scholarly journals Persistence of Vibrio parahaemolyticus in the Pacific Oyster, Crassostrea gigas, Is a Multifactorial Process Involving Pili and Flagella but Not Type III Secretion Systems or Phase Variation

2013 ◽  
Vol 79 (10) ◽  
pp. 3303-3305 ◽  
Author(s):  
Alisha M. Aagesen ◽  
Sureerat Phuvasate ◽  
Yi-Cheng Su ◽  
Claudia C. Häse
Keyword(s):  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Phase Variation ◽  
Type I ◽  
Secretion Systems ◽  
Content Type ◽  
Type Iii ◽  
Type Iv ◽  
Pacific Oysters ◽  
Type Iii Secretion Systems

ABSTRACTVibrio parahaemolyticuscan resist oyster depuration, suggesting that it possesses specific factors for persistence. We show that type I pili, type IV pili, and both flagellar systems contribute toV. parahaemolyticuspersistence in Pacific oysters whereas type III secretion systems and phase variation do not.

scholarly journals Identification of Potential Type III Secretion Proteins via Heterologous Expression of Vibrio parahaemolyticus DNA

2012 ◽  
Vol 78 (9) ◽  
pp. 3492-3494 ◽  
Author(s):  
Xiaohui Zhou ◽  
Seth D. Nydam ◽  
Jeffrey E. Christensen ◽  
Michael E. Konkel ◽  
Lisa Orfe ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Yersinia Enterocolitica ◽  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Genomic Islands ◽  
Secretion Systems ◽  
Content Type ◽  
Type Iii ◽  
Type Iii Secretion Systems ◽  
Secretion Assay

ABSTRACTWe employed a heterologous secretion assay to identify proteins potentially secreted by type III secretion systems (T3SSs) inVibrio parahaemolyticus. N-terminal sequences from 32 proteins within T3SS genomic islands and seven proteins from elsewhere in the chromosome included proteins that were recognized for export by theYersinia enterocoliticaflagellar T3SS.

scholarly journals The Bacterium Pantoea stewartii Uses Two Different Type III Secretion Systems To Colonize Its Plant Host and Insect Vector

2012 ◽  
Vol 78 (17) ◽  
pp. 6327-6336 ◽  
Author(s):  
Valdir R. Correa ◽  
Doris R. Majerczak ◽  
El-Desouky Ammar ◽  
Massimo Merighi ◽  
Richard C. Pratt ◽  
...  
Keyword(s):  
Type Iii Secretion ◽  
Flea Beetle ◽  
Insect Vector ◽  
Secretion Systems ◽  
Plant Host ◽  
Content Type ◽  
Type Iii ◽  
Pantoea Stewartii ◽  
Type Iii Secretion Systems ◽  
Animal Pathogens

ABSTRACTPlant- and animal-pathogenic bacteria utilize phylogenetically distinct type III secretion systems (T3SS) that produce needle-like injectisomes or pili for the delivery of effector proteins into host cells.Pantoea stewartiisubsp.stewartii(herein referred to asP. stewartii), the causative agent of Stewart's bacterial wilt and leaf blight of maize, carries phylogenetically distinct T3SSs. In addition to an Hrc-Hrp T3SS, known to be essential for maize pathogenesis,P. stewartiihas a second T3SS (Pantoeasecretion island 2 [PSI-2]) that is required for persistence in its flea beetle vector,Chaetocnema pulicaria(Melsh). PSI-2 belongs to the Inv-Mxi-Spa T3SS family, typically found in animal pathogens. Mutagenesis of the PSI-2psaNgene, which encodes an ATPase essential for secretion of T3SS effectors by the injectisome, greatly reduces both the persistence ofP. stewartiiin flea beetle guts and the beetle's ability to transmitP. stewartiito maize. Ectopic expression of thepsaNgene complements these phenotypes. In addition, the PSI-2psaNgene is not required forP. stewartiipathogenesis of maize and is transcriptionally upregulated in insects compared to maize tissues. Thus, the Hrp and PSI-2 T3SSs play different roles in the life cycle ofP. stewartiias it alternates between its insect vector and plant host.

