The toxin, called a retron, is produced by bacteria as a defense mechanism against viruses. Retrons are small pieces of DNA that can insert themselves into the genome of a virus, disrupting its ability to replicate. However, retrons are only active when they are bound to a specific protein called a chaperone.
The researchers found that the chaperone protein binds to the retron at a specific site, causing a conformational change that exposes the retron's active site. This allows the retron to insert itself into the viral genome and disrupt its replication.
"This is the first time that the molecular switch that activates a retron has been identified," said Eric Snijder, professor of molecular genetics and microbiology at UT Austin. "This discovery could lead to new treatments for viral infections by designing drugs that inhibit the interaction between the chaperone protein and the retron."
The researchers believe that retrons could be used to treat a variety of viral infections, including those caused by influenza, hepatitis C and HIV. Retrons could also be used to develop new vaccines against viruses.
"Retrons are a promising new class of antiviral agents," Snijder said. "We are excited to explore their potential for treating viral infections."
The research was published in the journal Nature Structural & Molecular Biology.
