Ion channel structure and function of the MERS coronavirus E protein
Name
sciadv.adx1788.pdf
Description
Published version
Size
1.63 MB
Format
Adobe PDF
Checksum (MD5)
dbb781042d556375c27d510b526ca5a3
Author(s)
Sučec, Iva
Xia, Bingqing
Somberg, Noah H
Wang, Yi
Jo, Hyunil
Li, Shuangqu
Perrone, Barbara
Gao, Zhaobing
Hong, Mei
Date Issued
July 9, 2025
Journal
Science Advances
Publisher
American Association for the Advancement of Science
Citation
Iva Sučec et al., Ion channel structure and function of the MERS coronavirus E protein. Sci. Adv. 11, eadx1788 (2025).
Version
Final published version
Abstract
Coronavirus envelope (E) proteins form drug-targeted ion channels that cause virulence to infected cells. The Middle East respiratory syndrome (MERS) virus has high mortality rates, but its E structure and function are unknown. We report the single-channel conductance and structure of membrane-bound MERS E protein. MERS E conducts K+ ions with a unitary conductance of 113 picosiemens, fivefold larger than the conductance of severe acute respiratory syndrome coronavirus 2 E. Solid-state nuclear magnetic resonance data indicate that the MERS E transmembrane domain forms a five-helix bundle that spans the lipid bilayer. The amino-terminal helical interface features multiple interacting phenylalanine (Phe) residues and an asparagine (Asn), whereas the carboxyl-terminal channel pore contains Phe33. Mutation of Phe17 abolished K+ conductance, whereas mutations of Phe33 and Asn15 suppressed most channel activity. These results indicate that MERS E contains two Phe-centered ion-conduction apparatuses, which likely permeate ions through cation-π interactions, providing the structural basis for developing antiviral drugs to inhibit this pathogenic viroporin.
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Creative Commons Attribution-NonCommercial
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DOI of Published Version
https://doi.org/10.1126/sciadv.adx1788
