-biphosphate [PI(4,5)P(2) ] and phosphatidylinositol 3-phosphate [PI(3)P], and their impacts on EIAV MA (matrix protein). These phosphoinositides are responsible for binding the matrix protein, which is crucial for virus assembly.
  • PI(4,5)P(2) is known for its involvement in HIV-1 (human immunodeficiency virus) assembly on the plasma membrane. Although EIAV is localized in internal compartments rather than the plasma membrane, the researchers found that PI(3)P showed a higher binding affinity with EIAV than PI(4,5)P(2).
  • EIAV’s Gag protein was found on the plasma membrane and within the compartments enriched with PI(3,5)P(2). When the cells were treated with YM201636, a kinase inhibitor that stops PI(3,5)P(2) production from PI(3)P, this caused Gag to come together with abnormal compartments, inhibiting the release of virus-like particles (VLPs).

    • Significance of Findings

    • This study implies the critical role of phosphoinositides in directing EIAV assembly and release, extending the understanding of virus-host interaction at a molecular level. Such understanding can contribute to the development of new antiviral strategies.
    • The research also indicates that disrupting the pathways of phosphoinositide, such as with YM201636 that blocks production of PI(3,5)P(2), can inhibit VLP release. This discovery can be valuable—with future research—for potential therapeutic strategies.
    • The study also hints towards potential differences in EIAV and HIV-1 virus assembly mechanisms, as EIAV VLP release was not significantly affected by depleting PI(4,5)P(2). Such understanding allows for the differentiation of virus-host interaction mechanisms in distinct species or virus types, therefore aiding tailored preventative and therapeutic solutions.

Cite This Article

APA
Fernandes F, Chen K, Ehrlich LS, Jin J, Chen MH, Medina GN, Symons M, Montelaro R, Donaldson J, Tjandra N, Carter CA. (2011). Phosphoinositides direct equine infectious anemia virus gag trafficking and release. Traffic, 12(4), 438-451. https://doi.org/10.1111/j.1600-0854.2010.01153.x

Publication

Traffic (Copenhagen, Denmark)
ISSN: 1600-0854
NlmUniqueID: 100939340
Country: England
Language: English
Volume: 12
Issue: 4
Pages: 438-451

Researcher Affiliations

Fernandes, Fiona
  • Department of Molecular Genetics & Microbiology, Life Sciences Building, Room 248, Stony Brook University, Stony Brook, NY 11794, USA.
Chen, Kang
    Ehrlich, Lorna S
      Jin, Jing
        Chen, Min H
          Medina, Gisselle N
            Symons, Marc
              Montelaro, Ronald
                Donaldson, Julie
                  Tjandra, Nico
                    Carter, Carol A

                      MeSH Terms

                      • Acid Anhydride Hydrolases / metabolism
                      • Aminopyridines / pharmacology
                      • Animals
                      • Antiviral Agents / pharmacology
                      • COS Cells
                      • Cell Membrane / metabolism
                      • Cells, Cultured
                      • Chlorocebus aethiops
                      • Gene Products, gag / genetics
                      • Gene Products, gag / metabolism
                      • HIV-1 / genetics
                      • HIV-1 / metabolism
                      • HIV-1 / physiology
                      • Heterocyclic Compounds, 3-Ring / pharmacology
                      • Horses
                      • Humans
                      • Infectious Anemia Virus, Equine / genetics
                      • Infectious Anemia Virus, Equine / metabolism
                      • Infectious Anemia Virus, Equine / physiology
                      • Mutation
                      • Phosphatidylinositol Phosphates / antagonists & inhibitors
                      • Phosphatidylinositol Phosphates / biosynthesis
                      • Phosphatidylinositol Phosphates / metabolism
                      • Protein Binding / physiology
                      • Protein Transport
                      • Transfection
                      • Virus Assembly / drug effects
                      • Virus Assembly / physiology

                      Grant Funding

                      • R01 AI068463-04 / NIAID NIH HHS
                      • Intramural NIH HHS
                      • R56 AI068463 / NIAID NIH HHS
                      • R56 AI068463-01A1 / NIAID NIH HHS
                      • R01 AI068463 / NIAID NIH HHS

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