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Replication of a Nipah Virus Encoding a Nuclear-Retained Matrix Protein

Marc Ringel1, Laura Behner1, Anja Heiner1

  • 1Institute of Virology, Philipps University Marburg, Marburg, Germany.

The Journal of Infectious Diseases
|October 31, 2019
PubMed

Insights

Nipah virus matrix protein (NiV M) nuclear import is essential for cell surface transport. Nuclear-retained NiV M impairs virus assembly and formation of plasma membrane inclusions, suggesting nuclear transit is critical.

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Nipah virus (NiV) matrix protein (NiV M) is crucial for viral assembly, involving nuclear transit and plasma membrane accumulation.
  • The necessity of nuclear transit for NiV M surface transport and its role in different cell types remain unclear.

Purpose of the Study:

  • To investigate if NiV M can reach the cell surface by bypassing the nucleus.
  • To characterize the impact of nuclear-retained NiV M on viral assembly and infectivity in a full viral context.

Main Methods:

  • Utilized a mutant NiV M protein with a defective nuclear export signal (MNESmut) to assess nuclear import.
  • Generated a recombinant NiV expressing MNESmut (NiV-MNESmut) to study its effects in infected cells.
  • Analyzed viral assembly, cell-cell fusion, virus titers, and inclusion body formation.

Main Results:

  • Nuclear import of NiV M is ubiquitous, as MNESmut was retained in the nuclei of all tested cell types.
  • NiV-MNESmut exhibited increased cell-cell fusion and reduced virus titers, indicating impaired viral assembly.
  • Perinuclear inclusions (IBperi) were observed, but plasma membrane inclusions (IBPM) were absent in NiV-MNESmut infected cells.
  • Transport-defective MNESmut was recruited to IBperi, preventing cytoplasmic and nuclear accumulation.

Conclusions:

  • Functional nuclear transit of NiV M is a prerequisite for its transport to the cell surface and efficient viral assembly.
  • Perinuclear inclusions (IBperi) serve as functionally relevant aggresome-like compartments that sequester nonfunctional NiV M.
  • These findings highlight the critical role of nuclear trafficking in the Nipah virus life cycle.
Keywords:
Nipah virusinclusion bodiesmatrix proteinnuclear transit

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