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Influenza virus M2 protein mediates ESCRT-independent membrane scission

Jeremy S Rossman1, Xianghong Jing, George P Leser

  • 1Department of Biochemistry, Northwestern University, Evanston, IL 60208, USA.

Cell
|September 21, 2010
PubMed

Insights

Influenza virus budding uses the M2 ion channel protein, not host ESCRT proteins. The M2 protein

Area of Science:

  • Virology
  • Cell Biology
  • Membrane Biology

Background:

  • Many viruses rely on host ESCRT proteins for efficient budding and release.
  • Influenza virus budding has been considered an ESCRT-independent process.

Purpose of the Study:

  • To investigate the role of the influenza virus M2 proton-selective ion channel protein in viral budding.
  • To elucidate the mechanism by which influenza virus achieves membrane scission and virion release.

Main Methods:

  • Analysis of M2 protein function in membrane curvature alteration using giant unilamellar vesicles.
  • Site-directed mutagenesis of the M2 cytoplasmic tail amphipathic helix.
  • In vivo transfection and observation of M2 protein budding and virion release.

Main Results:

  • A conserved amphipathic helix in the M2 cytoplasmic tail mediates cholesterol-dependent membrane curvature changes.
  • This M2 helix is sufficient for budding into model membranes and essential for in vivo budding.
  • M2 localizes to the budding site, and mutations in the helix prevent membrane scission and virus release.

Conclusions:

  • The influenza virus M2 protein plays a critical role in mediating the final stages of viral budding.
  • M2 facilitates membrane scission and virion release, bypassing the requirement for host ESCRT machinery.
  • This discovery offers a novel understanding of influenza virus replication strategies.

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