Rxivist logo

Binding Mechanism of the Matrix Domain of HIV-1 Gag to Lipid Membranes

By V. Monje-Galvan, Gregory A. Voth

Posted 08 May 2020
bioRxiv DOI: 10.1101/2020.05.06.080945

Aggregation of the HIV-1 Gag protein onto the plasma membrane (PM) enables viral budding and infection propagation. Gag assembly at the membrane interface is mediated by its matrix domain (MA), the Myristoylated (Myr) N-terminus. MA targets the PM through electrostatic interactions, mainly at its highly-basic-region (HBR). The mechanism of Myr insertion and its role in protein-membrane dynamics remains unclear. Using all-atom molecular dynamics, we examined an MA unit in the vicinity of lipid bilayers that model different characteristics of the PM. Interaction with PIP2 and PS lipids is highly favored around the HBR, and is enough to keep the protein bound. Additionally, we simulated three MA units near our bilayers and quantified the collective effects of free monomers vs. formed trimers on Myr insertion events. Micro-second-long trajectories allowed us to observe Myr insertion, propose a mechanism, quantify specific interactions with lipids, and examine the response of the local membrane environment. ### Competing Interest Statement The authors have declared no competing interest.

Download data

  • Downloaded 152 times
  • Download rankings, all-time:
    • Site-wide: 76,799 out of 88,877
    • In biophysics: 3,307 out of 3,870
  • Year to date:
    • Site-wide: 22,983 out of 88,877
  • Since beginning of last month:
    • Site-wide: 20,071 out of 88,877

Altmetric data


Downloads over time

Distribution of downloads per paper, site-wide


PanLingua

Sign up for the Rxivist weekly newsletter! (Click here for more details.)


News