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6. Synchronized HIV assembly by tunable PIP 2 changes reveals PIP 2 requirement for stable Gag anchoring.

Author

Mücksch F, Laketa V, Müller B, Schultz C, and Kräusslich HG

Subjects
Cell Line, Humans, Cell Membrane virology, HIV-1 physiology, Phosphatidylinositol 4,5-Diphosphate metabolism, Virus Assembly, gag Gene Products, Human Immunodeficiency Virus metabolism
Abstract

HIV-1 assembles at the plasma membrane (PM) of infected cells. PM association of the main structural protein Gag depends on its myristoylated MA domain and PM PI(4,5)P 2 . Using a novel chemical biology tool that allows rapidly tunable manipulation of PI(4,5)P 2 levels in living cells, we show that depletion of PI(4,5)P 2 completely prevents Gag PM targeting and assembly site formation. Unexpectedly, PI(4,5)P 2 depletion also caused loss of pre-assembled Gag lattices from the PM. Subsequent restoration of PM PI(4,5)P 2 reinduced assembly site formation even in the absence of new protein synthesis, indicating that the dissociated Gag molecules remained assembly competent. These results reveal an important role of PI(4,5)P 2 for HIV-1 morphogenesis beyond Gag recruitment to the PM and suggest a dynamic equilibrium of Gag-lipid interactions. Furthermore, they establish an experimental system that permits synchronized induction of HIV-1 assembly leading to induced production of infectious virions by targeted modulation of Gag PM targeting.

Published
2017
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