Analysis of Yops Secretion by Yersinia pestis Type III Secretion System

Author(s):  
Zongmin Du ◽  
Shiyang Cao
2011 ◽  
Vol 79 (6) ◽  
pp. 1445-1461 ◽  
Author(s):  
Rebecca Dewoody ◽  
Peter M. Merritt ◽  
Andrew S. Houppert ◽  
Melanie M. Marketon

2014 ◽  
Vol 196 (9) ◽  
pp. 1659-1670 ◽  
Author(s):  
C. A. Schiano ◽  
J. T. Koo ◽  
M. J. Schipma ◽  
A. J. Caulfield ◽  
N. Jafari ◽  
...  

2013 ◽  
Vol 58 (2) ◽  
pp. 839-850 ◽  
Author(s):  
Danielle L. Jessen ◽  
David S. Bradley ◽  
Matthew L. Nilles

ABSTRACTNumerous Gram-negative pathogens rely upon type III secretion (T3S) systems to cause disease. Several small-molecule inhibitors of the type III secretion systems have been identified; however, few targets of these inhibitors have been elucidated. Here we report that 2,2′-thiobis-(4-methylphenol) (compound D), inhibits type III secretion inYersinia pestis,Yersinia pseudotuberculosis, andPseudomonas aeruginosa. YopD, a protein involved in the formation of the translocon and regulatory processes of the type III secretion system, appears to play a role in the inhibition of secretion by compound D. The use of compound D in T3S regulatory mutants demonstrated a difference in secretion inhibition in the presence and absence of calcium. Interestingly, compound D was effective only under conditions without calcium, indicating that a secretion-active needle structure may be necessary for compound D to inhibit secretion.


2003 ◽  
Vol 71 (10) ◽  
pp. 5892-5899 ◽  
Author(s):  
Céline Pujol ◽  
James B. Bliska

ABSTRACT Yersinia pestis, the agent of plague, has arisen from a less virulent pathogen, Yersinia pseudotuberculosis, by a rapid evolutionary process. Although Y. pestis displays a large number of virulence phenotypes, it is not yet clear which of these phenotypes descended from Y. pseudotuberculosis and which were acquired independently. Y. pestis is known to replicate in macrophages, but there is no consensus in the literature on whether Y. pseudotuberculosis shares this property. We investigated whether the ability to replicate in macrophages is common to Y. pestis and Y. pseudotuberculosis or is a unique phenotype of Y. pestis. We also examined whether a chromosomal type III secretion system (TTSS) found in Y. pestis is present in Y. pseudotuberculosis and whether this system is important for replication of Yersinia in macrophages. A number of Y. pestis and Y. pseudotuberculosis strains of different biovars and serogroups, respectively, were tested for the ability to replicate in primary murine macrophages. Two Y. pestis strains (EV766 and KIM10+) and three Y. pseudotuberculosis strains (IP2790c, IP2515c, and IP2666c) were able to replicate in macrophages with similar efficiencies. Only one of six strains tested, the Y. pseudotuberculosis YPIII(p−) strain, was defective for intracellular replication. Thus, the ability to replicate in macrophages is conserved in Y. pestis and Y. pseudotuberculosis. Our results also indicate that a homologous TTSS is present on the chromosomes of Y. pestis and Y. pseudotuberculosis and that this secretion system is not required for replication of these bacteria in macrophages.


PLoS ONE ◽  
2011 ◽  
Vol 6 (5) ◽  
pp. e19716 ◽  
Author(s):  
Wieslaw Swietnicki ◽  
Daniel Carmany ◽  
Michael Retford ◽  
Mark Guelta ◽  
Russell Dorsey ◽  
...  

2008 ◽  
Vol 76 (9) ◽  
pp. 3911-3923 ◽  
Author(s):  
Sarit Lilo ◽  
Ying Zheng ◽  
James B. Bliska

ABSTRACT Pathogenic Yersinia species utilize a type III secretion system (T3SS) to translocate effectors called Yersinia outer proteins (Yops) into infected host cells. Previous studies demonstrated a role for effector Yops in the inhibition of caspase-1-mediated cell death and secretion of interleukin-1β (IL-1β) in naïve macrophages infected with Yersinia enterocolitica. Naïve murine macrophages were infected with a panel of different Yersinia pestis and Yersinia pseudotuberculosis strains to determine whether Yops of these species inhibit caspase-1 activation. Cell death was measured by release of lactate dehydrogenase (LDH), and enzyme-linked immunosorbent assay for secreted IL-1β was used to measure caspase-1 activation. Surprisingly, isolates derived from the Y. pestis KIM strain (e.g., KIM5) displayed an unusual ability to activate caspase-1 and kill infected macrophages compared to other Y. pestis and Y. pseudotuberculosis strains tested. Secretion of IL-1β following KIM5 infection was reduced in caspase-1-deficient macrophages compared to wild-type macrophages. However, release of LDH was not reduced in caspase-1-deficient macrophages, indicating that cell death occurred independently of caspase-1. Analysis of KIM-derived strains defective for production of functional effector or translocator Yops indicated that translocation of catalytically active YopJ into macrophages was required for caspase-1 activation and cell death. Release of LDH and secretion of IL-1β were not reduced when actin polymerization was inhibited in KIM5-infected macrophages, indicating that extracellular bacteria translocating YopJ could trigger cell death and caspase-1 activation. This study uncovered a novel role for YopJ in the activation of caspase-1 in macrophages.


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