Epsilon-Toxin Impairs the Barrier Function in MDCK Cell Monolayers in a Ca-Dependent Manner.

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ID: 265137
2020
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Abstract
Epsilon-toxin produced by significantly contributes to the pathogeneses of enterotoxemia in ruminants and multiple sclerosis in humans. Epsilon-toxin forms a heptameric oligomer in the host cell membrane, promoting cell disruption. Here, we investigate the effect of epsilon-toxin on epithelial barrier functions. Epsilon-toxin impairs the barrier integrity of Madin-Darby Canine Kidney (MDCK) cells, as demonstrated by decreased transepithelial electrical resistance (TEER), increased paracellular flux marker permeability, and the decreased cellular localization of junctional proteins, such as occludin, ZO-1, and claudin-1. U73122, an endogenous phospholipase C (PLC) inhibitor, inhibited the decrease in TEER and the increase in the permeability of flux marker induced by epsilon-toxin. The application of epsilon-toxin to MDCK cells resulted in the biphasic formation of 1,2-diacylglycerol (DAG) and inositol-1,4,5-triphosphate (IP). U73122 blocked the formation of DAG and IP induced by the toxin. Epsilon-toxin also specifically activated endogenous PLC-γ1. Epsilon-toxin dose-dependently increased the cytosolic calcium ion concentration ([Ca]i). The toxin-induced elevation of [Ca]i was inhibited by U73122. Cofilin is a key regulator of actin cytoskeleton turnover and tight-junction (TJ) permeability regulation. Epsilon-toxin caused cofilin dephosphorylation. These results demonstrate that epsilon-toxin induces Ca influx through activating the phosphorylation of PLC-γ1 and then causes TJ opening accompanied by cofilin dephosphorylation.
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nagahama2020toxins Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Nagahama, Masahiro;Seike, Soshi;Ochi, Sadayuki;Kobayashi, Keiko;Takehara, Masaya;
Journal Toxins
Year 2020
DOI
E286
URL
Keywords
cofilin c. perfringens epsilon-toxin ca2+ influx barrier integrity oligomer formation

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