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      Evidence in support of RNA-mediated inhibition of phosphatidylserine-dependent HIV-1 Gag membrane binding in cells.

      Journal of Biology

      metabolism, gag Gene Products, Human Immunodeficiency Virus, pharmacology, genetics, RNA, drug effects, Protein Binding, Phosphatidylserines, Humans, HeLa Cells, physiology, HIV-1, chemistry, Cell Membrane

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          Abstract

          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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          Author and article information

          Journal
          23552424
          3676091
          10.1128/JVI.00075-13

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