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m6A Regulates the Stability of Cellular Transcripts Required for Efficient KSHV Lytic Replication
Oliver Manners1, Belinda Baquero-Perez2, Timothy J Mottram1
1School of Molecular and Cellular Biology, Faculty of Biological Sciences and Astbury Centre of Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
Viruses
|June 28, 2023
Summary
The study reveals that N6-methyladenosine (m6A) RNA modification is vital for Kaposi's sarcoma-associated herpesvirus (KSHV) replication. It stabilizes GPRC5A mRNA, which regulates viral lytic replication through NF-κB signaling.
Area of Science:
- Molecular Biology
- Epigenetics
- Virology
Background:
- N6-methyladenosine (m6A) is a key epitranscriptomic modification in mammals, regulating mRNA fate and cellular processes.
- Kaposi's sarcoma-associated herpesvirus (KSHV) infection involves dynamic changes in m6A modification patterns on viral and host mRNAs.
- KSHV reactivation from latency is a critical step in viral pathogenesis.
Purpose of the Study:
- To investigate the role of m6A in cellular transcripts during KSHV lytic replication.
- To elucidate the function of GPRC5A mRNA, upregulated during KSHV infection.
- To understand how m6A-mediated regulation of cellular genes impacts viral replication.
Main Methods:
- Analysis of m6A modification patterns in KSHV-infected cells.
- Quantification of GPRC5A mRNA stability and expression.
- Investigation of GPRC5A's role in KSHV lytic replication and NF-κB signaling pathways.
Main Results:
- m6A modification is essential for the stability of GPRC5A mRNA, which is induced by KSHV's RTA protein.
- GPRC5A expression is upregulated during KSHV lytic replication.
- GPRC5A directly regulates NF-κB signaling, promoting efficient KSHV lytic replication.
Conclusions:
- m6A plays a critical role in stabilizing cellular GPRC5A mRNA during KSHV infection.
- GPRC5A is a key cellular factor essential for KSHV lytic replication, mediated through NF-κB signaling.
- This study underscores the significance of epitranscriptomic regulation in viral-host interactions.
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