Nejvíce citovaný článek - PubMed ID 38517277
A myristoyl switch at the plasma membrane triggers cleavage and oligomerization of Mason-Pfizer monkey virus matrix protein
We explored how a simple retrovirus, Mason-Pfizer monkey virus (M-PMV) to facilitate its replication process, utilizes DHX15, a cellular RNA helicase, typically engaged in RNA processing. Through advanced genetic engineering techniques, we showed that M-PMV recruits DHX15 by mimicking cellular mechanisms, relocating it from the nucleus to the cytoplasm to aid in viral assembly. This interaction is essential for the correct packaging of the viral genome and critical for its infectivity. Our findings offer unique insights into the mechanisms of viral manipulation of host cellular processes, highlighting a sophisticated strategy that viruses employ to leverage cellular machinery for their replication. This study adds valuable knowledge to the understanding of viral-host interactions but also suggests a common evolutionary history between cellular processes and viral mechanisms. This finding opens a unique perspective on the export mechanism of intron-retaining mRNAs in the packaging of viral genetic information and potentially develop ways to stop it.
- Klíčová slova
- DEAH-box RNA helicase, DHX15, G-patch, gRNA packaging, retrovirus,
- MeSH
- buněčné jádro metabolismus virologie MeSH
- DEAD-box RNA-helikasy metabolismus genetika MeSH
- genom virový MeSH
- HEK293 buňky MeSH
- lidé MeSH
- Masonův-Pfizerův opičí virus * genetika metabolismus fyziologie MeSH
- replikace viru genetika fyziologie MeSH
- RNA virová * metabolismus genetika MeSH
- RNA-helikasy metabolismus genetika MeSH
- sestavení viru * genetika fyziologie MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- DEAD-box RNA-helikasy MeSH
- DHX15 protein, human MeSH Prohlížeč
- RNA virová * MeSH
- RNA-helikasy MeSH