scholarly journals DIFFERENTIAL INHIBITORY EFFECTS OF CHOLERA TOXOIDS AND GANGLIOSIDE ON THE ENTEROTOXINS OF VIBRIO CHOLERAE AND ESCHERICHIA COLI

1973 ◽  
Vol 137 (4) ◽  
pp. 1009-1023 ◽  
Author(s):  
Nathaniel F. Pierce
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Competitive Inhibitor ◽  
Inhibitory Effect ◽  
Inhibitory Effects ◽  
E Coli ◽  
Stable Component ◽  
Heat Stable ◽  
Cholera Enterotoxin ◽  
Gut Mucosa

Natural cholera toxoid appears to act as a competitive inhibitor of cholera enterotoxin and is thus a useful tool for studying the interaction of cholera enterotoxin with cell membranes. Cholera enterotoxin binds to gut mucosa more rapidly than does its natural toxoid. Once binding occurs, however, it appears to be prolonged for both materials. Formalinized cholera toxoid has no inhibitory effect upon cholera enterotoxin. Enterotoxic activity, ability to bind to gut mucosa, and antitoxigenicity appear to be independent properties of cholera enterotoxin. Natural cholera toxoid does not inhibit Escherichia coli enterotoxin, indicating that although the two enterotoxins activate the same mucosal secretory mechanism they occupy different binding sites in the mucosa. Ganglioside, which may be the mucosal receptor of cholera enterotoxin, is highly efficient in deactivating cholera enterotoxin. By contrast, ganglioside is relatively inefficient in deactivating heat-labile E. coli enterotoxin and is without effect upon the heat-stable component of E. coli enterotoxin. These findings suggest that ganglioside is not likely to be the mucosal receptor for E. coli enterotoxin. Differences in cellular binding of E. coli and cholera enterotoxins may explain, at least in part, the marked differences in the time of onset and duration of their effects upon gut secretion.

Enhanced Inhibition of Escherichia coli O157:H7 by Lysozyme and Chelators

2003 ◽  
Vol 66 (10) ◽  
pp. 1783-1789 ◽  
Author(s):  
J. S. BOLAND ◽  
P. M. DAVIDSON ◽  
J. WEISS
Keyword(s):  
Escherichia Coli ◽  
Inhibitory Activity ◽  
Chelating Agents ◽  
Inhibitory Effect ◽  
Escherichia Coli O157 ◽  
Inhibitory Effects ◽  
Antimicrobial Spectrum ◽  
E Coli ◽  
Dilution Assay ◽  
Microbroth Dilution

This study examined the effects of three chelating agents (EDTA, disodium pyrophosphate [DSPP], and pentasodium tripolyphosphate [PSTPP]) on the inhibition of the growth of Escherichia coli O157:H7 by lysozyme. The objective of this study was to identify replacement chelators that exhibit synergistic properties similar to those of EDTA. The inhibitory effects of EDTA at 300 to 1,500 μg/ml and of DSPP and PSTPP at 3,000 to 15,000 μg/ml in combination with lysozyme at 200 to 600 μg/ml for up to 48 h at pHs of 6.0, 7.0, and 8.0 on four strains of E. coli O157:H7 was studied with the use of a microbroth dilution assay. The addition of EDTA enhanced lysozyme's inhibitory effect on strains of E. coli O157:H7. EDTA at ≥300 μg/ml combined with lysozyme at 200 to 600 μg/ml was sufficient to inhibit the growth of the strains at pHs of 6.0 and 8.0. At pH 7.0, lysozyme at 200 to 600 μg/ml and EDTA concentrations of ≥1,000 μg/ml were effective in inhibiting three of the four strains. DSPP at pH 6.0 was inhibitory at ≥10,000 μg/ml when combined with lysozyme at 200 to 300 μg/ml. In contrast, PSTPP increased the inhibitory activity of lysozyme more effectively at pH 8.0. Lysozyme at 200 to 600 μg/ml was effective against two strains of E. coli O157:H7 when used in conjunction with PSTPP at ≥5,000 μg/ml. The remaining strains were inhibited by PSTPP at ≥10,000 μg/ml. Our results indicate that inhibition occurred with each lysozyme-chelator combination, but the concentrations of phosphates required to increase the antimicrobial spectrum of lysozyme against E. coli O157:H7 were higher than the EDTA concentrations required to achieve the same effect.

scholarly journals Binding of Escherichia coli heat-stable enterotoxin to receptors on rat intestinal cells

1983 ◽  
Vol 245 (4) ◽  
pp. G492-G498 ◽  
Author(s):  
R. A. Giannella ◽  
M. Luttrell ◽  
M. Thompson
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Intestinal Epithelial Cells ◽  
Cell Number ◽  
Intestinal Cells ◽  
Negative Cooperativity ◽  
Intestinal Epithelial ◽  
Temperature Dependent ◽  
E Coli ◽  
Heat Stable

