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Ultrastructural organization of recombinant Marburg virus nucleoprotein: comparison with Marburg virus inclusions

L Kolesnikova1, E Mühlberger, E Ryabchikova

  • 1State Scientific Research Center of Virology, Vector Institute of Molecular Biology, Laboratory of Ultrastructure, 633159 Koltsovo, Novosibirsk Region, Russia.

Journal of Virology
|March 23, 2000
PubMed

Insights

Marburg virus nucleoprotein (NP) can self-assemble into hexagonal, tubule-like structures. These structures form independently of the viral genome, suggesting NP

Area of Science:

  • Virology
  • Cell Biology
  • Structural Biology

Background:

  • Marburg virus (MBGV) is a filovirus causing severe hemorrhagic fever.
  • Understanding the assembly of viral components is crucial for developing antiviral strategies.

Purpose of the Study:

  • To investigate the self-assembly properties of the Marburg virus nucleoprotein (NP).
  • To determine if MBGV NP can form nucleocapsid-like structures without the viral genome.

Main Methods:

  • Immunoelectron microscopy was used to study HeLa cells expressing recombinant MBGV NP.
  • Analysis of intracellular inclusions in MBGV-infected cells.

Main Results:

  • MBGV NP self-assembled into large aggregates associated with the rough endoplasmic reticulum.
  • These aggregates formed hexagonal, tubule-like structures.
  • Similar structures were observed in MBGV-infected cells, independent of the viral genome.

Conclusions:

  • Marburg virus nucleoprotein possesses intrinsic properties for self-assembly into nucleocapsid-like structures.
  • MBGV NP can form these structures in the absence of the viral genome and other associated proteins.

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