Influenza A matrix protein M1 induces lipid membrane deformation via protein multimerization

Ismail Dahmani1, Kai Ludwig2, Salvatore Chiantia3

  • 1University of Potsdam, Institute of Biochemistry and Biology, Karl-Liebknecht-Str. 24-25, Potsdam 14476, Germany.

Bioscience Reports
|July 21, 2019
PubMed

Insights

Influenza A virus matrix protein M1 induces membrane curvature essential for viral budding. Stable M1 interactions, not just binding, are key to forming a protein scaffold that deforms lipid bilayers.

Area of Science:

  • Virology
  • Biophysics
  • Cell Biology

Background:

  • The Influenza A virus (IAV) matrix protein M1 is implicated in viral assembly and budding.
  • Viral budding requires bending of the host cell's plasma membrane (PM).
  • The precise mechanism and viral proteins responsible for inducing membrane curvature remain debated.

Purpose of the Study:

  • To investigate the role of IAV matrix protein M1 in inducing membrane deformation.
  • To elucidate the biophysical mechanisms underlying M1-mediated membrane curvature in model systems.

Main Methods:

  • Utilized fluorescence microscopy, cryogenic transmission electron microscopy (cryo-TEM), and cryo-electron tomography (cryo-ET).
  • Employed scanning fluorescence correlation spectroscopy (sFCS) to analyze M1 interactions.
  • Studied M1's effect on model plasma membrane lipid bilayers.

Main Results:

  • Demonstrated that M1 induces membrane curvature in lipid bilayers containing negatively charged lipids.
  • Showed that M1 binding alone is insufficient; stable M1-M1 interactions and multimer formation are necessary.
  • Identified the formation of a protein scaffold by M1 multimers as the mechanism for bilayer restructuring.

Conclusions:

  • Matrix protein M1 actively drives membrane curvature, a critical step in Influenza A virus assembly.
  • M1 multimerization and scaffold formation are essential for M1-induced membrane deformation.
  • Physiological membrane deformation by M1 may be influenced by initial bilayer curvature and lipid domain organization.

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