Cholesterol-Mediated Clustering of the HIV Fusion Protein gp41 in Lipid Bilayers.

ABSTRACT: The envelope glycoprotein (Env) of the human immunodeficient virus (HIV-1) is known to cluster on the viral membrane surface to attach to target cells and cause membrane fusion for HIV-1 infection. However, the molecular structural mechanisms that drive Env clustering remain opaque. Here, we use solid-state NMR spectroscopy and molecular dynamics (MD) simulations to investigate nanometer-scale clustering of the membrane-proximal external region (MPER) and transmembrane domain (TMD) of gp41, the fusion protein component of Env. Using ¹⁹F solid-state NMR experiments of mixed fluorinated peptides, we show that MPER-TMD trimers form clusters with interdigitated MPER helices in cholesterol-containing membranes. Inter-trimer ¹⁹F-¹⁹F cross peaks, which are indicat

SUBMITTER: Tran N 

PROVIDER: S-EPMC8832541 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature