A novel curcumin derivative, C210, activates the Epstein–Barr virus (EBV) lytic cycle without producing infectious virions by disrupting HSP90. This discovery opens avenues for safer EBV-positive cancer therapies.
By Dr. Sanchari Sinha Dutta, Ph.D.Nov 5 2024 A new study reveals how C210, a curcumin derivative, selectively reactivates Epstein–Barr virus to kill cancer cells without infectious risks, paving the way for safer, targeted cancer therapies.
Background Epstein–Barr virus is a tumorigenic virus associated with a range of cancer types, including epithelial cancers and lymphomas. The virus persists in cancer cells in a latent state, and viral reactivation from the latent state to the lytic state leads to cancer cell death. Heat shock protein 90 is a molecular chaperone that promotes the proper folding and stability of several oncogenic proteins. Small-molecule inhibitors of HSP90 trigger proteasomal or autophagic degradation of HSP90 client proteins and exert antitumor effects.
Important Observations C210 specifically reduces levels of STAT3 and XPB, two proteins essential for EBV’s survival in its latent state, effectively enhancing EBV reactivation and limiting virion production. They further observed that C210-induced STAT3 degradation enhanced the cytotoxic activity and EBV-reactivating capacity of SAHA, a combination effect that resembled STAT3 knockdown results. Regarding the other HSP90 client protein, scientists found that C210-induced degradation of XPB inhibits the expression of SM-dependent late viral genes, thereby suppressing infectious virion production.
Conventional lytic inducers, such as histone deacetylase inhibitors, are known to induce the EBV lytic cycle by promoting histone acetylation. The study findings, however, show that C210 activates the EBV lytic cycle by inhibiting HSP90 function and upregulating XBP1s, two mechanisms that differ from those of established histone deacetylase inhibitors like SAHA.
Cancer Therapy Compound Curcumin Virus Carcinoma Cell Cell Death DNA Efficacy Genes Heat Protein Transcription
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