Journal of Virology · 2013 · 76 citations · 39 references
Life SciencesCell BiologyMolecular BiologyLipid BiochemistryMembrane BiochemistryMolecular VirologyLipid-protein InteractionsMembrane DomainsProtein-lipid InteractionsRna InterferenceRna-protein InteractionsViral Rna BiologyLipid Binding SpecificityLipid SpecificityPhosphatidylinositol 4, 5-BisphosphateProtein-lipid SpecificityRna Interference SuppressionRna Silencing SuppressionViral Envelope ProteinsViral Rna-protein Interactions
The matrix domain promotes plasma-membrane-specific binding of HIV-1 Gag through interaction with an acidic lipid phosphatidylinositol-(4,5)-bisphosphate. In in vitro systems, matrix-bound RNA suppresses Gag interactions with phosphatidylserine, an acidic lipid prevalent in various cytoplasmic membranes, thereby enhancing the lipid specificity of the matrix domain. Here we provide in vitro and cell-based evidence supporting the idea that this RNA-mediated suppression occurs in cells and hence is a physiologically relevant mechanism that prevents Gag from binding promiscuously to phosphatidylserine-containing membranes.
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Molecular cloning: A laboratory manual
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