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Histones as a target for influenza virus matrix protein M1

O P Zhirnov1, H D Klenk

  • 1D. I. Ivanovsky Institute of Virology, Moscow, Russia.

Virology
|September 1, 1997
PubMed

Insights

Influenza virus matrix protein M1 specifically binds to histones, crucial cellular proteins. This interaction, involving both M1 domains, is vital for the virus during its nuclear replication phase.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Influenza viruses possess a matrix protein M1 essential for viral structure and replication.
  • Understanding M1's interactions with host cellular components is key to elucidating viral mechanisms.

Purpose of the Study:

  • To investigate the specific binding interactions of influenza virus matrix protein M1 with cellular proteins.
  • To characterize the nature and requirements of the M1-histone interaction.

Main Methods:

  • Immune coprecipitation assays were employed to identify M1-interacting cellular proteins.
  • In vitro binding assays on PVDF membranes were used to confirm M1's specific binding to purified histones.
  • Chemical cleavage of M1 and salt treatment were performed to analyze domain involvement and conformational effects.

Main Results:

  • Matrix protein M1 selectively binds to histones H2A, H2B, H3, and H4, with weaker binding to H1.
  • M1-histone complex formation is dependent on pH and ionic strength, suggesting electrostatic interactions.
  • Both N-terminal and C-terminal domains of M1 contribute to histone binding, and M1 conformation influences this interaction.

Conclusions:

  • Matrix protein M1 specifically interacts with histones, indicating a role in nuclear processes.
  • The findings support the hypothesis of M1 interaction with nucleosomes during the nuclear phase of influenza virus replication.

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