Phosphatidylinositol Interactions with the SARS-CoV-2 Envelope Protein Investigated by Lipid ¹³ C Labeling and Solid-State NMR

C correlation spectra, indicating that a subpopulation of PI lipids has specific interactions with the protein. These protein-bound annular PI lipids interact with Thr, Asn and Ser residues at the N- and C-terminal ends of the transmembrane helix, likely through hydrogen bonding and other electrostatic interactions. These results provide direct evidence that the SARS E protein interact with anionic PI lipids, and this interaction may modulate cation conduction by this pathogenic viroporin.