The actin cytoskeleton inhibits pore expansion during PIV5 fusion protein-promoted cell-cell fusion
- Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington KY 40536 (United States)
- Mercer University School of Medicine, Division of Basic Medical Sciences, Macon, GA 31207 (United States)
Paramyxovirus fusion (F) proteins promote both virus-cell fusion, required for viral entry, and cell-cell fusion, resulting in syncytia formation. We used the F-actin stabilizing drug, jasplakinolide, and the G-actin sequestrant, latrunculin A, to examine the role of actin dynamics in cell-cell fusion mediated by the parainfluenza virus 5 (PIV5) F protein. Jasplakinolide treatment caused a dose-dependent increase in cell-cell fusion as measured by both syncytia and reporter gene assays, and latrunculin A treatment also resulted in fusion stimulation. Treatment with jasplakinolide or latrunculin A partially rescued a fusion pore opening defect caused by deletion of the PIV5 F protein cytoplasmic tail, but these drugs had no effect on fusion inhibited at earlier stages by either temperature arrest or by a PIV5 heptad repeat peptide. These data suggest that the cortical actin cytoskeleton is an important regulator of fusion pore enlargement, an energetically costly stage of viral fusion protein-mediated membrane merger.
- OSTI ID:
- 21460264
- Journal Information:
- Virology, Vol. 404, Issue 1; Other Information: DOI: 10.1016/j.virol.2010.04.024; PII: S0042-6822(10)00274-6; Copyright (c) 2010 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; ISSN 0042-6822
- Country of Publication:
- United States
- Language:
- English
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