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Chapter 11 : Shiga Toxin-Producing

Authors: Narjol Gonzalez-Escalona1, Jianghong Meng2, Michael P. Doyle3
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Affiliations: 1: Center for Food Safety and Applied Nutrition, Food and Drug Administration, College Park, Maryland; 2: Department of Nutrition and Food Science, University of Maryland, College Park, Maryland; 3: Center for Food Safety, University of Georgia, Griffin, Georgia
Content Type: Reference
Publication Year: 2019

Category: Food Microbiology

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Abstract:

This chapter summarizes the latest information available for Shiga toxin-producing (STEC). STEC was first recognized as a human pathogen in 1982, when O157:H7 was identified as the cause of two outbreaks of hemorrhagic colitis. Since then, many other serogroups of , such as O26, O111, O145, O45, O113, O121, and sorbitol-fermenting O157:NM, have also been associated with cases of hemorrhagic colitis and have been classified as STEC. However, serotype O157:H7 is the predominant cause of STEC-associated disease in the United States and many other countries. Production of Shiga toxins (Stxs) by O157:H7 was subsequently associated with a severe and sometimes fatal condition, hemolytic-uremic syndrome. organisms of many different serotypes can produce Stxs, with more than 600 serotypes being identified so far, including approximately 160 O serogroups and 50 H types. However, only strains that cause hemorrhagic colitis are considered enterohemorrhagic (EHEC), and there are at least 130 EHEC serotypes that have been recovered from human patients. Major non-O157 EHEC serogroups identified in the United States include O26, O45, O103, O111, O121, and O145. Here, we discuss many aspects of their biology, reservoirs, virulence, genomics, and antimicrobial resistance, as well as some recommendations for reduction of their numbers in different foods. We also present some web tools that could help us identify other uncommon causes or vehicles and track down the source of contamination in the future.

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
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Shiga Toxin-Producing Escherichia coli
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Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
/content/10.1128/9781555819972.ch11.ch11fig1
Figure 11.1
Snapshot of the two freely available databases containing all genomes as well as historical metadata (MLST) available for and and the web tool for determination of virulence genes, serotyping, and MLST for . (A) NCBI pathogen detection; (B) EnteroBase; (C) DTU web tool.
10.1128/9781555819972/9972ch11fig1_thmb.gif
10.1128/9781555819972/9972ch11fig1.gif
Image of Figure 11.1
Figure 11.1

Snapshot of the two freely available databases containing all genomes as well as historical metadata (MLST) available for and and the web tool for determination of virulence genes, serotyping, and MLST for . (A) NCBI pathogen detection; (B) EnteroBase; (C) DTU web tool.

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
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Figure 11.2
Neighbor-joining phylogenetic tree of 59 genomes available at NCBI using a custom-made core genome MLST analysis showing distribution on those genomes. The species-based phylogeny was inferred using 820 conserved core genome loci. The two EHEC lineages are shown as well as strains belonging to the German outbreak of . O104:H4 in 2011 ( EAEC). The colors represent the presence and type of gene.
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Image of Figure 11.2
Figure 11.2

Neighbor-joining phylogenetic tree of 59 genomes available at NCBI using a custom-made core genome MLST analysis showing distribution on those genomes. The species-based phylogeny was inferred using 820 conserved core genome loci. The two EHEC lineages are shown as well as strains belonging to the German outbreak of . O104:H4 in 2011 ( EAEC). The colors represent the presence and type of gene.

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
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Figure 11.3
Number of cases of STEC disease in the United States by year, 2010 to 2014 (https://www.cdc.gov/ecoli/surveillance.html). Unk, unknown.
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Image of Figure 11.3
Figure 11.3

Number of cases of STEC disease in the United States by year, 2010 to 2014 (https://www.cdc.gov/ecoli/surveillance.html). Unk, unknown.

