Structure of the membrane anchor of pestivirus glycoprotein E(rns), a long tilted amphipathic helix.

ABSTRACT: E(rns) is an essential virion glycoprotein with RNase activity that suppresses host cellular innate immune responses upon being partially secreted from the infected cells. Its unusual C-terminus plays multiple roles, as the amphiphilic helix acts as a membrane anchor, as a signal peptidase cleavage site, and as a retention/secretion signal. We analyzed the structure and membrane binding properties of this sequence to gain a better understanding of the underlying mechanisms. CD spectroscopy in different setups, as well as Monte Carlo and molecular dynamics simulations confirmed the helical folding and showed that the helix is accommodated in the amphiphilic region of the lipid bilayer with a slight tilt rather than lying parallel to the surface. This model was confirmed by NMR analyses that

SUBMITTER: Aberle D 

PROVIDER: S-EPMC3937272 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature