2. Academic Validation
  3. TRIM26 restricts Epstein-Barr virus infection in nasopharyngeal epithelial cells through K48-linked ubiquitination of HSP-90β

TRIM26 restricts Epstein-Barr virus infection in nasopharyngeal epithelial cells through K48-linked ubiquitination of HSP-90β

  • FASEB J. 2024 Jan;38(1):e23345. doi: 10.1096/fj.202300929RR.
Mingjiao Zhang 1 2 3,  Haiqi Tan 2 3,  Yibing Gong 2 3,  Oluwasijibomi Damola Faleti 2 3 4,  Dengke Li 5,  Jinlong Yang 2 3,  Jing Huang 2 3,  Jingyi Long 2 3,  Qingshuang Luo 2 3,  Gongfa Wu 6,  Lei Zheng 1,  Xiaoming Lyu 2 3
Affiliations

Affiliations

  • 1 Department of Laboratory Medicine, Nanfang Hospital, Southern Medical University, Guangzhou, China.
  • 2 Department of Laboratory Medicine, The Third Affiliated Hospital, Southern Medical University, Guangzhou, China.
  • 3 The Third School of Clinical Medicine, Southern Medical University, Guangzhou, China.
  • 4 Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hong Kong, China.
  • 5 Guangdong Provincial Key Laboratory of Tumor Immunotherapy, Cancer Research Institute, School of Basic Medical Sciences, Southern Medical University, Guangzhou, China.
  • 6 Department of pathology, The Fourth Affiliated Hospital of Guangzhou Medical University, Guangzhou, China.
PMID: 38038978 DOI: 10.1096/fj.202300929RR
Abstract

The tripartite interaction motif (TRIM) family of proteins is known for their Antiviral activity through different mechanisms, such as interfering with viral components, regulating immune responses, and participating in autophagy-mediated defense pathways. In this study, we investigated the role of tripartite interaction motif 26 (TRIM26), which is encoded by a major histocompatibility complex (MHC) gene, in regulating Epstein-Barr virus (EBV) Infection of nasopharyngeal epithelial cells. We found that TRIM26 expression was induced upon EBV Infection and that it indirectly targeted EphA2, a crucial epithelial receptor for EBV entry. Our results showed that TRIM26 interacted with heat shock protein 90-beta (HSP-90β) and promoted its polyubiquitination, which led to its degradation via the Proteasome pathway. This, in turn, affected EphA2 integrity and suppressed EBV Infection. These findings suggest that TRIM26 could be a valuable target for developing therapeutic interventions against EBV Infection and its associated pathogenesis.

Keywords

Ephrin receptor A2 (EphA2); Epstein-Barr virus (EBV); heat shock protein 90-beta(HSP-90β); infection; tripartite interaction motif 26 (TRIM26); ubiquitination.

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