What is it about?
Bornavirus is a virus that infects mammals and occasionally humans, sometimes leading to severe brain infections (encephalitis). Currently, there are no approved treatments or vaccines. Like many viruses, bornavirus depends on a molecular machine called a polymerase to copy its genetic material and produce more virus inside infected cells. This study reports the cryo-electron microscopy (cryo-EM) structures of the bornavirus polymerase and shows how it adopts multiple working states. These findings provide important insights into how the polymerase functions and may help guide the development of future antiviral drugs.
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Photo by National Institute of Allergy and Infectious Diseases on Unsplash
Why is it important?
1. By seeing how the polymerase changes shape, we can understand the steps required for it to make new virus. That helps us target the right part of the enzyme to stop it with drugs. 2. Because bornavirus polymerase has unique features (not found in all viruses) and the study shows how it responds dynamically to RNA/NTP binding, it opens potential ways to design specific antiviral drugs that are likely less toxic, because they can differ from human polymerases. 3. These insights could help in developing treatments, since bornavirus infection can be deadly and there are no current approved therapies.
Perspectives
Writing this article was an exciting journey, as it allowed us to tackle a virus that is still poorly understood but has serious health implications. I hope this work not only helps researchers in structural biology and virology but also sparks new interest in targeting viral polymerases for drug development. More than anything, I hope it inspires others to see how detailed molecular structures can translate into real opportunities for therapies against devastating infections.
Bin Liu
University of Minnesota Twin Cities
Read the Original
This page is a summary of: Structural insights into the dynamic mechanism of bornavirus polymerase, Proceedings of the National Academy of Sciences, September 2025, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2504779122.
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