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Cyclin D3 restricts SARS-CoV-2 envelope incorporation into virions and interferes with viral spread.

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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.


Funder: Lister Institute of Preventive Medicine (Lister Institute); Id:

Funder: Rosetrees Trust (Rosetrees); Id:


Fucci, SARS-CoV-2, assembly, cell cycle, cyclin D3, Humans, SARS-CoV-2, Cyclin D3, COVID-19, Pandemics, Cell Line, Virion, COVID-19 Drug Treatment

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Springer Science and Business Media LLC
Lister Institute of Preventive Medicine (Unknown)
Wellcome Trust (via Africa Health Research Institute) (107752/Z/15/Z)
Wellcome Trust (108082/A/15/Z)