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Updated: Jan 26, 2026

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes
09:35

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Published on: February 9, 2009

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MORC3 Is a Target of the Influenza A Viral Protein NS1

Yi Zhang1, JaeWoo Ahn1, Kelsie J Green2

  • 1Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.

Structure (London, England : 1993)
|April 23, 2019
PubMed

Insights

The influenza H3N2 virus NS1 protein binds to Microrchidia 3 (MORC3), a human ATPase involved in autoimmune disorders. This interaction disrupts MORC3

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Microrchidia 3 (MORC3) is a human ATPase implicated in autoimmune disorders.
  • MORC3's role in regulating influenza A virus has been described as both positive and negative.

Purpose of the Study:

  • To investigate the interaction between the MORC3 CW domain and the influenza H3N2 NS1 protein.
  • To elucidate the structural and functional consequences of this interaction on MORC3 activity and viral infectivity.

Main Methods:

  • X-ray crystallography to determine the complex structure of MORC3-CW and NS1.
  • Biochemical assays to measure binding affinities.
  • Cellular analyses to assess the impact on viral infectivity and immune response.

Main Results:

  • The C-terminal tail of influenza H3N2 NS1 protein targets the CW domain of MORC3.
  • NS1 binds to the MORC3-CW domain at the same site occupied by histone H3.
  • NS1 binding competes with histone H3, releasing MORC3 autoinhibition and activating its catalytic function.

Conclusions:

  • The influenza NS1 protein can modulate MORC3 activity by competing with its host ligand, histone H3.
  • MORC3 plays a role in the cellular immune response to influenza virus infection.
  • Targeting the MORC3-NS1 interaction may offer a novel strategy against influenza virus.
Keywords:
ATPaseCWMORC3NS1chromatinhistoneimmunereaderstructurevirus

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