Structural highlights
Function
VEMP_SARS2 Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis.[HAMAP-Rule:MF_04204]
Publication Abstract from PubMed
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.
Atomic structure of the open SARS-CoV-2 E viroporin.,Medeiros-Silva J, Dregni AJ, Somberg NH, Duan P, Hong M Sci Adv. 2023 Oct 13;9(41):eadi9007. doi: 10.1126/sciadv.adi9007. Epub 2023 Oct , 13. PMID:37831764[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Medeiros-Silva J, Dregni AJ, Somberg NH, Duan P, Hong M. Atomic structure of the open SARS-CoV-2 E viroporin. Sci Adv. 2023 Oct 13;9(41):eadi9007. PMID:37831764 doi:10.1126/sciadv.adi9007
