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Nipah virus matrix protein uses cortical actin to stabilize the virus assembly sites and promote budding

Jingjing Wang1, Vicky Kliemke1, Mengyu Zhang1

  • 1Institute of Parasitology, Faculty of Agricultural and Environmental Sciences, McGill University, Sainte-Anne-de-Bellevue, Quebec, Canada.

Science Advances
|September 19, 2025
PubMed

Insights

Host F-actin retains Nipah virus (NiV) assembly sites at the plasma membrane, promoting virus budding. The Arp2/3 complex further enhances virus-like particle production by driving actin branching.

Area of Science:

  • Virology
  • Cell Biology
  • Biochemistry

Background:

  • Enveloped viruses, like paramyxoviruses, bud from the host plasma membrane.
  • Nipah virus (NiV) matrix protein (M) drives assembly and budding via dimerization and plasma membrane interaction.

Purpose of the Study:

  • To investigate the role of host F-actin and the Arp2/3 complex in NiV assembly and budding.
  • To elucidate the mechanism by which NiV matrix protein interacts with the host cytoskeleton.

Main Methods:

  • Analysis of NiV-M-mediated virus-like particle (VLP) production kinetics.
  • Investigating NiV-M interaction with F-actin using its carboxyl-terminal domain.
  • Assessing the impact of disrupting actin dynamics and Arp2/3 complex activity on M organization and membrane retention.

Main Results:

  • NiV-M VLP production depends on F-actin interaction via its carboxyl-terminal domain.
  • F-actin retains NiV-M assembly sites at the plasma membrane, influencing M nanoscale organization and membrane retention.
  • The Arp2/3 complex promotes VLP production, enhances NiV-M retention, and aids protrusion formation.

Conclusions:

  • Host F-actin is crucial for retaining NiV assembly sites at the plasma membrane.
  • Arp2/3-driven actin branching facilitates NiV budding and virus-like particle production.

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