Journal
EMBO JOURNAL
Volume 41, Issue 22, Pages -Publisher
WILEY
DOI: 10.15252/embj.2022111653
Keywords
assembly; cell cycle; cyclin D3; Fucci; SARS-CoV-2
Categories
Funding
- Wellcome Trust [WT108082AIA]
- Lister Institute
- Rosetrees Institute
- Cambridge NIHR BRC Cell Phenotyping Hub
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SARS-CoV-2 infection triggers redistribution of cyclin D1 and D3 from the nucleus to the cytoplasm, followed by proteasomal degradation. Cyclin D3 interacts with SARS-CoV-2 proteins and affects the assembly and release of newly produced virions, highlighting the importance of understanding the virus-host interactions.
The COVID-19 pandemic caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) presents a great threat to human health. The interplay between the virus and host plays a crucial role in successful virus replication and transmission. Understanding host-virus interactions are essential for the development of new COVID-19 treatment strategies. Here, we show that SARS-CoV-2 infection triggers redistribution of cyclin D1 and cyclin D3 from the nucleus to the cytoplasm, followed by proteasomal degradation. No changes to other cyclins or cyclin-dependent kinases were observed. Further, cyclin D depletion was independent of SARS-CoV-2-mediated cell cycle arrest in the early S phase or S/G2/M phase. Cyclin D3 knockdown by small-interfering RNA specifically enhanced progeny virus titres in supernatants. Finally, cyclin D3 co-immunoprecipitated with SARS-CoV-2 envelope (E) and membrane (M) proteins. We propose that cyclin D3 impairs the efficient incorporation of envelope protein into virions during assembly and is depleted during SARS-CoV-2 infection to restore efficient assembly and release of newly produced virions.
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