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Related Experiment Video

Updated: Jul 30, 2025

In Vitro ELISA Test to Evaluate Rabies Vaccine Potency

In Vitro ELISA Test to Evaluate Rabies Vaccine Potency

Published on: May 11, 2020

Trim25 restricts rabies virus replication by destabilizing phosphoprotein.

Yueming Yuan^1,2, An Fang^1,2, Zongmei Wang^1,2

¹State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, 430070, China.

|May 16, 2023

Summary

This summary is machine-generated.

Tripartite motif-containing protein 25 (Trim25) limits rabies virus replication through both E3 ubiquitin ligase-dependent and independent pathways. Trim25 destabilizes viral phosphoprotein via autophagy, independent of its ligase activity.

Keywords:

Autophagy Phosphoprotein Protein stability Rabies virus Trim25

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Last Updated: Jul 30, 2025

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Area of Science:

Virology
Immunology
Molecular Biology

Background:

Tripartite motif-containing protein 25 (Trim25) is an E3 ubiquitin ligase known to activate RIG-I and enhance interferon responses against viruses.
Emerging evidence suggests Trim25 may also exert antiviral effects by directly binding and degrading viral proteins.

Purpose of the Study:

To investigate the role and mechanism of Trim25 in rabies virus (RABV) infection.
To elucidate the specific interactions and pathways through which Trim25 modulates RABV replication and pathogenicity.

Main Methods:

Assessing Trim25 expression levels in cells and mouse brains following RABV infection.
Evaluating the effect of Trim25 expression on RABV replication in cell culture.
Analyzing the impact of Trim25 overexpression on RABV pathogenicity in a mouse model.
Identifying the specific domains and mechanisms involved in Trim25-mediated inhibition of RABV.

Main Results:

Trim25 expression was significantly upregulated in response to RABV infection in both cellular and animal models.
Overexpression of Trim25 demonstrably limited RABV replication and reduced viral pathogenicity in mice.
Trim25 inhibited RABV replication through both E3 ubiquitin ligase-dependent and independent mechanisms.
The coiled-coil domain (CCD) of Trim25 was found to interact with RABV phosphoprotein (RABV-P) at amino acid 72, leading to RABV-P destabilization via autophagy.

Conclusions:

Trim25 plays a crucial role in restricting RABV replication.
A novel antiviral mechanism was identified where Trim25 destabilizes RABV-P through autophagy, independent of its E3 ubiquitin ligase activity.
These findings reveal a new facet of Trim25's antiviral repertoire and its potential as a therapeutic target against rabies virus.