NEW ANTIGENIC COMPONENT OF<i>PASTEURELLA PESTIS</i>FORMED UNDER SPECIFIED CONDITIONS OF pH AND TEMPERATURE

Ben-Efraim, Shlomo; Aronson, Moshe; Bichowsky-Slomnicki, Leah

doi:10.1128/jb.81.5.704-714.1961

Cited by 57 publications

(31 citation statements)

References 13 publications

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“…Y. pestis also produces surface fimbriae comprising an adhesin termed the pH 6 antigen, which is expressed from the genomic psa operon [38,39]. Thought previously to have a role in the cell-to-cell transmission of Y. pestis in the mammalian host, pH 6 antigen is now thought to bind plasma apo-B lipoprotein (mainly low-density lipoproteins) to the bacterial cell surface [40] to provide an antiphagocytic function [41,42].…”

Section: Expression Of Virulence Factors and Evasion Of Host Innate Imentioning

confidence: 99%

Protecting against plague: towards a next-generation vaccine

Williamson

Oyston

2013

Clinical and Experimental Immunology

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SummaryThe causative organism of plague is the bacterium Yersinia pestis. Advances in understanding the complex pathogenesis of plague infection have led to the identification of the F1-and V-antigens as key components of a nextgeneration vaccine for plague, which have the potential to be effective against all forms of the disease. Here we review the roles of F1-and V-antigens in the context of the range of virulence mechanisms deployed by Y. pestis, in order to develop a greater understanding of the protective immune responses required to protect against plague.

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Section: Expression Of Virulence Factors and Evasion Of Host Innate Imentioning

confidence: 99%

Protecting against plague: towards a next-generation vaccine

Williamson

Oyston

2013

Clinical and Experimental Immunology

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“…Previous studies showed that Y. pestis PsaA expression is only detected in cells grown at temperatures above 36 °C and pH below 6.7 (Lindler et al ., 1990, Ben-Efraim et al ., 1961, Price et al ., 1995). Using Western blotting with a PsaA-specific antibody, we confirmed this result: we were unable to detect PsaA expression from Y. pestis KIM6+ cells grown at 28 °C and pH 6.0 (28 °C/pH 6.0), 28 °C and pH 8.0 (28 °C/pH 8.0), and 37 °C and pH 8.0 (37 °C/pH 8.0), but we detected robust expression at 37 °C and pH 6.0 (37 °C/pH 6.0) (Figure 1A).…”

Section: Resultsmentioning

confidence: 99%

“…Among them, PsaA (“pH 6 antigen”) was first characterized in 1961 by Ben-Efraim and coworkers, and exists in all strains of Y. pestis . PsaA has been reported to be synthesized only at temperatures above 34 °C and pH below 6.7 (Ben-Efraim et al ., 1961). Y. pestis PsaA was reported to be a surface-exposed structure mediating agglutination of erythrocytes from several mammalian species (Bichowsky-Slomnicki & Ben-Efraim, 1963).…”

Section: Introductionmentioning

confidence: 99%

Dissectingpsalocus regulation inYersinia pestis

Wang

Smith

Shi

et al. 2019

Preprint

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The pH 6 antigen of Yersinia pestis is a virulence factor that is expressed in response to high temperature (37 °C) and low pH (6.0). Previous studies have implicated the PsaE and PsaF regulators in the temperature- and pH-dependent regulation of psaA. Here, we show that PsaE levels are themselves controlled by pH and temperature, explaining the regulation of psaA. We identify hundreds of binding sites for PsaE across the Y. pestis genome, with the majority of binding sites located in intergenic regions. However, we detect direct regulation of very few genes by PsaE, suggesting either that most binding sites are non-regulatory, or that they require additional environmental cues. We also identify the precise binding site for PsaE that is required for temperature- and pH-dependent regulation of psaA. Thus, our data reveal the critical function that PsaE plays in regulation of psaA, and suggest that PsaE may have many additional regulatory targets.

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“…Pla, which is absent from the enteric Yersinia , is an outer membrane adhesin and protease that facilitates degradation of extracellular matrix proteins and promotes bacterial dissemination (Sodeinde et al ., 1988; 1992). PsaA, also called MyfA, is present in all three Yersinia spp., but its expression is restricted to slightly acidic conditions at temperatures above 36°C (Ben‐Efraim et al ., ; Iriarte et al ., ; Yang et al ., ). Though Ail is present in all three Yersinia spp., its expression pattern and functionality differs.…”

Section: Introductionmentioning

confidence: 99%

Yersinia pestistargets neutrophils via complement receptor 3

et al. 2014

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Yersinia species display a tropism for lymphoid tissues during infection, and the bacteria select innate immune cells for delivery of cytotoxic effectors by the type III secretion system. Yet the mechanism for target cell selection remains a mystery. Here we investigate the interaction of Yersinia pestis with murine splenocytes to identify factors that participate in the targeting process. We find that interactions with primary immune cells rely on multiple factors. First, the bacterial adhesin Ail is required for efficient targeting of neutrophils in vivo. However, Ail does not appear to directly mediate binding to a specific cell type. Instead, we find that host serum factors direct Y. pestis to specific innate immune cells, particularly neutrophils. Importantly, specificity towards neutrophils was increased in the absence of bacterial adhesins due to reduced targeting of other cell types, but this phenotype was only visible in the presence of mouse serum. Addition of antibodies against complement receptor 3 and CD14 blocked target cell selection, suggesting that a combination of host factors participate in steering bacteria toward neutrophils during plague infection.

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NEW ANTIGENIC COMPONENT OFPASTEURELLA PESTISFORMED UNDER SPECIFIED CONDITIONS OF pH AND TEMPERATURE

Cited by 57 publications

References 13 publications

Protecting against plague: towards a next-generation vaccine

Protecting against plague: towards a next-generation vaccine

Dissectingpsalocus regulation inYersinia pestis

Yersinia pestistargets neutrophils via complement receptor 3

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