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Microtubule-dependent intracellular transport of murine polyomavirus
Norberto Sanjuan1, Analía Porrás, Javier Otero
1Laboratory of Experimental Pathology, Department of Microbiology, University of Buenos Aires School of Medicine, Buenos Aires, Argentina. patoexpe@fmed.uba.ar
Abstract:
The mechanisms used by murine polyomavirus for intracellular migration are yet to be clarified. In this work we selectively depolymerized microtubules or actin fibers and then studied the progression of polyomavirus infection in cultured cells. Our results demonstrate that microtubule depolymerization prevents polyomavirus migration toward the nucleus and from the nucleus to the cell surface, being also involved in viral release, while disruption of the actin microfilaments appears to have no detrimental effect on the virus ability to reach the nucleus. The ultrastructural observation of polyomavirus nonenveloped particles interacting with the free end and the lateral sides of microtubules together with the coimmunoprecipitation of tubulin and viral VP-1 further supports the idea that polyomavirus intracellular migration seems to be mediated by the interaction of polyomavirus major capsid protein VP-1 with tubulin.
Insights
Murine polyomavirus (MuPyV) intracellular migration relies on microtubules, not actin filaments. The viral VP-1 protein interacts with tubulin, facilitating MuPyV
Area of Science:
- Virology
- Cell Biology
- Microbiology
Background:
- Intracellular migration mechanisms of murine polyomavirus (MuPyV) remain unclear.
- Understanding viral transport is crucial for developing antiviral strategies.
Purpose of the Study:
- To elucidate the role of microtubules and actin filaments in MuPyV intracellular trafficking.
- To identify the viral components involved in MuPyV cell transport.
Main Methods:
- Selective depolymerization of microtubules or actin filaments in cultured cells.
- Monitoring MuPyV infection progression.
- Ultrastructural analysis of viral particles.
- Co-immunoprecipitation assays.
Main Results:
- Microtubule depolymerization blocked MuPyV nuclear import and cell surface export.
- Actin disruption did not impede MuPyV nuclear entry.
- Viral release was also affected by microtubule depolymerization.
- Ultrastructural and co-immunoprecipitation data revealed MuPyV VP-1 interaction with tubulin.
Conclusions:
- MuPyV intracellular migration is mediated by microtubules.
- The major viral capsid protein VP-1 interacts with tubulin, suggesting a direct role in viral transport.
- Actin filaments are not essential for MuPyV nuclear targeting.