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Regulation of pH by the M2 protein of influenza A viruses

F Ciampor1, C A Thompson, S Grambas

  • 1National Institute for Medical Research, London, U.K.

Virus Research
|March 1, 1992
PubMed

Insights

Amantadine inhibits influenza A virus M2 protein, causing a conformational change in hemagglutinin (HA) and low pH expression. This highlights M2

Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Influenza A virus hemagglutinin (HA) undergoes conformational changes crucial for viral entry.
  • The M2 protein of influenza A virus plays a role in regulating the pH of intracellular vesicles.
  • Amantadine is a known inhibitor of the M2 protein.

Purpose of the Study:

  • To investigate the effect of M2 protein inhibition by amantadine on HA conformation and expression.
  • To determine the role of M2 protein in regulating vesicular and intracellular pH.
  • To elucidate the relationship between M2 protein function and HA maturation.

Main Methods:

  • Immunofluorescence studies to observe HA expression on infected cells.
  • Use of pH probes (DAMP/anti-DNP and SNARF-1) to measure vesicular and intracellular pH.
  • Employing mutant HAs with varying pH stability to estimate pH values.
  • Analysis of the impact of mutations in both HA and M2 proteins.

Main Results:

  • Amantadine-induced M2 inhibition leads to HA conformational changes and expression of the low pH form.
  • This conversion is a direct result of reduced vesicular pH during HA transport through the Golgi.
  • The M2 protein is responsible for increasing vesicular pH by up to 0.8 units and reducing intracellular pH by 0.3-0.4 units.

Conclusions:

  • The M2 protein plays a critical role in regulating intracellular and vesicular pH.
  • M2 protein function is essential for the proper maturation of the HA glycoprotein.
  • The structural and functional interplay between HA and M2 is vital for influenza virus replication.

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