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A Prion-Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing.

Xiaoyue Zhang1,2,3, Zhengshuo Li1,2,3, Run Zheng1,2,3

  • 1Hunan Cancer Hospital and The Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, Hunan, 410013, China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|July 29, 2025
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Summary

Epstein-Barr virus nuclear antigen 1 (EBNA1) is a prion-like protein that drives tumor progression. Targeting its prion-like domain inhibits cancer cell growth and promotes normal splicing, offering new therapeutic strategies.

Keywords:
EBV‐encoded nuclear antigen 1alternative splicingphase separationprion‐like domainprotein aggregation

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Area of Science:

  • Virology
  • Molecular Biology
  • Oncology

Background:

  • Epstein-Barr virus nuclear antigen 1 (EBNA1) maintains viral episomes and promotes tumor cell survival.
  • Viruses can form sub-cellular compartments called "virus factories" via liquid-liquid phase separation (LLPS).
  • Prion-like domains (PrLDs) are known to drive LLPS.

Purpose of the Study:

  • To investigate the prion-like nature of EBNA1.
  • To determine the role of EBNA1's PrLD in viral replication, genomic instability, and tumor progression.
  • To explore therapeutic strategies targeting EBNA1's PrLD.

Main Methods:

  • Bioinformatic prediction of PrLD in EBNA1.
  • Experimental validation of EBNA1 aggregation and LLPS.
  • Analysis of EBNA1 interactions with splicing factors (e.g., SRSF1).
  • Assessment of alternative splicing regulation (SRRM1).
  • In vitro and in vivo studies using nasopharyngeal carcinoma models.

Main Results:

  • A PrLD was identified in EBNA1, and EBNA1 protein aggregation was observed in EBV-positive tumors.
  • EBNA1 drives LLPS, regulates alternative splicing of SRRM1 via SRSF1 interaction, and promotes nasopharyngeal carcinoma cell proliferation.
  • Deletion of the EBNA1 PrLD impaired aggregation, LLPS, splicing regulation, and cell proliferation.
  • Targeting EBNA1's PrLD inhibited protein aggregation, restored SRRM1 splicing, and suppressed tumor progression.

Conclusions:

  • EBNA1 is a prion-like protein, contributing to oncogenesis through LLPS and alternative splicing dysregulation.
  • Targeting EBNA1's PrLD presents a potential therapeutic strategy against EBV-associated cancers.
  • The prion-like nature of EBNA1 may also imply a role in neurodegenerative diseases.