Researchers have provided evidence of influenza-causing modifications to the enzyme, which makes copies of the influenza virus genome, and could, therefore, be used to produce new drugs. The team of researchers from Germany’s University of Muenster was able to provide evidence of 59 specific modifications to the polymerase of the influenza A virus, or, in other words, the pivotal enzyme responsible for producing copies of the virus genome.
What is special about the modifications described in the study, according to the study, is that they are transmitted by proteins in host cells – and, unlike virus proteins, they cannot mutate rapidly.
Therefore, the modifications represent a promising approach for producing new drugs, said the study published in the journal Nature Communications. Every year, the influenza season presents a challenge for hospitals.
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Older people, and especially patients with health problems, are at increased risk of developing a severe bout of influenza, even when vaccinated. What is particularly insidious about influenza viruses is their ability to mutate rapidly, which makes them increasingly resilient to drugs.
For this reason, there is an urgent need for new active ingredients to be able to provide effective treatments for the disease in the future. This study is an important step in this direction.
Influenza A virus polymerase (IAV polymerase) is a highly complex protein with more than just one function. One of these is that after structural changes, this virus can also make copies of genome, cRNA and vRNA.
Without this “switch” of functions, the virus is not able to spread. As Dr. Linda Brunotte and Dr. Franziska Guenel and a team of colleagues have now discovered, according to the study, the IAV polymerase needs to act as a “molecular switch” and bind proteins from the host cell to carry out its diverse functions. is required.
The study states that these proteins are enzymes that dock so-called ubiquitinated proteins at specific locations in the polymerase and, as a result, trigger signals to switch functions. “We were able to construct a map showing the 59 positions on the viral polymerase to which ubiquitin is attached through the host cell,” explained Brunotte, who initiated the study. reveal Achilles’ heel.” ,
The study noted that this ubiquitination had a definite effect on the activity of the polymerase at 17 sites. In addition, a specific position was discovered whose modification represents the signal for conversion and the associated switch of functions in the polymerase, the study said.
As a result, Dr. Guanel, lead author of the study, is now looking forward. “Based on our mapping of ubiquitination, further studies can now research which enzymes are specifically responsible for modification of the IAV polymerase.
“Drugs directed against these enzymes would be resistant to mutations in the influenza virus, thus demonstrating great potential for future treatments,” Guenel said.
(With inputs from PTI)