Cell Death Mediated by Vibrio parahaemolyticus Type III Secretion System 1 Is Dependent on ERK1/2 MAPK, but Independent of Caspases

2011 ◽  
Vol 21 (9) ◽  
pp. 903-913 ◽  
Author(s):  
Yu Jin Yang
Keyword(s):  
Cell Death ◽  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii ◽  
System 1

Type III secretion system 1 of Vibrio parahaemolyticus induces oncosis in both epithelial and monocytic cell lines

Microbiology ◽  
2009 ◽  
Vol 155 (3) ◽  
pp. 837-851 ◽  
Author(s):  
Xiaohui Zhou ◽  
Michael E. Konkel ◽  
Douglas R. Call
Keyword(s):  
Cell Death ◽  
Cell Lines ◽  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Active Form ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Monocytic Cell ◽  
Type Iii ◽  
System 1

The Vibrio parahaemolyticus type III secretion system 1 (T3SS1) induces cytotoxicity in mammalian epithelial cells. We characterized the cell death phenotype in both epithelial (HeLa) and monocytic (U937) cell lines following infection with V. parahaemolyticus. Using a combination of the wild-type strain and gene knockouts, we confirmed that V. parahaemolyticus strain NY-4 was able to induce cell death in both cell lines via a T3SS1-dependent mechanism. Bacterial contact, but not internalization, was required for T3SS1-induced cytotoxicity. The mechanism of cell death involves formation of a pore structure on the surface of infected HeLa and U937 cells, as demonstrated by cellular swelling, uptake of cell membrane-impermeable dye and protection of cytotoxicity by osmoprotectant (PEG3350). Western blot analysis showed that poly ADP ribose polymerase (PARP) was not cleaved and remained in its full-length active form. This result was evident for seven different V. parahaemolyticus strains. V. parahaemolyticus-induced cytotoxicity was not inhibited by addition of the pan-caspase inhibitor carbobenzoxy-valyl-alanyl-aspartyl-[O-methyl]-fluoromethylketone (Z-VAD-FMK) or the caspase-1 inhibitor N-acetyl-tyrosyl-valyl-alanyl-aspartyl-aldehyde (Ac-YVAD-CHO); thus, caspases were not involved in T3SS1-induced cytotoxicity. DNA fragmentation was not evident following infection and autophagic vacuoles were not observed after monodansylcadaverine staining. We conclude that T3SS1 of V. parahaemolyticus strain NY-4 induces a host cell death primarily via oncosis rather than apoptosis, pyroptosis or autophagy.

scholarly journals Regulatory actions of ToxR and CalR on their own genes and type III secretion system 1 in Vibrio parahaemolyticus

Oncotarget ◽  
2017 ◽  
Vol 8 (39) ◽  
pp. 65809-65822 ◽  
Author(s):  
George Osei-Adjei ◽  
He Gao ◽  
Ying Zhang ◽  
Lingyu Zhang ◽  
Wenhui Yang ◽  
...  
Keyword(s):  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii ◽  
System 1 ◽  
Regulatory Actions

scholarly journals The small RNA Spot 42 regulates the expression of the type III secretion system 1 (T3SS1) chaperone protein VP1682 inVibrio parahaemolyticus

2015 ◽  
Vol 362 (21) ◽  
pp. fnv173 ◽  
Author(s):  
Tomotaka Tanabe ◽  
Katsushiro Miyamoto ◽  
Hiroshi Tsujibo ◽  
Shigeo Yamamoto ◽  
Tatsuya Funahashi
Keyword(s):  
Small Rna ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii ◽  
Chaperone Protein ◽  
System 1

scholarly journals SseK1 and SseK3 Type III Secretion System Effectors Inhibit NF-κB Signaling and Necroptotic Cell Death in Salmonella-Infected Macrophages

2017 ◽  
Vol 85 (3) ◽  
Author(s):  
Regina A. Günster ◽  
Sophie A. Matthews ◽  
David W. Holden ◽  
Teresa L. M. Thurston
Keyword(s):  
Cell Death ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Host Cells ◽  
Macrophage Infection ◽  
Content Type ◽  
Type Iii ◽  
Tnf Α ◽  
Arginine Residues

ABSTRACT Within host cells such as macrophages, Salmonella enterica translocates virulence (effector) proteins across its vacuolar membrane via the SPI-2 type III secretion system. Previously, it was shown that when expressed ectopically, the effectors SseK1 and SseK3 inhibit tumor necrosis factor alpha (TNF-α)-induced NF-κB activation. In this study, we show that ectopically expressed SseK1, SseK2, and SseK3 suppress TNF-α-induced, but not Toll-like receptor 4- or interleukin-induced, NF-κB activation. Inhibition required a DXD motif in SseK1 and SseK3, which is essential for the transfer of N-acetylglucosamine to arginine residues (arginine-GlcNAcylation). During macrophage infection, SseK1 and SseK3 inhibited NF-κB activity in an additive manner. SseK3-mediated inhibition of NF-κB activation did not require the only known host-binding partner of this effector, the E3-ubiquitin ligase TRIM32. SseK proteins also inhibited TNF-α-induced cell death during macrophage infection. Despite SseK1 and SseK3 inhibiting TNF-α-induced apoptosis upon ectopic expression in HeLa cells, the percentage of infected macrophages undergoing apoptosis was SseK independent. Instead, SseK proteins inhibited necroptotic cell death during macrophage infection. SseK1 and SseK3 caused GlcNAcylation of different proteins in infected macrophages, suggesting that these effectors have distinct substrate specificities. Indeed, SseK1 caused the GlcNAcylation of the death domain-containing proteins FADD and TRADD, whereas SseK3 expression resulted in weak GlcNAcylation of TRADD but not FADD. Additional, as-yet-unidentified substrates are likely to explain the additive phenotype of a Salmonella strain lacking both SseK1 and SseK3.

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