Enzyme weak point found as the key against SARS-CoV-2 – healing practice

COVID-19: Target structure for new therapeutic approaches

Despite intensive research, there is still no causal treatment available for the COVID-19 disease caused by the SARS-CoV-2 coronavirus. But researchers have now found indications that an enzyme could cause the virus to doom.

Corona vaccinations have started in numerous countries, but hopes continue to be directed towards being able to better treat the disease COVID-19 caused by the pathogen. Researchers are now reporting that they have discovered a target structure for new therapeutic approaches.

No causal treatment possible yet

A causal treatment of the disease COVID-19 caused by the coronavirus SARS-CoV-2 is currently not available. The focus is therefore on treatment measures against the prevailing symptoms.

The virus itself must be fought by the body’s own defenses, it says on the portal “gesund.bund.de“Of the Federal Ministry of Health.

Researchers from Marburg, the Netherlands and Russia have now gained new insights into possible treatment options for COVID-19.

New antiviral therapy approaches

Can an enzyme present in all coronaviruses cause the COVID-19 (SARS-CoV-2) pathogen to doom? According to a recent Message of the Justus Liebig University in Giessen, these results from the working group of the Giessen virologist Prof. Dr. John Ziebuhr in collaboration with scientists from the Philipps University of Marburg as well as from the Netherlands and Russia.

With an evolutionarily conserved enzyme activity, the researchers have identified a possible target structure for new antiviral therapeutic approaches for COVID-19 diseases. The study is published in the renowned specialist journal “PNAS“Has been published.

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Preserved with all known coronaviruses

As explained in the communication, the genetic material of coronaviruses consists of RNA, which is multiplied by an RNA polymerase in the course of virus replication.

Coronaviral RNA polymerases have an additional protein domain called NiRAN. This can only be found in viruses of the Nidovirales order, which also includes coronaviruses.

In their study, the researchers were able to show that this additional domain is essential for virus replication. It catalyzes a chemical modification called protein NMPylation.

The RNA polymerase interacts with another protein of the viral replication-transcription complex by means of its NiRAN domain and transfers a nucleoside monophosphate (NMP), which is obtained from the cleavage of a nucleoside triphosphate (NTP).

The scientists were also able to determine the target molecule of this NMPylation in their study: the NMP is transferred to a small viral RNA binding protein called nsp9. According to the experts, this enzymatic reaction takes place very specifically, and the amino acid residues involved are conserved in all known coronaviruses.

Point of attack for the development of new drugs

“Our data provide experimental evidence that both the NiRAN activity and the specific nsp9-NMPylation are essential for coronavirus replication,” explains Prof. Ziebuhr.

“The study provides an excellent basis for functional studies of other nidovirus NMPylation activities and offers a possible target for the development of new antiviral drugs.” (Ad)

Author and source information

Sources:

  • Justus Liebig University Giessen: New target structure for COVID-19 therapies discovered, (accessed: 25.01.2021), Justus-Liebig university of Giessen
  • Heiko Slanina, Ramakanth Madhugiri, Ganesh Bylapudi, Karin Schultheiß, Nadja Karl, Anastasia Gulyaeva, Alexander E. Gorbalenya, Uwe Linne and John Ziebuhr: Coronavirus replication–transcription complex: Vital and selective NMPylation of a conserved site in nsp9 by the NiRAN-RdRp subunit; in: PNAS, (veröffentlicht: 20.01.2021), PNAS
  • Federal Ministry of Health: COVID-19: an overview of the disease, (accessed: 25.01.2021), gesund.bund.de

Important NOTE:
This article is for general guidance only and should not be used for self-diagnosis or self-treatment. He can not substitute a visit at the doctor.

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