The Vibrio alginolyticus T3SS effectors, Val1686 and Val1680, induce cell rounding, apoptosis and lysis of fish epithelial cells
文献类型： 外文期刊
作者： Zhao, Zhe 1 ; Liu, Jinxin 1 ; Deng, Yiqin 2 ; Huang, Wen 2 ; Ren, Chunhua 2 ; Call, Douglas R. 3 ; Hu, Chaoqun 2 ;
作者机构： 1.Hohai Univ, Coll Oceanog, Inst Marine Biol, 1 Xikang Rd, Nanjing 210098, Jiangsu, Peoples R China
2.Chinese Acad Sci, South China Sea Inst Oceanol, Key Lab Appl Marine Biol Guangdong Prov, Key Lab Marine Bioresources Sustainable Utilizat, Guangzhou, Guangdong, Peoples R China
3.Washington State Univ, Paul G Allen Sch Global Anim Hlth, Pullman, WA 99164 USA
4.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Minist Agr, Key Lab South China Sea Fishery Resources Exploit, Guangzhou, Guangdong, Peoples R China
关键词： Vibrio alginolyticus; T3SS; effector protein; apoptosis; fish disease
期刊名称：VIRULENCE （ 影响因子：5.882； 五年影响因子：6.489 ）
ISSN： 2150-5594
年卷期： 2018 年 9 卷 1 期
页码：
收录情况： SCI
摘要： Vibrio alginolyticus is a Gram-negative bacterium that is an opportunistic pathogen of both marine animals and people. Its pathogenesis likely involves type III secretion system (T3SS) mediated induction of rapid apoptosis, cell rounding and osmotic lysis of infected eukaryotic cells. Herein, we report that effector proteins, Val1686 and Val1680 from V. alginolyticus, were responsible for T3SS-mediated death of fish cells. Val1686 is a Fic-domain containing protein that not only contributed to cell rounding by inhibiting Rho guanosine triphosphatases (GTPases), but was requisite for the induction of apoptosis because the deletion mutant (Delta val1686) was severely weakened in its ability to induce cell rounding and apoptosis in fish cells. In addition, Val1686 alone was sufficient to induce cell rounding and apoptosis as evidenced by the transfection of Val1686 into fish cells. Importantly, the Fic-domain essential for cell rounding activity was equally important to activation of apoptosis of fish cells, indicating that apoptosis is a downstream event of Val1686-dependent GTPase inhibition. V. alginolyticus infection likely activates JNK and ERK pathways with sequential activation of caspases (caspase-8/-10, -9 and -3) and subsequent apoptosis. Val1680 contributed to T3SS-dependent lysis of fish cells in V. alginolyticus, but did not induce autophagy as has been reported for its homologue (VopQ) in V. parahaemolyticus. Together, Val1686 and Val1680 work together to induce apoptosis, cell rounding and cell lysis of V. alginolyticus-infected fish cells. These findings provide new insights into the mechanism of cell death caused by T3SS of V. alginolyticus.
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