RRC ID 56070
著者 Nagahama M, Takehara M, Miyamoto K, Ishidoh K, Kobayashi K.
タイトル Acid Sphingomyelinase Promotes Cellular Internalization of Clostridium perfringens Iota-Toxin.
ジャーナル Toxins (Basel)
Abstract Clostridium perfringens iota-toxin is a binary actin-ADP-ribosylating toxin composed of the enzymatic component Ia and receptor binding component Ib. Ib binds to a cell surface receptor, forms Ib oligomer in lipid rafts, and associates with Ia. The Ia-Ib complex then internalizes by endocytosis. Here, we showed that acid sphingomyelinase (ASMase) facilitates the cellular uptake of iota-toxin. Inhibitions of ASMase and lysosomal exocytosis by respective blockers depressed cell rounding induced by iota-toxin. The cytotoxicity of the toxin increased in the presence of Ca2+ in extracellular fluids. Ib entered target cells in the presence but not the absence of Ca2+. Ib induced the extracellular release of ASMase in the presence of Ca2+. ASMase siRNA prevented the cell rounding induced by iota-toxin. Furthermore, treatment of the cells with Ib resulted in the production of ceramide in cytoplasmic vesicles. These observations showed that ASMase promotes the internalization of iota-toxin into target cells.
巻・号 10(5)
公開日 2018-5-20
DOI 10.3390/toxins10050209
PII toxins10050209
PMID 29783772
PMC PMC5983265
MeSH ADP Ribose Transferases / pharmacology* Animals Bacterial Toxins / pharmacology* Biological Transport Dogs Madin Darby Canine Kidney Cells Recombinant Proteins / pharmacology Sphingomyelin Phosphodiesterase / metabolism*
IF 3.895
引用数 2
リソース情報
ヒト・動物細胞 MDCK(RCB0995)