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Kinetic analysis of the M2 proton conduction of the influenza virus

Rafal M Pielak1, James J Chou

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, United States.

Journal of the American Chemical Society
|November 25, 2010
PubMed

Insights

The M2 protein

Area of Science:

  • Virology
  • Biophysics
  • Molecular Biology

Background:

  • The M2 protein of influenza viruses is crucial for viral replication, forming a proton-selective channel.
  • Previous models of M2 proton conduction lack detailed kinetic analysis.
  • Understanding M2 channel function is key to developing antiviral strategies.

Purpose of the Study:

  • To perform a detailed kinetic analysis of the M2 proton channel activity.
  • To elucidate the mechanism of proton conduction through the M2 channel.
  • To identify key residues influencing M2 channel conduction rates.

Main Methods:

  • Utilized a liposome proton flux assay to measure M2 protein conduction across a pH gradient.
  • Conducted detailed conduction versus pH measurements for M2 and its variants.
  • Employed Nuclear Magnetic Resonance (NMR) spectroscopy and mutagenesis for structural and functional analysis.

Main Results:

  • M2 proton transport exhibits Michaelis-Menten-like kinetics with two saturation steps.
  • Pore-lining His37 and Trp41 are central to the proton conduction mechanism.
  • Histidine protonation and M2 channel gate opening are synchronized events, influencing conduction rates.

Conclusions:

  • The study provides a detailed kinetic model for M2 proton channel function.
  • His37 and Trp41 play coordinated roles in proton transport.
  • Key residues affecting M2 channel conduction rates were identified, offering potential targets for antiviral development.

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