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EIF3i affects vesicular stomatitis virus growth by interacting with matrix protein
Wei Pan1, Deguang Song1, Wenqi He1
1Key Laboratory of Zoonosis, Ministry of Education, College of Veterinary Medicine, Jilin University, 5333 Xi'an Road, Changchun, 130062, China.
Veterinary Microbiology
|November 28, 2017
Summary
Vesicular stomatitis virus (VSV) matrix protein interacts with eukaryotic translation initiation factor 3, subunit i (eIF3i). This interaction influences viral replication and host antiviral responses, impacting VSV infection dynamics.
Area of Science:
- Virology
- Molecular Biology
- Cellular Biology
Background:
- The VSV matrix (M) protein is crucial for viral replication and modulates host signaling pathways.
- Understanding M protein interactions is key to deciphering VSV pathogenesis.
Purpose of the Study:
- To identify cellular partners interacting with the VSV M protein.
- To investigate the role of the identified partner, eIF3i, in VSV replication and host response.
Main Methods:
- Yeast two-hybrid system to screen for M protein interactors.
- GST pull-down and laser confocal microscopy for interaction validation.
- RNA interference for gene knockdown and mutagenesis for protein analysis.
Main Results:
- eIF3i was identified as an M-binding partner, with interaction mapped to M amino acids 122-181.
- eIF3i knockdown initially decreased, then increased VSV replication and transcription.
- eIF3i modulated Akt1 activity and the expression of ISGs regulated by phospho-Akt1.
Conclusions:
- eIF3i plays a complex role in VSV replication, affecting early and late stages.
- eIF3i influences VSV pathogenesis by regulating the host antiviral response via the Akt1 pathway.
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