scholarly journals Vibrio parahaemolyticus ExsE is requisite for initial adhesion and subsequent type III secretion system 1-dependent autophagy in HeLa cells

Microbiology ◽  
2012 ◽  
Vol 158 (9) ◽  
pp. 2303-2314 ◽  
Author(s):  
Daniel P. Erwin ◽  
Seth D. Nydam ◽  
Douglas R. Call
Keyword(s):  
Hela Cells ◽  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii ◽  
Initial Adhesion ◽  
System 1

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

Functional cloning of Vibrio parahaemolyticus type III secretion system 1 in Escherichia coli K-12 strain as a molecular syringe

2012 ◽  
Vol 427 (2) ◽  
pp. 242-247 ◽  
Author(s):  
Yukihiro Akeda ◽  
Tomomi Kimura ◽  
Aiko Yamasaki ◽  
Toshio Kodama ◽  
Tetsuya Iida ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii ◽  
K 12 ◽  
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 Identification of Proteins Secreted via Vibrio parahaemolyticus Type III Secretion System 1

2006 ◽  
Vol 74 (2) ◽  
pp. 1032-1042 ◽  
Author(s):  
Takahiro Ono ◽  
Kwon-Sam Park ◽  
Mayumi Ueta ◽  
Tetsuya Iida ◽  
Takeshi Honda
Keyword(s):  
Hela Cells ◽  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Type Iii Secretion System ◽  
Gene Clusters ◽  
Secretion System ◽  
Secreted Proteins ◽  
Large Chromosome ◽  
Two Dimensional Gel Electrophoresis ◽  
Type Iii

ABSTRACT Vibrio parahaemolyticus, a gram-negative marine bacterium, is an important pathogen causing food-borne gastroenteritis or septicemia. Recent genome sequencing of the RIMD2210633 strain (a Kanagawa phenomenon-positive clinical isolate of serotype O3:K6) revealed that the strain has two sets of gene clusters that encode the type III secretion system (TTSS) apparatus. The first cluster, TTSS1, is located on the large chromosome, and the second, TTSS2, is on the small chromosome. Previously, we reported that TTSS1 is involved in the cytotoxicity of the RIMD2210633 strain against HeLa cells. Here, we analyzed proteins secreted via the TTSS apparatus encoded by TTSS1 by using two-dimensional gel electrophoresis and identified the proteins encoded by genes VP1680, VP1686, and VPA450. To investigate the roles of those secreted proteins, we constructed and analyzed a series of deletion mutants. Flow cytometry analysis using fluorescence-activated cell sorting with fluorescein isothiocyanate-labeled annexin V demonstrated that the TTSS1-dependent cell death was by apoptosis. The cytotoxicity to HeLa cells was related to one of the newly identified secreted proteins encoded by VP1680. Adenylate cyclase fusion protein studies proved that the newly identified secreted proteins were translocated into HeLa cells. Thus, these appear to be the TTSS effector proteins in V. parahaemolyticus.

scholarly journals Identification and characterization of a type III secretion-associated chaperone in the type III secretion system 1 ofVibrio parahaemolyticus

2009 ◽  
Vol 296 (1) ◽  
pp. 18-25 ◽  
Author(s):  
Yukihiro Akeda ◽  
Kanna Okayama ◽  
Tomomi Kimura ◽  
Rikard Dryselius ◽  
Toshio Kodama ◽  
...  
Keyword(s):  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Type Iii ◽  
System 1 ◽  
Identification And Characterization

scholarly journals SepZ/EspZ Is Secreted and Translocated into HeLa Cells by the Enteropathogenic Escherichia coli Type III Secretion System

2005 ◽  
Vol 73 (7) ◽  
pp. 4327-4337 ◽  
Author(s):  
Kristen J. Kanack ◽  
J. Adam Crawford ◽  
Ichiro Tatsuno ◽  
Mohamed A. Karmali ◽  
James B. Kaper
Keyword(s):  
Escherichia Coli ◽  
Hela Cells ◽  
Type Iii Secretion ◽  
Type Iii Secretion System ◽  
Secretion System ◽  
Bacterial Attachment ◽  
Host Cells ◽  
Dependent Manner ◽  
Cell Infection ◽  
Type Iii

ABSTRACT Enteropathogenic Escherichia coli (EPEC) is a major bacterial cause of infantile diarrhea in developing countries and is the prototype for a group of gastrointestinal pathogens causing characteristic attaching and effacing (A/E) histopathology on intestinal epithelia. A/E pathogens utilize a type III secretion system (TTSS), encoded by the locus of enterocyte effacement (LEE) pathogenicity island, to deliver effector proteins into host cells. Here, we investigate sequence divergence of the LEE-encoded SepZ protein and identify it as a TTSS-secreted and -translocated molecule. SepZ is hypervariable among A/E pathogens, with sequences sharing between 60 to 81% amino acid identity with SepZ of EPEC. A SepZ-CyaA fusion was secreted and translocated into HeLa cells in a TTSS-dependent manner. Additionally, we determined that the first 20 amino acids of SepZ were sufficient to direct its translocation. In contrast to previous studies suggesting a role in invasion and the structure and/or regulation of the TTSS, we found that SepZ does not mediate uptake of EPEC into host cells or affect translocation and tyrosine phosphorylation of the translocated intimin receptor. Immunohistochemistry reveals that, after an extended HeLa cell infection, accumulated SepZ can be detected beneath the site of bacterial attachment in a subset of pedestal regions. To indicate its newly identified status as a translocated effector protein, we propose to rename SepZ as EspZ.

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
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