Abstract
Assembly of an infectious retroviral particle relies on multimerization of the Gag polyprotein at the inner leaflet of the plasma membrane. The three domains of Gag common to all retroviruses – MA, CA, and NC – provide the signals for membrane binding, assembly, and viral RNA packaging, respectively. These signals do not function independently of one another. For example, Gag multimerization enhances membrane binding and is more efficient when NC is interacting with RNA. MA binding to the plasma membrane is governed by several principles, including electrostatics, recognition of specific lipid head groups, hydrophobic interactions, and membrane order. HIV-1 uses many of these principles while Rous sarcoma virus (RSV) appears to use fewer. This review describes the principles that govern Gag interactions with membranes, focusing on RSV and HIV-1 Gag. The review also defines lipid and membrane behavior, and discusses the complexities in determining how lipid and membrane behavior impact Gag membrane binding.
Highlights
In enveloped viruses the common function of the viral membrane is to help protect the genome
Spuma viruses require expression of the viral envelope glycoprotein for budding to occur, and the specific interaction between Gag and Env that underlies this finding has recently been characterized (Goldstone et al, 2013). In this case the immature but not yet enveloped virus particle is assembled near the microtubule organizing center (MTOC), enveloped by budding through the endoplasmic reticulum, and transported to the plasma membrane (PM)
We focus on the most widely studied retroviruses in the genera called alpharetrovirus (e.g., Rous sarcoma virus, RSV in chickens), gammaretrovirus, deltaretrovirus, and lentiretrovirus
Summary
Reviewed by: Akira Ono, University of Michigan Medical School, USA Robert V. Indiana University School of Medicine-South Bend, USA. The three domains of Gag common to all retroviruses – MA, CA, and NC – provide the signals for membrane binding, assembly, and viral RNA packaging, respectively. These signals do not function independently of one another. Gag multimerization enhances membrane binding and is more efficient when NC is interacting with RNA. This review describes the principles that govern Gag interactions with membranes, focusing on RSV and HIV-1 Gag. The review defines lipid and membrane behavior, and discusses the complexities in determining how lipid and membrane behavior impact Gag membrane binding
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