Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes from ³¹P NMR.

ABSTRACT: HIV-1 entry into cells requires coordinated changes of the conformation and dynamics of both the fusion protein, gp41, and the lipids in the cell membrane and virus envelope. Commonly proposed features of membrane deformation during fusion include high membrane curvature, lipid disorder, and membrane surface dehydration. The virus envelope and target cell membrane contain a diverse set of phospholipids and cholesterol. To dissect how different lipids interact with gp41 to contribute to membrane fusion, here we use ³¹P solid-state NMR spectroscopy to investigate the curvature, dynamics, and hydration of POPE, POPC and POPS membranes, with and without cholesterol, in the presence of a peptide comprising the membrane proximal external region (MPER) and transmembrane domain (TMD) of

SUBMITTER: Sutherland M 

PROVIDER: S-EPMC8826538 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature