Structure of a protein that helps coronavirus replicate
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The protein, called the envelope protein E, plays a key role in the virus’s ability to replicate itself and stimulate the host cell’s inflammation response.
- If ways could be devised to block this pathway of the virus, it may help reduce the pathogenicity of the virus and interfere with viral replication.
- The binding sites of two drugs that block the channel used by the envelope protein E.
- These drugs bind weakly, however, and they would not be effective inhibitors of the E protein.
- It is made of bundles of several helical proteins.
- The researchers were able to clone and purify the E protein in two-and-a-half months.
- They then analysed it with nuclear magnetic resonance (NMR) spectroscopy for two months.
- They found that the part of the E protein assembles into a bundle of five helices.
- The helices remain largely immobile within this bundle, creating a tight channel.
- At one end of the channel, there were several amino acids that may attract positively charged ions such as calcium into the channel.
- The structure they have described is the closed state of the channel.
- The determination of the structure of the open state, which should shed light on how the channel opens and closes.
- The researchers also found that two drugs — amantadine, used to treat influenza, and hexamethylene amiloride, used to treat high blood pressure — can block the entrance of the E channel.
- If stronger inhibitors could be developed, they could be potential drug candidates to treat Covid-19.