Degradation of nuclear Ubc9 induced by listeriolysin O is dependent on K+ efflux
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其它資訊
摘要Listeriolysin O (LLO) is a pore-forming toxin produced by L. monocytogenes, and is belonged to a protein family of cholesterol-dependent cytolysins (CDCs). Previous studies have demonstrated that LLO triggers Ubc9 degradation and disrupts host SUMOylation to facilitate bacterial infection. However, the underlying mechanism of Ubc9 degradation is unclear. Here we show that LLO-induced down-regulation of Ubc9 is independent of Ubc9-SUMO interaction, however, it may involve phosphorylation signaling. Additionally, LLO exerts its effects primarily on nuclear Ubc9 and this process is mediated by K+ efflux. Interestingly, for intracellular CDCs such as pneumolysin and suilysin, blockage of K+ efflux enhances degradation of nuclear Ubc9, suggesting that extracellular and intracellular pathogens may exploit different mechanisms to modulate host SUMOylation system. Furthermore, up-regulation of SUMOylation by stable expression of SUMO-1 or SUMO-2 shows a delay in membrane perforation by LLO, indicating that SUMO modification of host proteins may act at the frontline for the defense response against LLO. Taken together, our study provides insights to the understanding of host-pathogen interactions.
著者LI Jiexin, LAM Wendy Wai Ling, LAI Tsz Wah, AU Shannon Wing Ngor
期刊名稱Biochemical and Biophysical Research Communications
出版年份2017
月份11
日期18
卷號493
期次2
頁次1115 - 1121
國際標準期刊號0006-291X
電子國際標準期刊號1090-2104
語言美式英語

上次更新時間 2020-18-10 於 02:41