AI Article Synopsis
- Sirtuin 1 (SIRT1) is a lysine deacetylase involved in various physiological processes, but its role during viral infections in crustaceans, particularly in the red claw crayfish, is not well understood.
- Gene knockdown of SIRT1 in crayfish cells was found to inhibit the transcription of a viral gene, while activating SIRT1 increased the replication of the white spot syndrome virus (WSSV).
- SIRT1 was shown to co-localize and interact with key viral envelope proteins, suggesting a significant role in WSSV infection and revealing new insights into the function of lysine deacetylases in crustaceans.
Article Abstract
Sirtuin 1 (SIRT1), a member of the class III lysine deacetylases, exhibits powerful functional diversity in physiological processes and disease occurrences. However, the potential molecular mechanism underlying the role of SIRT1 during viral infection in crustaceans is poorly understood. Herein, SIRT1 was functionally characterized from the red claw crayfish , which possesses typically conserved deacetylase domains and strong evolutionary relationships across various species. Moreover, gene knockdown of SIRT1 in crayfish haematopoietic tissue (Hpt) cell culture inhibited white spot syndrome virus (WSSV) late envelope gene transcription. In contrast, enhancement of deacetylase activity using a pharmacological activator promoted the replication of WSSV. Mechanically, SIRT1 was co-localized with viral envelope protein VP28 in the nuclei of Hpt cells and directly bound to VP28 with protein pulldown and co-immunoprecipitation assays. Furthermore, SIRT1 also interacted with another two viral envelope proteins, VP24 and VP26. To the best of our knowledge, this is the first report that WSSV structural proteins are linked to lysine deacetylases, providing a better understanding of the role of SIRT1 during WSSV infection and novel insights into the basic mechanism underlying the function of lysine deacetylases in crustaceans.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9414731 | PMC |
| http://dx.doi.org/10.3390/v14081733 | DOI Listing |
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