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Role of Shiga/Vero Toxins in Pathogenesis

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  • Authors: Fumiko Obata1, Tom Obrig2
  • Editors: Vanessa Sperandio3, Carolyn J. Hovde4
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    Affiliations: 1: University of Maryland School of Medicine, Baltimore, MD 21201; 2: University of Maryland School of Medicine, Baltimore, MD 21201; 3: University of Texas Southwestern Medical Center, Dallas, TX; 4: University of Idaho, Moscow, ID
    • Source: microbiolspec June 2014 vol. 2 no. 3 doi:10.1128/microbiolspec.EHEC-0005-2013
  • Received 01 May 2013 Accepted 29 July 2013 Published 20 June 2014
  • Fumiko Obata, [email protected]
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  • Abstract:

    Shiga toxin (Stx) is the primary cause of severe host responses including renal and central nervous system disease in Shiga toxin-producing (STEC) infections. The interaction of Stx with different eukaryotic cell types is described. Host responses to Stx and bacterial lipopolysaccharide are compared as related to the features of the STEC-associated hemolytic-uremic syndrome (HUS). Data derived from animal models of HUS and central nervous system disease in vivo and eukaryotic cells in vitro are evaluated in relation to HUS disease of humans.

  • Citation: Obata F, Obrig T. 2014. Role of Shiga/Vero Toxins in Pathogenesis. Microbiol Spectrum 2(3):EHEC-0005-2013. doi:10.1128/microbiolspec.EHEC-0005-2013.

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2014-06-20
2021-04-22

Abstract:

Shiga toxin (Stx) is the primary cause of severe host responses including renal and central nervous system disease in Shiga toxin-producing (STEC) infections. The interaction of Stx with different eukaryotic cell types is described. Host responses to Stx and bacterial lipopolysaccharide are compared as related to the features of the STEC-associated hemolytic-uremic syndrome (HUS). Data derived from animal models of HUS and central nervous system disease in vivo and eukaryotic cells in vitro are evaluated in relation to HUS disease of humans.

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Role of Shiga/Vero Toxins in Pathogenesis
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Citation: Obata F, Obrig T. 2014. Role of shiga/vero toxins in pathogenesis. microbiolspec 2(3): doi:10.1128/microbiolspec.EHEC-0005-2013
/content/microbiolspec/10.1128/microbiolspec.EHEC-0005-2013.fig1
FIGURE 1
Schema: Shiga toxin interaction with eukaryotic cells.
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FIGURE 1

Schema: Shiga toxin interaction with eukaryotic cells.

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FIGURE 2
Proposed pathways of Stx and LPS actions in mice. Data derived from a Stx/LPS murine model of HUS indicate that LPS is the primary elicitor of fibrin deposition in kidneys. This pathway requires chemokines and platelets but is not responsible for renal failure. Stx is responsible for renal failure in this murine model in a process that involves nonendothelial renal cell types.
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FIGURE 2

Proposed pathways of Stx and LPS actions in mice. Data derived from a Stx/LPS murine model of HUS indicate that LPS is the primary elicitor of fibrin deposition in kidneys. This pathway requires chemokines and platelets but is not responsible for renal failure. Stx is responsible for renal failure in this murine model in a process that involves nonendothelial renal cell types.

Source: microbiolspec June 2014 vol. 2 no. 3 doi:10.1128/microbiolspec.EHEC-0005-2013
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FIGURE 3
Anti-inflammatory actions of adenosine in HUS. Data derived from an Stx/LPS murine model of HUS suggest adenosine A2a receptor agonist, i.e., adenosine, effectively blocks the actions of LPS (enhanced by Stx2) at the level of different renal cell types to prevent platelet activation and coagulation.
microbiolspec/2/3/EHEC-0005-2013-fig3_thmb.gif
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FIGURE 3

Anti-inflammatory actions of adenosine in HUS. Data derived from an Stx/LPS murine model of HUS suggest adenosine A2a receptor agonist, i.e., adenosine, effectively blocks the actions of LPS (enhanced by Stx2) at the level of different renal cell types to prevent platelet activation and coagulation.

