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The phosphorylation of the integral membrane (M1) protein of influenza virus

A Gregoriades1, G G Guzman, E Paoletti

  • 1Department of Basic Sciences, New York College of Podiatric Medicine, NY 10035.

Virus Research
|April 1, 1990
PubMed

Insights

Influenza virus M1 protein phosphorylation is conserved across virus types and occurs within hydrophobic regions. This suggests a crucial role for M1 protein phosphorylation in influenza virus biology.

Area of Science:

  • Virology
  • Molecular Biology
  • Protein Chemistry

Background:

  • The M1 protein is a key internal and integral membrane component of the influenza virus.
  • Understanding M1 protein modifications like phosphorylation is crucial for deciphering viral assembly and function.

Purpose of the Study:

  • To investigate the phosphorylation status of the influenza virus M1 protein.
  • To determine the conservation and location of M1 protein phosphorylation across different influenza virus types.
  • To identify the potential kinases responsible for M1 phosphorylation.

Main Methods:

  • Analysis of phosphate content in M1 protein.
  • Comparative studies across influenza A, B, and C viruses.
  • Infection of cells with vaccinia virus recombinants expressing M1 protein.
  • Cyanogen bromide fragmentation and amino acid sequence analysis.

Main Results:

  • Influenza M1 protein contains at least two moles of phosphate per mole of M1.
  • M1 protein phosphorylation is conserved among influenza A, B, and C viruses, along with other characteristics like lipid vesicle partitioning.
  • M1 protein is phosphorylated in cells infected with a vaccinia recombinant containing only the M1 gene, indicating involvement of viral or cellular kinases.
  • The phosphate group is located within or near the major hydrophobic amino acid stretch of the M1 protein.

Conclusions:

  • M1 protein phosphorylation is a conserved feature of influenza viruses.
  • The phosphorylation site is associated with the protein's hydrophobic domain, potentially influencing its interaction with membranes or other viral components.
  • Both viral and cellular kinases may contribute to M1 protein phosphorylation.

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