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Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein
09:39

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein

Published on: April 21, 2015

Interferon-induced Sus scrofa Mx1 blocks endocytic traffic of incoming influenza A virus particles

Mélanie Palm1, Mutien-Marie Garigliany, François Cornet

  • 1Department of Pathology, University of Liège, FMV Sart Tilman B43, 4000 Liège, Belgium.

Veterinary Research
|February 20, 2010
PubMed

Insights

The porcine Mx1 protein (poMx1) blocks influenza A virus replication by inhibiting viral RNA transcription. It disrupts endocytic vesicle transport to late endosomes in infected cells.

Area of Science:

  • Virology
  • Molecular Biology
  • Immunology

Background:

  • Interferon-induced Mx proteins are dynamin-like GTPases with antiviral properties.
  • Some Mx protein isoforms inhibit RNA virus replication by targeting specific life cycle stages.

Purpose of the Study:

  • To investigate the antiviral activity of porcine Mx1 protein (poMx1) against influenza A virus.
  • To determine the specific step in the viral life cycle inhibited by poMx1.

Main Methods:

  • Assessing viral nucleoprotein transcript levels in cycloheximide-treated infected cells expressing poMx1.
  • Analyzing viral particle binding and internalization.
  • Evaluating endocytic vesicle trafficking and early endosome morphology in the presence of poMx1.

Main Results:

  • Porcine Mx1 significantly reduces viral nucleoprotein transcript levels, indicating a pretranscriptional block.
  • Viral binding and internalization are unaffected by poMx1.
  • poMx1 disrupts centripetal traffic of endocytic vesicles to late endosomes, altering early endosome autoantigen 1 binding and morphology.

Conclusions:

  • Porcine Mx1 protein exhibits anti-influenza A virus activity through a pretranscriptional block.
  • The antiviral mechanism involves the disruption of endocytic pathway transport to late endosomes.

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