On the SARS-Cov-2 Inhibitor Track

15 Apr 2020

To develop specific anti-coronavirus therapeutics and prophylactics, the molecular mechanism that underlies viral infection must first be defined. The recent study published in Cell Research solved the X-ray crystal structure of six-helical bundle (6-HB) core of the HR1 and HR2 domains in the SARS-CoV-2 S protein S2 subunit, revealing that several mutated amino acid residues in the HR1 domain may be associated with enhanced interactions with the HR2 domain, as compared to SARS-CoV. Previously developed a pan-coronavirus fusion inhibitor, EK1, which targeted the HR1 domain, was used as a starting molecule to design a series of new inhibitors, of which EK1C4 potently inhibited the replication of 5 live human coronaviruses examined, including SARS-CoV-2. Intranasal application of EK1C4 before or after challenge with HCoV-OC43 protected mice from infection, suggesting that EK1C4 could be used for prevention and treatment of infection by the currently circulating SARS-CoV-2 and other emerging SARSr-CoVs.

 

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