Researchers at Purdue University may have successfully targeted the weakness of the Middle East respiratory syndrome (MERS) virus. Two Purdue professors Andrew Mesecar, PhD, and Arun Ghosh, PhD, who have been studying MERS since shortly after the virus’ discovery in 2012, led a team of researchers that identified molecules that inhibit an enzyme essential to MERS virus replication in a recent study, according to a report from Becker’s Infection Control & Clinical Quality.
The enzyme 3C-like protease was targeted within the MERS virus by the researchers. Without the enzyme, the virus cannot create more viruses to further an infection, and in order to form the virus’ dimer and shut the replication process down, a single copy of the 3C-like protease must find and bond to another identical 3C-like protease “twin,” as noted on the Becker’s Infection Control report.
The research team found that the formation of the MERS protease dimer can be stimulated by binding a third molecule at a particular site on its surface trigger the formation of a strong dimer. However, the researchers also discovered while adding inhibitor molecules to interact with the protease that, at low doses, the inhibitor increased the ability of a single MERS protease to find a twin, effectively activating the protease, according to Becker’s Infection Control report.
Mesecar states, “We were very surprised to see that this inhibitor molecule that could potentially shut down the virus may also have the potential to increase its activity. At low inhibitor concentrations we saw an increase in the protease’s activity, but at high concentrations it was shut down completely.”
According to Mesecar, the findings suggest that will be complicated to turn this inhibitor into a viable treatment, but the team will continue to investigate the interaction of the inhibitor molecule with 3C-like protease isolated from the MERS virus, as well as other potential inhibitor molecules.
Source: Becker’s Infection Control & Clinical Quality
