Overview
- The study, published in Cell Reports and reported by CCMB on Tuesday, Sept. 29, shows that RNA G‑quadruplexes (rG4s) formed by influenza and SARS‑CoV‑2 can bind the neuronal protein alpha‑synuclein and speed its conversion into amyloid aggregates linked to Parkinson’s disease.
- Researchers found that the RNA helicase DDX39A moves from the nucleus into the cytoplasm during infection, binds both rG4s and alpha‑synuclein, and can unwind rG4s to reduce viral replication and slow amyloid formation in infected cells.
- The authors describe a molecular trade‑off: DDX39A’s interaction with alpha‑synuclein increases its rG4‑unwinding activity but may also alter protein phase behaviour in ways that can favor aggregation under some conditions.
- The findings come from peer‑reviewed experiments in infected cells and provide a plausible molecular bridge between respiratory RNA‑virus infection and processes seen in Parkinson’s, but they do not demonstrate that ordinary infections cause Parkinson’s in people.
- CCMB researchers are now pursuing animal models, longer‑term cellular studies and population research to test whether routine or repeated viral exposures cause cumulative molecular changes that raise long‑term neurodegenerative risk and to clarify what this means for patients and public health.