scholarly journals Migration of Type III Secretion System Transcriptional Regulators Links Gene Expression to Secretion

mBio ◽  
2018 ◽  
Vol 9 (4) ◽  
Author(s):  
Spyridoula N. Charova ◽  
Anastasia D. Gazi ◽  
Efstratios Mylonas ◽  
Charalambos Pozidis ◽  
Blanca Sabarit ◽  
...  
Keyword(s):  
Gene Expression ◽  
Type Iii Secretion ◽  
Ternary Complex ◽  
Pathogenic Bacteria ◽  
Transcriptional Regulators ◽  
Economic Importance ◽  
Secretion Systems ◽  
Content Type ◽  
Type Iii ◽  
Type Iii Secretion Systems

ABSTRACTMany plant-pathogenic bacteria of considerable economic importance rely on type III secretion systems (T3SSs) of the Hrc-Hrp 1 family to subvert their plant hosts. T3SS gene expression is regulated through the HrpG and HrpV proteins, while secretion is controlled by the gatekeeper HrpJ. A link between the two mechanisms was so far unknown. Here, we show that a mechanistic coupling exists between the expression and secretion cascades through the direct binding of the HrpG/HrpV heterodimer, acting as a T3SS chaperone, to HrpJ. The ternary complex is docked to the cytoplasmic side of the inner bacterial membrane and orchestrates intermediate substrate secretion, without affecting early substrate secretion. The anchoring of the ternary complex to the membranes potentially keeps HrpG/HrpV away from DNA. In their multiple roles as transcriptional regulators and gatekeeper chaperones, HrpV/HrpG provide along with HrpJ potentially attractive targets for antibacterial strategies.IMPORTANCEOn the basis of scientific/economic importance,Pseudomonas syringaeandErwinia amylovoraare considered among the top 10 plant-pathogenic bacteria in molecular plant pathology. Both employ type III secretion systems (T3SSs) of the Hrc-Hrp 1 family to subvert their plant hosts. For Hrc-Hrp 1, no functional link was known between the key processes of T3SS gene expression and secretion. Here, we show that a mechanistic coupling exists between expression and secretion cascades, through formation of a ternary complex involving the T3SS proteins HrpG, HrpV, and HrpJ. Our results highlight the functional and structural properties of a hitherto-unknown complex which orchestrates intermediate T3SS substrate secretion and may lead to better pathogen control through novel targets for antibacterial strategies.

scholarly journals Development of Two Animal Models To Study the Function of Vibrio parahaemolyticus Type III Secretion Systems

2010 ◽  
Vol 78 (11) ◽  
pp. 4551-4559 ◽  
Author(s):  
Pablo Piñeyro ◽  
Xiaohui Zhou ◽  
Lisa H. Orfe ◽  
Patrick J. Friel ◽  
Kevin Lahmers ◽  
...  
Keyword(s):  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Type Strain ◽  
Deletion Mutant ◽  
Wild Type Strain ◽  
Wild Type ◽  
Secretion Systems ◽  
Type Iii ◽  
Type Iii Secretion Systems ◽  
Mutant Strains

ABSTRACT Vibrio parahaemolyticus is an emerging food- and waterborne pathogen that encodes two type III secretion systems (T3SSs). Previous studies have linked type III secretion system 1 (T3SS1) to cytotoxicity and T3SS2 to intestinal fluid accumulation, but animal challenge models needed to study these phenomena are limited. In this study we evaluated the roles of the T3SSs during infection using two novel animal models: a model in which piglets were inoculated orogastrically and a model in which mice were inoculated in their lungs (intrapulmonarily). The bacterial strains employed in this study had equivalent growth rates and beta-hemolytic activity based on in vitro assays. Inoculation of 48-h-old conventional piglets with 1011 CFU of the wild-type strain (NY-4) or T3SS1 deletion mutant strains resulted in acute, self-limiting diarrhea, whereas inoculation with a T3SS2 deletion mutant strain failed to produce any clinical symptoms. Intrapulmonary inoculation of C57BL/6 mice with the wild-type strain and T3SS2 deletion mutant strains (5 × 105 CFU) induced mortality or a moribund state within 12 h (80 to 100% mortality), whereas inoculation with a T3SS1 deletion mutant or a T3SS1 T3SS2 double deletion mutant produced no mortality. Bacteria were recovered from multiple organs regardless of the strain used in the mouse model, indicating that the mice were capable of clearing the lung infection in the absence of a functional T3SS1. Because all strains had a similar beta-hemolysin phenotype, we surmise that thermostable direct hemolysin (TDH) plays a limited role in these models. The two models introduced herein produce robust results and provide a means to determine how different T3SS1 and T3SS2 effector proteins contribute to pathogenesis of V. parahaemolyticus infection.

