SARS-CoV-2 envelope structural protein found to form voltage-activated and calcium-activated calcium channels biorixvpreprint dundeeuni COVID19 SARSCoV2 Envelope Protein CalciumChannel
By Pooja Toshniwal PahariaOct 14 2022Reviewed by Aimee Molineux In a recent study posted to the bioRxiv* preprint server, researchers investigated severe acute respiratory syndrome coronavirus 2 envelope protein activity in terms of calcium cations cations.
About the study In the present study, researchers explored the prime physiological function of SARS-CoV-2 E upon viral infection. In addition, the effects of post-translational modifications on the E protein function were explored by palmitoylating all the cysteine residues in every subunit in the EFL pentamers of SARS-CoV-2 E protein channels. Further, the effects of luminal Ca2+ concentrations on EFL gating properties were evaluated.
The hydrophobically gated ion channel activity of the viral E protein and viroporins were regulated by elevated luminal Ca2+ concentrations , electrochemical gradients, pH, PTMs, ERGIC phospholipids with negative charges, and voltage applied to the membranes. Palmitoylation of ≥1 cysteine residue promoted the formation of open and stable E protein pores. Ca2+ ions activated ER-luminal channels and maintained the pores in the open state.
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