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Atomic structure of the open SARS-CoV-2 E viroporin
João Medeiros-Silva1, Aurelio J Dregni1, Noah H Somberg1
1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Science Advances
|October 13, 2023
Summary
The SARS-CoV-2 envelope (E) protein forms calcium channels linked to COVID-19 inflammation. Solid-state NMR revealed the open ETM structure, detailing its ion selectivity and transport mechanism.
Area of Science:
- Structural Biology
- Virology
- Biophysics
Background:
- The SARS-CoV-2 envelope (E) protein forms cation channels in infected cells.
- E protein's calcium channel activity is linked to COVID-19-induced inflammation.
Purpose of the Study:
- To determine the open-state structure of the ETM in lipid bilayers.
- To understand the mechanism of ion permeation through the ETM.
Main Methods:
- Solid-state Nuclear Magnetic Resonance (ssNMR) spectroscopy was used.
- The study analyzed the ETM's structure within lipid bilayers.
Main Results:
- The open ETM structure features an amino-terminal chamber, a phenylalanine aromatic belt, and a constricted carboxyl-terminal pore.
- Specific residues (glutamate, threonine, phenylalanine, arginine) are crucial for channel function and ion selectivity.
- The structure elucidates how protons and calcium ions are selected and transported.
Conclusions:
- The determined open-state ETM structure provides critical insights into viroporin ion channel function.
- This structural information aids in understanding the molecular basis of SARS-CoV-2 pathogenesis and inflammation.
- The findings may inform the development of antiviral strategies targeting E protein channels.
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