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
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Figure 11.4
Electron microscopy image of an A/E lesion and schematic illustration of A/E lesion formation in EHEC. Effector proteins undergo A/E translocation through the T3SS, which forms a pore through the membranes of EHEC. EHEC translocates a number of proteins: EspB and EspD, which form a translocon in the plasma membrane; the cytoplasmic proteins EspF, EspG, and Map; the translocated intimin receptor Tir, which inserts into the plasma membrane; and other unidentified effectors. Formation of the EHEC pedestal is also shown. EHEC intimately attaches to the host cell through intimin-Tir binding. The binding triggers the formation of actin-rich pedestals beneath adherent bacteria after Wiskott-Aldrich syndrome protein and the heptameric actin-related protein Arp2/3 are recruited to the pedestal tip. Reproduced from reference with permission.
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Image of Figure 11.4
Figure 11.4

Electron microscopy image of an A/E lesion and schematic illustration of A/E lesion formation in EHEC. Effector proteins undergo A/E translocation through the T3SS, which forms a pore through the membranes of EHEC. EHEC translocates a number of proteins: EspB and EspD, which form a translocon in the plasma membrane; the cytoplasmic proteins EspF, EspG, and Map; the translocated intimin receptor Tir, which inserts into the plasma membrane; and other unidentified effectors. Formation of the EHEC pedestal is also shown. EHEC intimately attaches to the host cell through intimin-Tir binding. The binding triggers the formation of actin-rich pedestals beneath adherent bacteria after Wiskott-Aldrich syndrome protein and the heptameric actin-related protein Arp2/3 are recruited to the pedestal tip. Reproduced from reference with permission.

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
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Figure 11.5
Genetic organization of the EHEC LEE and EHEC prophages CP-933U, CP-933K, and CP-933P. Reproduced from reference .
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Image of Figure 11.5
Figure 11.5

Genetic organization of the EHEC LEE and EHEC prophages CP-933U, CP-933K, and CP-933P. Reproduced from reference .

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
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Figure 11.6
T3SS apparatus of EHEC. The basal body of the T3SS is composed of the secretin EscC, the inner membrane proteins EscR, EscS, EscT, EscU, and EscV, and the EscJ lipoprotein, which connects the inner and outer membrane ring structures. EscF constitutes the needle structure, whereas EspA subunits polymerize to form the EspA filament. EspB and EspD form the translocation pore in the host cell plasma membrane, connecting the bacteria with the eukaryotic cell via EspA filaments. The cytoplasmic ATPase EscN provides the energy to the system by hydrolyzing ATP molecules into ADP. SepD and SepL are represented as cytoplasmic components of the T3SS. Reproduced from reference .
10.1128/9781555819972/9972ch11fig6_thmb.gif
10.1128/9781555819972/9972ch11fig6.gif
Image of Figure 11.6
Figure 11.6

T3SS apparatus of EHEC. The basal body of the T3SS is composed of the secretin EscC, the inner membrane proteins EscR, EscS, EscT, EscU, and EscV, and the EscJ lipoprotein, which connects the inner and outer membrane ring structures. EscF constitutes the needle structure, whereas EspA subunits polymerize to form the EspA filament. EspB and EspD form the translocation pore in the host cell plasma membrane, connecting the bacteria with the eukaryotic cell via EspA filaments. The cytoplasmic ATPase EscN provides the energy to the system by hydrolyzing ATP molecules into ADP. SepD and SepL are represented as cytoplasmic components of the T3SS. Reproduced from reference .

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
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Tables

Shiga Toxin-Producing Escherichia coli
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Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
/content/10.1128/9781555819972.ch11.ch11tab1
Table 11.1
Comparison of values for O157:H7 and spp. in ground beef
Generic image for table
Table 11.1

Comparison of values for O157:H7 and spp. in ground beef

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
/content/10.1128/9781555819972.ch11.ch11tab2
Table 11.2
Vehicles of foodborne outbreaks and associated cases of O157 infections in the United States between 2011 and 2015
Generic image for table
Table 11.2

Vehicles of foodborne outbreaks and associated cases of O157 infections in the United States between 2011 and 2015

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
/content/10.1128/9781555819972.ch11.ch11tab3
Table 11.3
Representative foodborne and waterborne outbreaks of O157:H7 and other STEC infections
Generic image for table
Table 11.3

Representative foodborne and waterborne outbreaks of O157:H7 and other STEC infections

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11
/content/10.1128/9781555819972.ch11.ch11tab4
Table 11.4
Nomenclature and biological characteristics of Stxs
Generic image for table
Table 11.4

Nomenclature and biological characteristics of Stxs

Citation: Gonzalez-Escalona N, Meng J, Doyle M. 2019. Shiga Toxin-Producing , p 289-315. In Doyle M, Diez-Gonzalez F, Hill C (ed), Food Microbiology: Fundamentals and Frontiers, 5th Edition. ASM Press, Washington, DC. doi: 10.1128/9781555819972.ch11

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