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Updated: Jul 9, 2025
Isolation and Quantification of Epstein-Barr Virus from the P3HR1 Cell Line
Published on: September 28, 2022
TRIM26 restricts Epstein-Barr virus infection in nasopharyngeal epithelial cells through K48-linked ubiquitination of
Mingjiao Zhang1,2,3, Haiqi Tan2,3, Yibing Gong2,3
1Department of Laboratory Medicine, Nanfang Hospital, Southern Medical University, Guangzhou, China.
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.
Insights
Tripartite interaction motif 26 (TRIM26) protein suppresses Epstein-Barr virus (EBV) infection by degrading EphA2, a key viral entry receptor. This discovery offers a potential therapeutic target for EBV-related diseases.
Area of Science:
- Virology
- Immunology
- Cell Biology
Background:
- The Tripartite Interaction Motif (TRIM) protein family exhibits diverse antiviral mechanisms, including immune regulation and autophagy.
- Epstein-Barr virus (EBV) establishes lifelong infections, particularly in nasopharyngeal epithelial cells, utilizing specific cellular receptors for entry.
Purpose of the Study:
- To elucidate the role of Tripartite Interaction Motif 26 (TRIM26) in regulating Epstein-Barr virus (EBV) infection.
- To investigate the molecular mechanism by which TRIM26 influences EBV entry into nasopharyngeal epithelial cells.
Main Methods:
- Analysis of TRIM26 expression levels following EBV infection in nasopharyngeal epithelial cells.
- Investigation of TRIM26 interaction with heat shock protein 90-beta (HSP-90β) and its subsequent ubiquitination and proteasomal degradation.
- Assessment of the impact of TRIM26 on EphA2 receptor integrity and EBV infectivity.
Main Results:
- TRIM26 expression is upregulated upon EBV infection.
- TRIM26 interacts with HSP-90β, promoting its polyubiquitination and proteasomal degradation.
- The degradation of HSP-90β by TRIM26 leads to compromised EphA2 receptor integrity, thereby suppressing EBV infection.
Conclusions:
- TRIM26 plays a critical role in restricting EBV infection by targeting the EphA2 entry pathway via HSP-90β modulation.
- TRIM26 represents a potential therapeutic target for developing novel interventions against EBV infection and associated pathologies.
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