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SUMO Modification Stabilizes Enterovirus 71 Polymerase 3D To Facilitate Viral Replication
Yan Liu1, Zhenhua Zheng2, Bo Shu1
1Key Laboratory of Special Pathogens and Biosafety, Center for Emerging Infectious Diseases, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, China.
Journal of Virology
|September 16, 2016
Summary
Viruses like enterovirus 71 (EV71) use host cell modifications, including SUMOylation and ubiquitination, to replicate. These processes enhance viral polymerase stability and activity, offering potential targets for antiviral therapies.
Area of Science:
- Virology
- Molecular Biology
- Posttranslational Modifications
Background:
- Viruses, such as enterovirus 71 (EV71), exploit host cellular machinery for replication.
- Posttranslational modifications (PTMs), including ubiquitination and SUMOylation, are crucial for regulating protein function and cellular processes.
- The interplay between SUMOylation and ubiquitination in viral infection is not well understood.
Purpose of the Study:
- To investigate the role of SUMOylation and ubiquitination in enterovirus 71 (EV71) replication.
- To identify the specific SUMOylation sites on the EV71 3D protein (RNA-dependent RNA polymerase).
- To elucidate how these PTMs influence viral polymerase activity and stability.
Main Methods:
- Bioinformatics prediction and site-directed mutagenesis to identify SUMOylation sites on EV71 3D protein.
- In vitro primer-dependent polymerase assays to assess the impact of SUMOylation site mutations.
- Analysis of SUMOylation and ubiquitination levels during EV71 infection and in vitro.
- Investigation of the relationship between SUMOylation and ubiquitination of the 3D protein.
Main Results:
- The EV71 3D protein is modified by SUMOylation (small ubiquitin-like modifier 1) during infection and in vitro.
- Specific residues (K159 and L150/D151/L152) were identified as critical for 3D SUMOylation.
- Mutations at SUMOylation sites impaired 3D polymerase activity and viral replication.
- 3D protein ubiquitination is SUMOylation-dependent, and SUMOylation enhances 3D protein stability.
- Increased SUMO-1 levels augmented 3D SUMOylation and ubiquitination, enhancing EV71 replication.
Conclusions:
- SUMOylation and ubiquitination cooperatively regulate EV71 infection, enhancing viral polymerase stability and activity.
- The interplay between SUMOylation and ubiquitination, potentially through hybrid chains or sequential modification, is crucial for efficient EV71 replication.
- Targeting these PTMs offers a potential therapeutic strategy against EV71 and other enteroviruses.
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