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A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
13:56

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

Published on: July 18, 2013

Exploration of binary virus-host interactions using an infectious protein complementation assay.

Sandie Munier1, Thomas Rolland, Cédric Diot

  • 1Institut Pasteur, Unité de Génétique Moléculaire des Virus à ARN, Département de Virologie, F-75015 Paris, France;

Molecular & Cellular Proteomics : MCP
|July 3, 2013
PubMed
Summary

This study introduces a new method to map virus-host interactions during infection, identifying novel protein interactions for influenza A virus and revealing its subversion of host cell transport pathways.

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Area of Science:

  • Virology
  • Molecular Biology
  • Infectious Diseases

Background:

  • Accurate mapping of pathogen-host interactions is crucial for understanding infection and pathogenesis.
  • Current interactomics methods like yeast two-hybrid and tandem affinity purification mass spectrometry have limitations in recapitulating infection dynamics or distinguishing direct interactions.
  • There is a need for novel technologies to improve the mapping of pathogen-host interactions during actual viral infections.

Purpose of the Study:

  • To develop and validate a new protein-protein interaction mapping strategy for influenza A virus during infection.
  • To identify novel host proteins interacting with the influenza A virus polymerase.
  • To investigate the role of identified host factors in viral replication and pathogenesis.

Main Methods:

  • Engineered infectious recombinant influenza A viruses encoding a Gluc1-tagged polymerase subunit.
  • Infected cultured cells transiently expressing Gluc2-tagged host proteins involved in nucleocytoplasmic trafficking.
  • Utilized a trans-complementation assay based on Gaussia princeps luciferase fragments for detecting binary interactions.
  • Performed gene silencing experiments to validate the role of identified interactors.

Main Results:

  • Successfully detected known and identified novel binary interactions between influenza A virus polymerase and host proteins during infection.
  • Revealed 30% novel viral-host protein-protein interactions in an exploratory set.
  • Identified nucleocytoplasmic trafficking proteins, including NUP62, NXF1, RMB15B, and DDX19B, as novel interactors of the viral polymerase.
  • Demonstrated that NUP62 is essential for efficient viral replication.

Conclusions:

  • The developed infectious protein complementation assay is sensitive and accurate for mapping viral-host interactions in infected cells.
  • Influenza A viruses subvert host nucleocytoplasmic trafficking pathways, involving identified host factors like NUP62.
  • This strategy holds potential for high-throughput interactomics studies of various pathogens.