Expression of the low calcium response in Yersinia pestis

Mehigh, Richard J.; Sample, Allen K.; Brubaker, Robert R.

doi:10.1016/0882-4010(89)90070-3

Cited by 34 publications

(49 citation statements)

References 44 publications

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“…We observed moderate (30%) cytotoxicity by the KIM5 ⌬yopB mutant in THP-1 cells in a separate study as well (73). During the course of these infections, some phospho-YopE-ELK was cleaved by Pla, and cleavage of Yops by Pla has been reported previously (46,63,67). However, we were able to detect this cleaved form of phospho-YopE-ELK and include it in our assessment of Yop delivery efficiencies ( Fig.…”

Section: Resultssupporting

confidence: 75%

“…In the ⌬pla mutant, one also observes strong delivery, as analyzed with anti-phospho-ELK antibody, but the anti-ELK antibody reveals that in the ⌬pla mutant, YopE-ELK is no longer cleaved during transfer to host cells (as expected, since cleavage is mediated by Pla). Cleavage of Yops by Pla has been reported previously (46,63,67). One also sees restoration of phospho-YopE-ELK cleavage at all time points in THP-1 cells for the ⌬ail ⌬pla ⌬psaA triple mutant when Pla is reintroduced on a plasmid (see Fig.…”

Section: Methodsmentioning

confidence: 71%

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Three Yersinia pestis Adhesins Facilitate Yop Delivery to Eukaryotic Cells and Contribute to Plague Virulence

2010

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Section: Resultssupporting

confidence: 75%

Section: Methodsmentioning

confidence: 71%

Three Yersinia pestis Adhesins Facilitate Yop Delivery to Eukaryotic Cells and Contribute to Plague Virulence

2010

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“…Nonetheless, Gendlina et al indicated that the Tc proteins may be secreted via the T3SS (9). To further investigate this, we determined if the Y. pestis Tc proteins YitA and YipA are secreted into the culture supernatant during growth under conditions known to be optimal for T3SS-dependent secretion of effector Yop proteins (9,25,29,30). Y. pestis strain KIM10 was used preferentially because it lacks the Pla protease, which is implicated in the degradation of secreted effector proteins (31), although KIM5 and KIM6 variants were also tested.…”

Section: Fig 4 Tc Proteins Do Not Inhibit Killing Of Intracellular Ymentioning

confidence: 98%

Role of Yersinia pestis Toxin Complex Family Proteins in Resistance to Phagocytosis by Polymorphonuclear Leukocytes

Spinner¹,

Carmody

Jarrett

et al. 2013

Infect Immun

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“…Also, metabolic, structural, and enzymatic proteins were differentially expressed, including some potentially involved in virulence, such as OmpA, AmpD3, and ␣-enolase. Other differentially expressed proteins are associated with the Y. pestis inner and outer membranes, including Pla, the maltose binding protein periplasmic protein precursor, Ymt, KatY, and OmpA (24,37,47). The detection of multiple membrane-associated proteins suggests that membrane proteins can be studied by Table 1. VOL.…”

Section: Differential Protein Expression Following Change From 26°cmentioning

confidence: 99%

Proteomic Characterization ofYersinia pestisVirulence

et al. 2005

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The Yersinia pestis proteome was studied as a function of temperature and calcium by two-dimensional differential gel electrophoresis. Over 4,100 individual protein spots were detected, of which hundreds were differentially expressed. A total of 43 differentially expressed protein spots, representing 24 unique proteins, were identified by mass spectrometry. Differences in expression were observed for several virulence-associated factors, including catalase-peroxidase (KatY), murine toxin (Ymt), plasminogen activator (Pla), and F1 capsule antigen (Caf1), as well as several putative virulence factors and membrane-bound and metabolic proteins. Differentially expressed proteins not previously reported to contribute to virulence are candidates for more detailed mechanistic studies, representing potential new virulence determinants.Yersinia pestis, the etiological agent of plague, is a gram-negative bacterium that is both a natural environmental pathogen and a biothreat agent (4,8,32). Early studies of Yersinia physiology uncovered the low calcium response (LCR), whereby bacterial cultures grown in rich medium at an elevated temperature (37°C) exhibit a growth defect upon chelation of calcium ions. The growth arrest was shown to be a result of one of the two type III secretion systems (TTSSs) in Y. pestis, the Ysc TTSS, and is responsible for the secretion of virulence factors known as Yersinia outer proteins, or Yops (21, 29; for a review, see reference 61). This TTSS can be activated in vitro and virulence factors can be released into the medium when Y. pestis is grown at 37°C with submillimolar calcium (for a review, see reference 16). Upon interaction with the host, the TTSS enables virulence factors to enter the host cell through a specialized apparatus, the injectisome (15). Once inside the host cell, Yops affect a variety of host pathways, with detectable expression changes in the pathogen as well as the host (14,52,82).The Y. pestis proteome was previously examined using twodimensional electrophoresis (57,60,71,72). These studies demonstrated that virulence factors were not induced at 26°C or 37°C in the presence of calcium concentrations similar to that found in mammalian plasma (2.5 mM) (71). More recently, the introduction of two-dimensional differential gel electrophoresis (2-D DIGE) has significantly improved the quality of gel-based proteomics through fluorescence-based multiplex analyses providing relative quantitation of expression differences and improved gel-to-gel comparisons (75). Several examples of 2-D DIGE bacterial proteomics have been reported (23), including characterizations of the gram-negative bacterium Escherichia coli (1, 76, 81). Here we report the characterization of the soluble cell-associated proteome of Y. pestis as a function of temperature and calcium, which were used to effect virulence induction. Differentially expressed proteins include virulence-associated factors, membrane-bound proteins, metabolic and housekeeping proteins, and potential new virulence determinants.Bacterial ...

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Expression of the low calcium response in Yersinia pestis

Cited by 34 publications

References 44 publications

Three Yersinia pestis Adhesins Facilitate Yop Delivery to Eukaryotic Cells and Contribute to Plague Virulence

Three Yersinia pestis Adhesins Facilitate Yop Delivery to Eukaryotic Cells and Contribute to Plague Virulence

Role of Yersinia pestis Toxin Complex Family Proteins in Resistance to Phagocytosis by Polymorphonuclear Leukocytes

Proteomic Characterization ofYersinia pestisVirulence

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