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The good, the bad, and the cleaved: 14-3-3η in viral battles

The good, the bad, and the cleaved: 14-3-3η in viral battles
Illustration of the proposed model during viral infection. Credit: National Taiwan University

Scientists from NTU have made a discovery about a protein named 14-3-3η, revealing its complex role in the host's defense against RNA viruses.

Initially, 14-3-3η acts as a crucial ally in the . It works with another called MDA5 to detect and alert the immune system about the presence of RNA viruses. This is essential for mounting a swift and effective defense.

However, the story doesn't end there. Under certain circumstances, 14-3-3η can be cleaved by an enzyme known as Caspase-3, transforming it into a new form that counteracts its original function. This newly generated version of 14-3-3η can actually inhibit MDA5's activity, potentially limiting the immune response.

The paper is published in the journal PLOS Pathogens.

This dynamic interplay between 14-3-3η's dual roles is crucial for maintaining a delicate balance. The host needs to be able to effectively fight off infections, but it also needs to prevent excessive inflammation, which can be harmful. 14-3-3η helps to regulate this process, ensuring that the immune response is appropriate and controlled.

Unfortunately, some RNA viruses have evolved strategies to exploit 14-3-3η's dual nature. They can manipulate the body's signaling pathways to favor the production of the inhibitory form of 14-3-3η, allowing them to evade detection and potentially establish .

This new understanding of 14-3-3η's role in opens up exciting possibilities for therapeutic intervention. In conclusion, the discovery of 14-3-3η dual roles in the immune response against RNA viruses provides valuable insights into the complex interplay between the host and the pathogen.

By targeting the mechanisms that regulate 14-3-3η, researchers may be able to develop novel strategies to enhance the immune response against RNA viruses. Additionally, understanding how viruses manipulate 14-3-3η could lead to the development of antiviral agents that disrupt these viral tactics.

More information: Yun-Jui Chan et al, Temporal regulation of MDA5 inactivation by Caspase-3 dependent cleavage of 14-3-3η, PLOS Pathogens (2024). DOI: 10.1371/journal.ppat.1012287

Journal information: PLoS Pathogens

Provided by National Taiwan University

Citation: The good, the bad, and the cleaved: 14-3-3η in viral battles (2024, August 29) retrieved 29 August 2024 from https://phys.org/news/2024-08-good-bad-cleaved-viral.html
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