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In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
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Membrane remodeling by the M2 amphipathic helix drives influenza virus membrane scission

Agnieszka Martyna1, Basma Bahsoun1, Matthew D Badham1

  • 1School of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, United Kingdom.

Scientific Reports
|March 21, 2017
PubMed

Insights

The M2 protein

Area of Science:

  • Cell Biology
  • Virology
  • Biochemistry

Background:

  • Membrane scission is vital for cellular processes like endocytosis and viral budding.
  • The molecular mechanisms of protein-mediated membrane scission are not fully understood.

Purpose of the Study:

  • To investigate the role of the influenza virus M2 protein in membrane scission.
  • To elucidate the molecular details of M2-mediated scission.

Main Methods:

  • Analysis of M2 protein residues 50-61 forming an amphipathic alpha-helix (AH).
  • Investigating M2AH's interaction with lipid tails and headgroups.
  • Assessing M2AH's effect on membrane curvature, lipid ordering, and neck constriction.

Main Results:

  • The M2 protein's amphipathic alpha-helix (M2AH) binds to membranes via hydrophobic interactions.
  • M2AH induces membrane curvature and lipid ordering, leading to neck constriction and scission.
  • Similar scission mechanisms were observed for cellular proteins Arf1 and Epsin1.

Conclusions:

  • The M2 protein's amphipathic alpha-helix is a key mediator of influenza virus budding.
  • Membrane-induced amphipathic alpha-helices represent a conserved mechanism for membrane scission.
  • This mechanism is relevant across diverse biological pathways, including viral budding and endocytosis.

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