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The native structure of the assembled matrix protein 1 of influenza A virus

Julia Peukes1,2,3, Xiaoli Xiong4,5, Simon Erlendsson1

  • 1Structural Studies Division, Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.

Nature
|September 10, 2020
PubMed

Insights

Matrix protein 1 (M1) forms linear strands essential for influenza virus assembly. This structure reveals how M1 polymerizes and acts as a pH-sensitive switch for virus disassembly after cell entry.

Area of Science:

  • Structural Biology
  • Virology
  • Molecular Biology

Background:

  • Influenza A virus causes millions of severe illnesses annually.
  • Matrix protein 1 (M1) is the most abundant protein in influenza virions.
  • M1 mediates virus assembly by forming an internal scaffold, but its structure and oligomerization are unknown.

Purpose of the Study:

  • To determine the complete structure of assembled M1 within intact influenza virus particles.
  • To elucidate how M1 oligomerizes to mediate virion assembly.
  • To understand the mechanism of influenza virus disassembly.

Main Methods:

  • Determination of M1 structure within intact virus particles.
  • Reconstitution and structural analysis of M1 oligomers in vitro.

Main Results:

  • The C-terminal domain of M1, disordered in solution, folds and binds to the N-terminal domain of another M1 monomer.
  • M1 polymerizes into linear strands coating the inner surface of the assembling virion membrane.
  • A cluster of five histidine residues from three M1 monomers forms a pH-sensitive disassembly switch.

Conclusions:

  • The study reveals the mechanism of M1 polymerization driving influenza virus assembly.
  • Identified M1 structure explains its role in forming the viral endoskeleton.
  • Discovered a pH-sensitive histidine cluster acting as a viral disassembly switch.

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