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FIGURE 4
Neutrophil-endothelial cell interactions in HUS. In the Stx2/LPS murine model of HUS, analysis of renal gene activation and neutrophil infiltration into kidneys demonstrates a concomitant increase in PMNs and VCAM-1 expression, suggesting a mechanism of PMN-endothelial association. ♦, Neutrophils in the glomeruli; ▪, VCAM-1 in the glomeruli.
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FIGURE 4

Neutrophil-endothelial cell interactions in HUS. In the Stx2/LPS murine model of HUS, analysis of renal gene activation and neutrophil infiltration into kidneys demonstrates a concomitant increase in PMNs and VCAM-1 expression, suggesting a mechanism of PMN-endothelial association. ♦, Neutrophils in the glomeruli; ▪, VCAM-1 in the glomeruli.

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FIGURE 5
Renal gene activation in the Stx/LPS murine model. Shown are the nine most upregulated genes in the temporal response of mice to either LPS or Stx2. Gene microarrays were employed to analyze kidney gene activation over a 72-h response of C57BL/6 mice to 300 µg/kg of LPS or 100 ng/kg of Stx2.
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FIGURE 5

Renal gene activation in the Stx/LPS murine model. Shown are the nine most upregulated genes in the temporal response of mice to either LPS or Stx2. Gene microarrays were employed to analyze kidney gene activation over a 72-h response of C57BL/6 mice to 300 µg/kg of LPS or 100 ng/kg of Stx2.

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FIGURE 6
Metabolic and catabolic pathway enzymes for Gb synthesis. A part of Gb synthesis pathway is shown. From lactosylceramide (LacCer) to Gb, alpha 1, 4-galactosyltransferase (EC 2.4.1.228) adds a galactose to LacCer to produce Gb. Likewise, UDP-GalNAc: beta 1,3-galactosaminyltransferase (EC 2.4.1.79) works on Gb to make Gb. In the catabolic pathway, beta-hexosaminidase (EC 3.2.1.52) degrades Gb to Gb, and alpha-galactosidase (EC 3.2.1.22) makes LacCer from Gb.
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FIGURE 6

Metabolic and catabolic pathway enzymes for Gb synthesis. A part of Gb synthesis pathway is shown. From lactosylceramide (LacCer) to Gb, alpha 1, 4-galactosyltransferase (EC 2.4.1.228) adds a galactose to LacCer to produce Gb. Likewise, UDP-GalNAc: beta 1,3-galactosaminyltransferase (EC 2.4.1.79) works on Gb to make Gb. In the catabolic pathway, beta-hexosaminidase (EC 3.2.1.52) degrades Gb to Gb, and alpha-galactosidase (EC 3.2.1.22) makes LacCer from Gb.

Source: microbiolspec June 2014 vol. 2 no. 3 doi:10.1128/microbiolspec.EHEC-0005-2013
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Role of Shiga/Vero Toxins in Pathogenesis
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Citation: Obata F, Obrig T. 2014. Role of shiga/vero toxins in pathogenesis. microbiolspec 2(3): doi:10.1128/microbiolspec.EHEC-0005-2013
/content/microbiolspec/10.1128/microbiolspec.EHEC-0005-2013.T1
TABLE 1
STEC oral administration model with CNS descriptions
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TABLE 1

STEC oral administration model with CNS descriptions

Source: microbiolspec June 2014 vol. 2 no. 3 doi:10.1128/microbiolspec.EHEC-0005-2013
/content/microbiolspec/10.1128/microbiolspec.EHEC-0005-2013.T2
TABLE 2
Observed CNS symptoms in animal models
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TABLE 2

Observed CNS symptoms in animal models

Source: microbiolspec June 2014 vol. 2 no. 3 doi:10.1128/microbiolspec.EHEC-0005-2013
/content/microbiolspec/10.1128/microbiolspec.EHEC-0005-2013.T3
TABLE 3
Shiga toxin and/or LPS administration model with CNS descriptions
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TABLE 3

Shiga toxin and/or LPS administration model with CNS descriptions

Source: microbiolspec June 2014 vol. 2 no. 3 doi:10.1128/microbiolspec.EHEC-0005-2013

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