tetano
Editor, Senior Moderator
Sci Adv
. 2025 Jul 11;11(28):eadx1788.
doi: 10.1126/sciadv.adx1788. Epub 2025 Jul 9. Ion channel structure and function of the MERS coronavirus E protein
Iva Sučec[SUP] 1 [/SUP], Bingqing Xia[SUP] 2 [/SUP], Noah H Somberg[SUP] 1 [/SUP], Yi Wang[SUP] 2 [/SUP], Hyunil Jo[SUP] 3 [/SUP], Shuangqu Li[SUP] 2 [/SUP], Barbara Perrone[SUP] 4 [/SUP], Zhaobing Gao[SUP] 2 [/SUP], Mei Hong[SUP] 1 [/SUP]
Affiliations
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[SUP]+[/SUP] 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 Phe[SUP]33[/SUP]. Mutation of Phe[SUP]17[/SUP] abolished K[SUP]+[/SUP] conductance, whereas mutations of Phe[SUP]33[/SUP] and Asn[SUP]15[/SUP] 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.
. 2025 Jul 11;11(28):eadx1788.
doi: 10.1126/sciadv.adx1788. Epub 2025 Jul 9. Ion channel structure and function of the MERS coronavirus E protein
Iva Sučec[SUP] 1 [/SUP], Bingqing Xia[SUP] 2 [/SUP], Noah H Somberg[SUP] 1 [/SUP], Yi Wang[SUP] 2 [/SUP], Hyunil Jo[SUP] 3 [/SUP], Shuangqu Li[SUP] 2 [/SUP], Barbara Perrone[SUP] 4 [/SUP], Zhaobing Gao[SUP] 2 [/SUP], Mei Hong[SUP] 1 [/SUP]
Affiliations
- PMID: 40632851
- PMCID: PMC12239962
- DOI: 10.1126/sciadv.adx1788
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[SUP]+[/SUP] 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 Phe[SUP]33[/SUP]. Mutation of Phe[SUP]17[/SUP] abolished K[SUP]+[/SUP] conductance, whereas mutations of Phe[SUP]33[/SUP] and Asn[SUP]15[/SUP] 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.