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08:53
Assay to Measure Nucleocytoplasmic Transport in Real Time within Motor Neuron-like NSC-34 Cells
Published on: May 16, 2017
Nucleocytoplasmic traffic disorder induced by cardioviruses
Peter V Lidsky1, Stanleyson Hato, Maryana V Bardina
1M. P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region, Russia.
Journal of Virology
|February 28, 2006
Summary
Encephalomyocarditis virus (EMCV) alters nuclear transport by increasing nuclear envelope permeability, unlike poliovirus. This viral cardiovirus mechanism involves the leader protein, not protease 2A(pro), affecting nucleocytoplasmic traffic.
Area of Science:
- Virology
- Cell Biology
- Molecular Biology
Background:
- Picornaviruses like poliovirus disrupt nuclear transport via protease 2A(pro).
- Encephalomyocarditis virus (EMCV), a cardiovirus, lacks 2A(pro) but also affects nucleocytoplasmic traffic.
Purpose of the Study:
- To investigate the mechanism of nucleocytoplasmic traffic alteration by EMCV.
- To compare EMCV's mechanism with that of poliovirus.
Main Methods:
- Utilized fluorescent "Timer" protein to track nuclear import/efflux.
- Examined nuclear envelope permeability in digitonin-treated infected cells.
- Analyzed viral RNA translation products and protein mutations (leader protein, zinc finger, phosphorylation site).
- Assessed nucleoporin integrity via electron microscopy.
Main Results:
- EMCV infection increased bidirectional nucleocytoplasmic traffic, primarily via nuclear efflux of existing proteins.
- EMCV-induced nuclear envelope permeability was mediated by the viral leader protein, dependent on its zinc finger motif.
- Leader protein phosphorylation influenced efflux rate; staurosporine inhibited the activity.
- Unlike poliovirus, EMCV did not degrade nucleoporins but altered nuclear pore structure.
Conclusions:
- Cardioviruses (EMCV) and enteroviruses (poliovirus) similarly disrupt nucleocytoplasmic traffic but employ distinct molecular mechanisms.
- EMCV utilizes its leader protein to increase nuclear envelope permeability, contrasting with poliovirus's reliance on protease 2A(pro).
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