HIV-1 matrix-31 membrane binding peptide interacts differently with membranes containing PS vs. PI(4,5)P₂.

ABSTRACT: Efficient assembly of HIV-1 at the plasma membrane (PM) of the T-cell specifically requires PI(4,5)P₂. It was previously shown that a highly basic region (HBR) of the matrix protein (MA) on the Gag precursor polyprotein Pr55^Gag is required for membrane association. MA is N-terminally myristoylated, which enhances its affinity to membranes. In this work we used X-ray scattering and neutron reflectivity to determine how the physical properties and structure of lipid bilayers respond to the addition of binding domain peptides, either in the myristoylated form (MA₃₁myr) or without the myristoyl group (MA₃₁). Neutron reflectivity measurements showed the peptides predominantly located in the hydrocarbon interior. Diffuse X-ray scattering showed differe

SUBMITTER: O'Neil L 

PROVIDER: S-EPMC5097034 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature