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Updated: Feb 17, 2026

Co-immunoprecipitation of the Mouse Mx1 Protein with the Influenza A Virus Nucleoprotein
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Influenza virus Matrix Protein M1 preserves its conformation with pH, changing multimerization state at the priming

Eleonora V Shtykova1,2, Liubov A Dadinova1, Natalia V Fedorova3

  • 1Shubnikov Institute of Crystallography of Federal Scientific Research Centre "Crystallography and Photonics" of Russian Academy of Sciences, Moscow, Russia.

Scientific Reports
|December 3, 2017
PubMed

Insights

Influenza A virus matrix protein M1

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Influenza A virus matrix protein M1 (M1) is crucial for virus replication.
  • The complete functional and structural characteristics of M1 remain incompletely understood.

Purpose of the Study:

  • To characterize the structural properties and pH-dependent association behavior of full-length Influenza A virus M1 protein.
  • To elucidate the role of M1 domains in protein self-assembly and interactions.

Main Methods:

  • Small-angle X-ray scattering (SAXS)
  • Atomic force microscopy (AFM)
  • Zeta-potential measurements
  • Protein sequence analysis
  • Electrostatic modeling

Main Results:

  • M1 protein comprises a globular N-terminal domain and a flexible C-terminal extension.
  • M1 multimerization is pH-dependent and reversible, with dissociation occurring around pH 6.
  • The C-terminal domain's flexibility significantly influences M1 self-assembly and M1-lipid interactions.

Conclusions:

  • The flexible C-terminal domain of M1 plays a key role in scaffold formation during the influenza A virus lifecycle.
  • Understanding M1 structure and behavior provides insights into virus assembly mechanisms.

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