Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid binding.

ABSTRACT: The envelope glycoprotein gp41 mediates the process of membrane fusion that enables entry of the HIV-1 virus into the host cell. Strong lipid affinity of the ectodomain suggests that its heptad repeat regions play an active role in destabilizing membranes by directly binding to the lipid bilayers and thereby lowering the free-energy barrier for membrane fusion. In such a model, immediately following the shedding of gp120, the N-heptad and C-heptad helices dissociate and melt into the host cell and viral membranes, respectively, pulling the destabilized membranes into juxtaposition, ready for fusion. Post-fusion, reaching the final 6-helix bundle (6 HB) conformation then involves competition between intermolecular interactions needed for formation of the symmetric 6 HB trimer and the membra

SUBMITTER: Roche J 

PROVIDER: S-EPMC4398632 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature