Ubiquitin protein approach may be Influenza virus’ undoing

March 20, 2023 | Biology

Influenza viruses’ stealthiness can be attributed to its ability to mutate rapidly, making them more resilient to medicines. Consequently, there is a dire need for the production of new active ingredients to be able to continuously provide effective treatment of the illness in the future.

A team from the University of Münster provided crucial evidence of 59 specific modifications to polymerase (IAV polymerase) , the enzyme responsible for the production of copies of the virus genome. Without this, the virus could not proliferate. 

Dr. Linda Brunotte, Dr. Franziska Günl, and their colleagues discovered that IAV polymerase needs proteins from host cells to play as molecular switches and execute its various functions.These proteins are enzymes which transmit ubiquitin to specific places in the polymerase, triggering the switch of functions. The production of a comprehensive map showing the 59 positions on the polymerase to which ubiquitin was attached to the host cell reveals the Achilles’ heel of influenza virus.

The ubiquitin had a distinct influence on the activity of polymerase at 17 spots. One specific position was identified where modification represents the signal for conversion and is linked to switch of functions in the polymerase. 

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 These findings meant that future studies can now explore which particular enzymes are responsible for the modification of the IAV polymerase. Medicines and treatments with great potential should be resilient and are able to attack these enzymes and stop rapid mutations from happening.

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