Structure of a Key Coronavirus Protein Determined

  • Author: ChemistryViews
  • Published: 14 November 2020
  • Copyright: Wiley-VCH GmbH
thumbnail image: Structure of a Key Coronavirus Protein Determined

Mei Hong, Massachusetts Institute of Technology (MIT), Cambridge, MA, USA, and colleagues have determined the molecular structure of a protein found in the SARS-CoV-2 virus. This envelope protein E forms a cation-selective channel and plays a key role in the ability of the virus to replicate itself and stimulate the host cell’s inflammation response. The researchers assume that blocking this channel disrupts virus replication and thus reduces the pathogenicity of the virus.

To determine the structure of the E protein, the researchers embedded it in a lipid bilayer, similar to a cell membrane, and analyzed it with solid-state NMR. The team found that the part of the E protein embedded in the lipid bilayer, the so-called transmembrane domain, assembles into a bundle of five helices. The helices remain largely immobile within this bundle, creating a homopentameric cation channel.

The SARS-CoV-2 E protein is different from adequate ion channel proteins of influenza and HIV-1 viruses. The M2 protein of influenza viruses is much more mobile and forms a much narrower channel. The Vpu protein of HIV-1 has a much shorter transmembrane helix and a wider pore. The scientists are currently investigating the effects of these differences.
In the SARS-CoV-2 E protein, the team has found several amino acids at one end of the channel that could attract positively charged ions such as calcium into the channel.

The drug amantadine, which is used to treat influenza, and hexamethyleneamiloride, which is used to treat high blood pressure, can block the entrance of the E channel. However, both drugs bind only weakly to the E protein. The researchers suspect that stronger E inhibitors are potential drug candidates for treating Covid-19.


Also of Interest

  • Collection: SARS-CoV-2 Virus
    What we know about the new coronavirus and COVID-19



Article Views: 1852

Sign in Area

Please sign in below

Additional Sign In options

Please note that to comment on an article you must be registered and logged in.
Registration is for free, you may already be registered to receive, e.g., the newsletter. When you register on this website, please ensure you view our terms and conditions. All comments are subject to moderation.

Article Comments - To add a comment please sign in

If you would like to reuse any content, in print or online, from, please contact us first for permission. more

Follow on Facebook Follow on Twitter Follow on YouTube Follow on LinkedIn Follow on Instagram RSS Sign up for newsletters

Magazine of Chemistry Europe (16 European Chemical Societies) published by Wiley-VCH