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Published on: April 19, 2016
Rotavirus disrupts cytoplasmic P bodies during infection
Rahul Bhowmick1, Arpita Mukherjee1, Upayan Patra1
1Division of Virology, National Institute of Cholera and Enteric Diseases, P-33, C.I.T. Road, Scheme-XM, Beliaghata, Kolkata 700010, West Bengal, India.
Abstract:
Cytoplasmic Processing bodies (P bodies), the RNA-protein aggregation foci of translationally stalled and potentially decaying mRNA, have been reported to be differentially modulated by viruses. Rotavirus, the causative agent of acute infantile gastroenteritis is a double stranded RNA virus which completes its entire life-cycle exclusively in host cell cytoplasm. In this study, the fate of P bodies was investigated upon rotavirus infection. It was found that P bodies get disrupted during rotavirus infection. The disruption occurred by more than one different mechanism where deadenylating P body component Pan3 was degraded by rotavirus NSP1 and exonuclease XRN1 along with the decapping enzyme hDCP1a were relocalized from cytoplasm to nucleus. Overall the study highlights decay and subcellular relocalization of P body components as novel mechanisms by which rotavirus subverts cellular antiviral responses.
Insights
Rotavirus infection disrupts cellular Processing bodies (P bodies) by degrading key components and relocating others to the nucleus. This viral strategy helps rotavirus evade the host
Area of Science:
- Virology
- Cell Biology
- Molecular Biology
Background:
- Cytoplasmic Processing bodies (P bodies) are crucial sites for mRNA regulation, including decay.
- Viruses are known to manipulate P bodies to facilitate their replication.
- Rotavirus, a common cause of infantile gastroenteritis, replicates in the host cell cytoplasm.
Purpose of the Study:
- To investigate the impact of rotavirus infection on the integrity and function of P bodies.
- To elucidate the mechanisms by which rotavirus affects P bodies.
Main Methods:
- Confocal microscopy to visualize P body components.
- Western blotting to assess protein degradation.
- Subcellular fractionation to determine protein localization.
Main Results:
- Rotavirus infection leads to the disruption of P bodies.
- The P body component Pan3 is degraded by rotavirus non-structural protein 1 (NSP1).
- Exonuclease XRN1 and decapping enzyme hDCP1a are relocalized from the cytoplasm to the nucleus.
Conclusions:
- Rotavirus employs novel strategies involving protein degradation and subcellular relocalization to disrupt P bodies.
- These mechanisms contribute to the subversion of cellular antiviral responses by rotavirus.
- Understanding these interactions can reveal new targets for antiviral therapies.
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