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• W2081644840 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. In this study, we show that the cell protein Myosin IIA is needed for the human pathogen Shigella flexneri to efficiently infect human cells." @default.
• W2081644840 created "2016-06-24" @default.
• W2081644840 creator A5023033615 @default.
• W2081644840 creator A5051890003 @default.
• W2081644840 date "2014-07-01" @default.
• W2081644840 modified "2023-10-16" @default.
• W2081644840 title "Myosin IIA is essential for<i>Shigella flexneri</i>cell-to-cell spread" @default.
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• W2081644840 doi "https://doi.org/10.1111/2049-632x.12202" @default.
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