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Interaction of influenza virus proteins with nucleosomes

Inmaculada Garcia-Robles1, Hatice Akarsu, Christoph W Müller

  • 1EMBL Grenoble Outstation, BP 181, 38042 Grenoble Cedex 9, France.

Virology
|January 22, 2005
PubMed

Insights

Influenza virus ribonucleoproteins (RNPs) and M1 protein bind to histones within the cell nucleus. NS2/NEP protein did not bind to nucleosomes, impacting viral replication and nuclear release.

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Influenza virus transcription and replication occur in the host cell nucleus.
  • Viral ribonucleoproteins (RNPs) associate with the nuclear matrix upon entry.
  • Understanding RNP and protein interactions with host chromatin is crucial for viral lifecycle comprehension.

Purpose of the Study:

  • To investigate the binding interactions of influenza RNPs, M1 protein, and NS2/NEP protein with host cell nucleosomes and histones.
  • To elucidate the specific binding sites of these viral components on chromatin structures.

Main Methods:

  • Analysis of protein binding to purified nucleosomes, reconstituted histone octamers, and single histones.
  • Biochemical assays to determine binding affinities and locations.

Main Results:

  • Influenza RNPs bind to the histone tails of nucleosomes.
  • M1 protein binds to the globular domain of histone octamers.
  • NS2/NEP protein showed no detectable binding to nucleosomes.

Conclusions:

  • Viral RNPs and M1 protein interact with distinct sites on host chromatin components.
  • These interactions may influence the nuclear release of newly synthesized RNPs.
  • Findings provide insights into host-pathogen interactions during influenza virus infection.

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