Press "Enter" to skip to content

A promising new drug candidate against Omicron and other SARS-CoV-2 strains is the next-generation Mpro inhibitor

More than 6.8 million people have already died as a result of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), which is to blame for the ongoing coronavirus disease 2019 (COVID-19) pandemic.

A recent study published in Nature Signal Transduction and Targeted Therapy showed that a novel Mpro inhibitor (SY110) may have antiviral properties against SARS-CoV-2 Omicron and its sublineages. Moreover, it was discovered to be effective against additional human coronaviruses, including Middle East respiratory syndrome coronavirus and severe acute respiratory syndrome coronavirus 1 (SARS-CoV-1) (MERS-CoV)Despite the fact that there are a number of COVID-19 vaccinations that are commercially accessible, their effectiveness has decreased as a result of the ongoing development of new COVID-19 variations like the Alpha, Beta, Delta, and the most recent Omicron.

Many SARS-CoV-2 variations are capable of evading immunological reactions brought either by vaccination or unintentional infection. There is a significant chance that SARS-CoV-2 will persist for a very long time, according to previous data. Thus, there is an urgent need for new antivirals against present and future SARS-CoV-2 variations in addition to more potent COVID-19 vaccines.

SARS-CoV-2 is a member of the Coronaviridae family of the coronavirus genus. This virus has 14 open reading frames (ORFs), which code for two large polyproteins, pp1a and pp1ab, as well as four structural proteins and nine auxiliary proteins. Using two cysteine proteases, specifically, the polyproteins break into sixteen non-structural proteins (NSPs)A conserved gene of the virus and its variation is Mpro, also known as 3CLpro. Moreover, the Middle East respiratory syndrome coronavirus and the severe acute respiratory syndrome coronavirus-1 (SARS-CoV-1) both include this protease (MERS-CoV).

Thirteen NSPs are generated by Mpro by cleaving pp1a and pp1b. Mechanistically, Mpro specifically recognizes and cleaves amino acid sequences, with cleavage sites most frequently found at the Leu-Gln sequence. It’s significant that no human protease has the same specificity.