PH- and Calcium-Dependent Aromatic Network in the SARS-CoV-2 Envelope Protein.

ABSTRACT: The envelope (E) protein of the SARS-CoV-2 virus is a membrane-bound viroporin that conducts cations across the endoplasmic reticulum Golgi intermediate compartment (ERGIC) membrane of the host cell to cause virus pathogenicity. The structure of the closed state of the E transmembrane (TM) domain, ETM, was recently determined using solid-state NMR spectroscopy. However, how the channel pore opens to mediate cation transport is unclear. Here, we use ¹³C and ¹⁹F solid-state NMR spectroscopy to investigate the conformation and dynamics of ETM at acidic pH and in the presence of calcium ions, which mimic the ERGIC and lysosomal environment experienced by the E protein in the cell. Acidic pH and calcium ions increased the conformational disorder of the N- and C-terminal re

SUBMITTER: Medeiros-Silva J 

PROVIDER: S-EPMC9188436 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature