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Scientists Develop Atomic-Level Resolution for Replication of Novel Coronavirus

Image credits: Rockefeller University.

Image credits: Rockefeller University.

In a recent discovery, Rockefeller scientists have arrived at an atomic-level resolution view for novel coronavirus, SARS-CoV-2 replication system developing a structural template helpful for drug developers.

Scientists across the world have been working to develop a vaccine for the cure of COVID-19, but they have not got any great breakthrough.

Several labs globally have been conducting trials of COVID-19 vaccines, however, there is no surety when a drug for combating the deadly virus will be out in the market.

Now, Rockefeller scientists have come up with an atomic-level resolution view of SARS-CoV-2's replication system. This could prove helpful for researchers in discovering new drugs for containing novel coronavirus in its tracks.

"We now have an additional structural template that can be really helpful for drug developers trying to find new compounds that could get into this molecular machine and make it stop," says Elizabeth Campbell, a research associate professor at Rockefeller.

The findings of their study have been published in Cell. The study revealed that SARS-CoV-2 duplicated itself with the help of a complex enzyme named RNA-dependent RNA polymerase, or RdRp. This enzyme does not work alone, but in tandem with a number of other proteins.

These proteins include another crucial enzyme called the helicase, which is an important component for the discovery of drugs for COVID-19.

The research divulged that some existing antivirals like remdesivir or those under investigation for the infection act on RdRp.

These drugs work by attempting to enter every part of RdRp molecule. As a result of this, they bring the replication process to a halt.

In order to produce a successful compound, scientists need to have the most detailed picture of the RdRp.

The researchers produced a 3-D map of the RdRp-helicase complex using an imaging technique called cryo-electron microscopy.

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