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Updated: Oct 15, 2025

Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis
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Structure of Machupo virus polymerase in complex with matrix protein Z

Jun Ma1, Shuangyue Zhang1,2, Xinzheng Zhang3,4,5

  • 1National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, China.

Nature Communications
|October 26, 2021
PubMed

Insights

Machupo virus L protein structure reveals how the Z protein inhibits viral replication. This finding offers a new strategy for developing antiviral drugs against dangerous hemorrhagic fevers.

Area of Science:

  • Virology
  • Structural Biology
  • Drug Discovery

Background:

  • Arenaviridae viruses cause severe hemorrhagic fevers with high mortality.
  • No effective countermeasures are currently available.
  • The arenavirus L protein is crucial for viral transcription and replication, making it a key drug target.

Purpose of the Study:

  • To determine the structure of the Machupo virus L protein in complex with the Z protein.
  • To elucidate the mechanism by which the Z protein inhibits L protein activity.

Main Methods:

  • Cryo-electron microscopy was used to determine the structure.
  • Structural analysis of the L-Z protein complex.

Main Results:

  • The Z protein binds the L protein with 1:1 stoichiometry.
  • Z protein binding occurs at a critical interface between L protein domains.
  • This interaction likely stabilizes L protein domains, inhibiting its catalytic activity.

Conclusions:

  • The structure provides insight into the inhibitory mechanism of arenavirus replication.
  • This provides a novel structural basis for developing arenavirus antiviral drugs.

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