Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/89368
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Type: Journal article
Title: Myosin IIA is essential for Shigella flexneri cell-to-cell spread
Author: Lum, M.
Morona, R.
Citation: Pathogens and Disease, 2014; 72(3):174-187
Publisher: Oxford University Press (OUP)
Issue Date: 2014
ISSN: 2049-632X
2049-632X
Statement of
Responsibility: 
Mabel Lum, Renato Morona
Abstract: A key feature of Shigella pathogenesis is the ability to spread from cell-to-cell post-invasion. This is dependent on the bacteria's ability to initiate de novo F-actin tail polymerisation, followed by protrusion formation, uptake of bacteria-containing protrusion and finally, lysis of the double membrane vacuole in the adjacent cell. In epithelial cells, cytoskeletal tension is maintained by the actin-myosin II networks. In this study, the role of myosin II and its specific kinase, myosin light chain kinase (MLCK), during Shigella intercellular spreading was investigated in HeLa cells. Inhibition of MLCK and myosin II, as well as myosin IIA knockdown, significantly reduced Shigella plaque and infectious focus formation. Protrusion formation and intracellular bacterial growth was not affected. Low levels of myosin II were localised to the Shigella F-actin tail. HeLa cells were also infected with Shigella strains defective in cell-to-cell spreading. Unexpectedly loss of myosin IIA labelling was observed in HeLa cells infected with these mutant strains. This phenomenon was not observed with WT Shigella or with the less abundant myosin IIB isoform, suggesting a critical role for myosin IIA.
Keywords: ML-7; ML-9; MLCK; Shigella flexneri; blebbistatin; myosin IIB
Description: First published online: 8 January 2015
Rights: © 2014 Federation of European Microbiological Societies. Published by John Wiley & Sons Ltd. All rights reserved.
RMID: 0030008878
DOI: 10.1111/2049-632X.12202
Grant ID: http://purl.org/au-research/grants/nhmrc/565526
Appears in Collections:Microbiology and Immunology publications

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