Enterovirus 71 and TRIM38 Interaction
Author Information
Author(s): Liu Xinlei, Lei Xiaobo, Zhou Zhuo, Sun Zhenmin, Xue Qinghua, Wang Jianwei, Hung Tao
Primary Institution: State Key Laboratory of Molecular Virology and Genetic Engineering, Institute of Pathogen Biology, Peking Union Medical College & Chinese Academy of Medical Sciences
Hypothesis
TRIM38 functions as an E3 ubiquitin ligase and is degraded during enterovirus 71 infection.
Conclusion
TRIM38 has E3 ubiquitin ligase activity and is degraded during enterovirus 71 infection, suggesting its role in viral pathogenesis.
Supporting Evidence
- TRIM38 is localized in the cytoplasm and increases ubiquitination of cellular proteins.
- Enterovirus 71 infection leads to the degradation of TRIM38.
- An intact RING domain is crucial for TRIM38's E3 ligase activity.
Takeaway
TRIM38 is a protein that helps control other proteins in our cells, and when a virus called enterovirus 71 infects cells, it makes TRIM38 disappear.
Methodology
The study involved characterizing TRIM38's E3 ligase activity through ex vivo ubiquitylation assays and analyzing its expression in response to EV71 infection using qRT-PCR and Western blot.
Digital Object Identifier (DOI)
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