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The Cellular DExD/H-Box RNA Helicase UAP56 Co-localizes With the Influenza A Virus NS1 Protein

Shiho Chiba1, Lindsay Hill-Batorski1, Gabriele Neumann1

  • 1Influenza Research Institute, Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin-Madison, Madison, WI, United States.

Frontiers in Microbiology
|September 28, 2018
PubMed

Insights

The RNA helicase UAP56 interacts with influenza A virus NS1 protein, which suppresses host immunity. This interaction does not impact NS1

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • UAP56 (RNA helicase) is crucial for pre-mRNA splicing and mRNA export.
  • In influenza A virus infection, UAP56 aids viral mRNA export and nucleoprotein complex formation.
  • UAP56 may influence antiviral host responses by interacting with MxA and PKR.

Purpose of the Study:

  • To investigate the interaction between UAP56 and influenza A virus NS1 protein.
  • To determine the functional relevance of the UAP56-NS1 association in the context of host innate immune responses.

Main Methods:

  • Co-localization studies to assess UAP56 and NS1 proximity in infected cells.
  • Analysis of UAP56-NS1 binding domains using specific mutations in NS1.
  • Reporter gene assays to evaluate the impact of UAP56-NS1 interaction on NS1-mediated immune suppression.

Main Results:

  • UAP56 co-localizes with influenza A virus NS1 protein.
  • The UAP56-NS1 association depends on RNA-binding residues R38 and K41 in NS1 and may involve single-stranded RNA.
  • UAP56 binding to NS1 did not alter NS1's ability to downregulate innate immune pathways in reporter assays.

Conclusions:

  • UAP56 interacts with influenza A virus NS1 protein, potentially via RNA.
  • The biological significance of the UAP56-NS1 interaction remains unclear as it does not affect NS1's immune evasion function.
Keywords:
UAP56host factorsinfluenza A NS1influenza A virusnuclear localization

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