scholarly journals Characterization of the Mode of Action of Aurodox, a Type III Secretion System Inhibitor fromStreptomyces goldiniensis

2018 ◽  
Vol 87 (2) ◽  
Author(s):  
Rebecca E. McHugh ◽  
Nicky O’Boyle ◽  
James P. R. Connolly ◽  
Paul A. Hoskisson ◽  
Andrew J. Roe
Keyword(s):  
Escherichia Coli ◽  
Shiga Toxin ◽  
Type Iii Secretion ◽  
Secretion System ◽  
Transcriptional Level ◽  
Secretion Systems ◽  
Content Type ◽  
Type Iii ◽  
Type Iii Secretion Systems

ABSTRACTRecent work has demonstrated that the polyketide natural product Aurodox fromStreptomyces goldiniensisis able to block the pathogenesis of the murine pathogenCitrobacter rodentium. In this work, we aimed to gain a better understanding of the mechanism of action of the compound. We show that Aurodox downregulates the expression of the type III secretion systems of enteropathogenic and enterohemorrhagicEscherichia coli. Furthermore, we have used transcriptomic analysis to show that Aurodox inhibits the expression at the transcriptional level by repressing the master regulator,ler. Our data support a model in which Aurodox acts upstream oflerand not directly on the secretion system itself. Finally, we have shown that Aurodox, unlike some traditional antibiotics, does not induce expression of RecA, which is essential for the production of Shiga toxin. We propose that these properties nominate Aurodox as a promising antivirulence therapy for the treatment of these infections.

scholarly journals The Vibrio parahaemolyticus Type III Secretion Systems manipulate host cell MAPK for critical steps in pathogenesis

2010 ◽  
Vol 10 (1) ◽  
pp. 329 ◽  
Author(s):  
Ksenia Matlawska-Wasowska ◽  
Rebecca Finn ◽  
Ana Mustel ◽  
Conor P O'Byrne ◽  
Alan W Baird ◽  
...  
Keyword(s):  
Host Cell ◽  
Type Iii Secretion ◽  
Vibrio Parahaemolyticus ◽  
Secretion Systems ◽  
Type Iii ◽  
Type Iii Secretion Systems

scholarly journals Tandem Translation Generates a Chaperone for the Salmonella Type III Secretion System Protein SsaQ

2011 ◽  
Vol 286 (41) ◽  
pp. 36098-36107 ◽  
Author(s):  
Xiu-Jun Yu ◽  
Mei Liu ◽  
Steve Matthews ◽  
David W. Holden
Keyword(s):  
Type Iii Secretion ◽  
Ex Vivo ◽  
Eukaryotic Cell ◽  
Effector Proteins ◽  
Secretion Systems ◽  
Type Iii ◽  
Type Iii Secretion Systems ◽  
Function Loss ◽  
Bacterial Cytoplasm

Type III secretion systems (T3SSs) of bacterial pathogens involve the assembly of a surface-localized needle complex, through which translocon proteins are secreted to form a pore in the eukaryotic cell membrane. This enables the transfer of effector proteins from the bacterial cytoplasm to the host cell. A structure known as the C-ring is thought to have a crucial role in secretion by acting as a cytoplasmic sorting platform at the base of the T3SS. Here, we studied SsaQ, an FliN-like putative C-ring protein of the Salmonella pathogenicity island 2 (SPI-2)-encoded T3SS. ssaQ produces two proteins by tandem translation: a long form (SsaQL) composed of 322 amino acids and a shorter protein (SsaQS) comprising the C-terminal 106 residues of SsaQL. SsaQL is essential for SPI-2 T3SS function. Loss of SsaQS impairs the function of the T3SS both ex vivo and in vivo. SsaQS binds to its corresponding region within SsaQL and stabilizes the larger protein. Therefore, SsaQL function is optimized by a novel chaperone-like protein, produced by tandem translation from its own mRNA species.

scholarly journals Type III secretion systems and the evolution of mutualistic endosymbiosis

2002 ◽  
Vol 99 (19) ◽  
pp. 12397-12402 ◽  
Author(s):  
C. Dale ◽  
G. R. Plague ◽  
B. Wang ◽  
H. Ochman ◽  
N. A. Moran
Keyword(s):  
Type Iii Secretion ◽  
Secretion Systems ◽  
Type Iii ◽  
Type Iii Secretion Systems
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