Journal
VIRUS RESEARCH
Volume 193, Issue -, Pages 108-115Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.virusres.2014.06.015
Keywords
HIV-1 Gag; P1(4,5)P-2; Membrane binding; Acyl chains; Virus assembly
Categories
Funding
- National Institute of Allergy and Infectious Diseases [R01 AI071727, R56 AI089282]
- American Heart Association [0850133Z]
- amfAR [107449-45-RGHF]
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The MA domain mediates plasma membrane (PM) targeting of HIV-1 Gag, leading to particle assembly at the PM. The interaction between MA and acidic phospholipids, in addition to N-terminal myristoyl moiety, promotes Gag binding to lipid membranes. Among acidic phospholipids, PI(4,5)P-2, a PM-specific phosphoinositide, is essential for proper HIV-1 Gag localization to the PM and efficient virus particle production. Recent studies further revealed that MA-bound RNA negatively regulates HIV-1 Gag membrane binding and that PI(4,5)P-2 is necessary to overcome this RNA-imposed block. In this review, we will summarize the current understanding of Gag-membrane interactions and discuss potential roles played by acidic phospholipids. (C) 2014 Elsevier B.V. All rights reserved.
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