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NSUN2 mediates distinct pathways to regulate enterovirus 71 replication.

Lishi Liu1, Zhen Chen2, Kui Zhang1

  • 1Center for Emerging Infectious Diseases, Wuhan Institute of Virology, Center for Biosafety Mega-Science, Chinese Academy of Sciences, Wuhan, Hubei, 430071, China; University of Chinese Academy of Sciences, Beijing, 100049, China.

Virologica Sinica
|May 20, 2024
PubMed
Summary
This summary is machine-generated.

The methyltransferase NSUN2 modifies viral RNA with 5-methylcytosine (m5C), enhancing enterovirus 71 (EV71) replication and stability. NSUN2 also stabilizes viral protein VP1, crucial for EV71 pathogenicity.

Keywords:
5-methylcytosineEnterovirus 71NSUN2PathogenicityUbiquitination

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Area of Science:

  • Virology
  • Molecular Biology
  • Epigenetics

Background:

  • The methyltransferase NSUN2 catalyzes 5-methylcytosine (m5C) modifications on viral RNAs, impacting viral replication.
  • While m5C deposition is understood, NSUN2's broader roles in viral replication are largely unknown.

Purpose of the Study:

  • To map m5C residues on enterovirus 71 (EV71) RNAs modified by NSUN2.
  • To elucidate the multifaceted roles of NSUN2 and m5C modifications in the EV71 life cycle.

Main Methods:

  • Mapping of m5C residues on EV71 RNAs.
  • Analysis of NSUN2 binding to viral protein VP1.
  • Assessment of viral replication and pathogenicity in mice following m5C mutation.

Main Results:

  • NSUN2-catalyzed m5C modifications enhance EV71 RNA translational efficiency and stability.
  • NSUN2 binds viral protein VP1, inhibiting its ubiquitination and increasing stability.
  • Mutation of m5C residues significantly attenuates EV71 replication and pathogenicity in mice.

Conclusions:

  • NSUN2 regulates EV71 replication through distinct pathways, including m5C RNA modifications and VP1 protein stabilization.
  • m5C modifications on EV71 RNAs are critical for viral replication and pathogenicity.