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- W2157880008 abstract "Summary Salivary histatin 5 (Hst 5) is a cationic salivary protein with high fungicidal activity against Candida albicans . Binding to the cell wall followed by intracellular translocation is required for killing; however, specific binding components and critical toxic events are not understood. In this study, laminarin (β‐1,3‐glucan) but not sialic acid, mannan or pustulan mediated Hst 5 binding to C. albicans , and was disassociated by 100 mM NaCl. Time‐lapse confocal microscopy revealed a dose‐dependent rate of cytosolic uptake of Hst 5 that invariably preceded propidium iodide (PI) entry, demonstrating that translocation itself does not disrupt membrane integrity. Cell toxicity was manifest by vacuolar expansion followed by PI entrance; however, loss of endocytotic vacuolar trafficking of Hst 5 did not reduce killing. Extracellular NaCl (100 mM), but not sorbitol, prevented vacuolar expansion and PI entry in cells already containing cytosolic Hst 5, thus showing a critical role for ionic balance in Hst 5 toxicity. Hst 5 uptake, but not cell wall binding, was blocked by pretreatment with azide or carbonyl cyanide m‐chlorophenylhydrazone; however, 10% of de‐energized cells had membrane disruption. Thus, Hst 5 is capable of heterogeneous intracellular entry routes, but only direct cytosolic translocation causes cell death as a result of ionic efflux." @default.
- W2157880008 created "2016-06-24" @default.
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- W2157880008 date "2010-07-01" @default.
- W2157880008 modified "2023-10-16" @default.
- W2157880008 title "Salivary histatin 5 internalization by translocation, but not endocytosis, is required for fungicidal activity in Candida albicans" @default.
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- W2157880008 doi "https://doi.org/10.1111/j.1365-2958.2010.07210.x" @default.
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