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Atomic structure of the open SARS-CoV-2 E viroporin.

ABSTRACT: The envelope (E) protein of the SARS-CoV-2 virus forms cation-conducting channels in the endoplasmic reticulum Golgi intermediate compartment (ERGIC) of infected cells. The calcium channel activity of E is associated with the inflammatory responses of COVID-19. Using solid-state NMR (ssNMR) spectroscopy, we have determined the open-state structure of E's transmembrane domain (ETM) in lipid bilayers. Compared to the closed state, open ETM has an expansive water-filled amino-terminal chamber capped by key glutamate and threonine residues, a loose phenylalanine aromatic belt in the middle, and a constricted polar carboxyl-terminal pore filled with an arginine and a threonine residue. This structure gives insights into how protons and calcium ions are selected by ETM and how they permeate across the hydrophobic gate of this viroporin.

SUBMITTER: Medeiros-Silva J

PROVIDER: S-EPMC10575589 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature

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Atomic structure of the open SARS-CoV-2 E viroporin.

Medeiros-Silva João J Dregni Aurelio J AJ Somberg Noah H NH Duan Pu P Hong Mei M

Science advances 20231013 41

The envelope (E) protein of the SARS-CoV-2 virus forms cation-conducting channels in the endoplasmic reticulum Golgi intermediate compartment (ERGIC) of infected cells. The calcium channel activity of E is associated with the inflammatory responses of COVID-19. Using solid-state NMR (ssNMR) spectroscopy, we have determined the open-state structure of E's transmembrane domain (ETM) in lipid bilayers. Compared to the closed state, open ETM has an expansive water-filled amino-terminal chamber cappe ...[more]

PMID: 37831764

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