A stochastic assembly model for Nipah virus revealed by super-resolution microscopy

Understanding virus assembly mechanisms is important for developing therapeutic interventions. Nipah virus (NiV) is of interest because of its high mortality rate and efficient human–human transmissions. The current model for most enveloped viruses suggests that matrix proteins (M) recruit attachmen...

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Bibliographic Details
Published in:Nature communications 2018-08, Vol.9 (1), p.3050-7, Article 3050
Main Authors: Liu, Qian, Chen, Lei, Aguilar, Hector C., Chou, Keng C.
Format: Article
Language:English
Subjects:
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Animals
Assembly
Cell Line
Cell Membrane - virology
Glycoproteins
Glycoproteins - metabolism
HeLa Cells
Humanities and Social Sciences
Humans
Membranes
Microscopy
Microscopy - methods
multidisciplinary
Nipah virus
Nipah Virus - physiology
Nipah Virus - ultrastructure
Plasma
Proteins
Science
Science (multidisciplinary)
Stochasticity
Therapeutic applications
Transfection
Viral Envelope Proteins - metabolism
Viral Fusion Proteins - metabolism
Viral Fusion Proteins - ultrastructure
Viral Matrix Proteins - metabolism
Viral Matrix Proteins - ultrastructure
Virion - metabolism
Virus Assembly
Virus-like particles
Viruses
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Summary:Understanding virus assembly mechanisms is important for developing therapeutic interventions. Nipah virus (NiV) is of interest because of its high mortality rate and efficient human–human transmissions. The current model for most enveloped viruses suggests that matrix proteins (M) recruit attachment glycoproteins (G) and fusion glycoproteins (F) to the assembly site at the plasma membrane. Here we report an assembly model that differs in many aspects from the current one. Examining NiV proteins on the cell plasma membrane using super-resolution microscopy reveals that clusters of F and G are randomly distributed on the plasma membrane regardless of the presence or absence of M. Our data suggests a model in which the M molecules assemble at the plasma membrane to form virus-like particles (VLPs), while the incorporation of F and G into the nascent VLPs is stochastic. The current model for Nipah virus assembly suggests that packaging is orchestrated by the matrix protein at the plasma membrane. Here, using super-resolution microscopy and Nipah virus-like particles, Liu et al. show that Nipah virus assembly is stochastic.
ISSN:2041-1723
2041-1723
DOI:10.1038/s41467-018-05480-2