This study was performed to determine whether receptors for Escherichia coli heat-stable enterotoxin (ST) exist on intestinal epithelial cells. Binding sites for 125I-ST were found on rat jejunal and ileal villus cells. Binding was rapid, reversible, linear with cell number, saturable, and temperature dependent. Significant degradation of 125I-ST occurred when incubated with cells at 37 degrees C but not at 25 degrees C. Binding was specific to ST since binding of 125I-ST was competitively inhibited by increasing concentrations of human or porcine ST but not by E. coli heat-labile, cholera, or staphylococcal enterotoxins. Addition of excess unlabeled ST to cells preincubated with 125I-ST resulted in dissociation of much but not all of the bound 125I-ST. Binding of 125I-ST to jejunal and ileal cells occurs with two affinities, and this is due to the phenomenon of negative cooperativity. The potency of ST for inhibiting the binding of 125I-ST was identical to the potency of ST in stimulating cGMP production. These data support the existence of receptors for ST on intestinal cells, and these receptors may be involved in the action of ST.

scholarly journals Increasing the Oxidative Stress Response Allows Escherichia coli To Overcome Inhibitory Effects of Condensed Tannins

2003 ◽  
Vol 69 (6) ◽  
pp. 3406-3411 ◽  
Author(s):  
Alexandra H. Smith ◽  
James A. Imlay ◽  
Roderick I. Mackie
Keyword(s):  
Oxidative Stress ◽  
Escherichia Coli ◽  
Stress Response ◽  
Condensed Tannins ◽  
Resistant Mutant ◽  
Inhibitory Effect ◽  
Oxidative Stress Response ◽  
Inhibitory Effects ◽  
Acacia Mearnsii ◽  
E Coli

ABSTRACT Tannins are plant-derived polyphenols with antimicrobial effects. The mechanism of tannin toxicity towards Escherichia coli was determined by using an extract from Acacia mearnsii (Black wattle) as a source of condensed tannins (proanthocyanidins). E. coli growth was inhibited by tannins only when tannins were exposed to oxygen. Tannins auto-oxidize, and substantial hydrogen peroxide was generated when they were added to aerobic media. The addition of exogenous catalase permitted growth in tannin medium. E. coli mutants that lacked HPI, the major catalase, were especially sensitive to tannins, while oxyR mutants that constitutively overexpress antioxidant enzymes were resistant. A tannin-resistant mutant was isolated in which a promoter-region point mutation increased the level of HPI by 10-fold. Our results indicate that wattle condensed tannins are toxic to E. coli in aerobic medium primarily because they generate H2O2. The oxidative stress response helps E. coli strains to overcome their inhibitory effect.

Inhibitory effect of Zanthoxylum bungeanum essential oil (ZBEO) on Escherichia coli and intestinal dysfunction

2017 ◽  
Vol 8 (4) ◽  
pp. 1569-1576 ◽  
Author(s):  
Lei Hong ◽  
Wu Jing ◽  
Wang Qing ◽  
Su Anxiang ◽  
Xue Mei ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Essential Oil ◽  
Inhibitory Effect ◽  
Intestinal Health ◽  
Inhibitory Effects ◽  
E Coli ◽  
Zanthoxylum Bungeanum

The inhibitory effects of Zanthoxylum bungeanum essential oil (ZBEO) on Escherichia coli (E. coli) in vitro and in vivo were investigated, as well as its function of improvement of intestinal health.

scholarly journals The purification and properties of Escherichia coli methylglyoxal synthase

1972 ◽  
Vol 128 (2) ◽  
pp. 321-329 ◽  
Author(s):  
D. J. Hopper ◽  
R. A. Cooper
Keyword(s):  
Escherichia Coli ◽  
Binding Sites ◽  
Competitive Inhibitor ◽  
Dihydroxyacetone Phosphate ◽  
Ph Optimum ◽  
E Coli ◽  
Atp Formation ◽  
Purification And Properties ◽  
K 12 ◽  
Methylglyoxal Synthase

1. Methylglyoxal synthase was purified over 1500-fold from glycerol-grown Escherichia coli K 12 strain CA 244. The purified enzyme was inactivated by heat or proteolysis, had a molecular weight of approx. 67000, a pH optimum of 7.5 and was specific for dihydroxyacetone phosphate with Km 0.47mm. 2. The possibility that a Schiff-base intermediate was involved in the reaction mechanism was investigated but not confirmed. 3. The purified enzyme lost activity, especially at low temperature, but could be stabilized by Pi. Two binding sites for Pi may be present on the enzyme. Of other compounds tested only the substrate, dihydroxyacetone phosphate, and bovine serum albumin showed any significant stabilizing effect. 4. Phosphoenolpyruvate, 3-phosphoglycerate, PPi and Pi were potent inhibitors of the enzyme. Kinetic experiments showed that PPi was apparently a simple competitive inhibitor, but inhibition by the other compounds was more complex. In the presence of Pi the enzyme behaved co-operatively, with at least three binding sites for dihydroxyacetone phosphate. 5. It is proposed that methylglyoxal synthase and glyceraldehyde 3-phosphate dehydrogenase play important roles in the catabolism of the triose phosphates in E. coli. Channelling of dihydroxyacetone phosphate via methylglyoxal would not be linked to ATP formation and could be involved in the uncoupling of catabolism and anabolism.

Screening of Commercial and Pecan Shell–Extracted Liquid Smoke Agents as Natural Antimicrobials against Foodborne Pathogens

2012 ◽  
Vol 75 (6) ◽  
pp. 1148-1152 ◽  
Author(s):  
ELLEN J. VAN LOO ◽  
D. BABU ◽  
PHILIP G. CRANDALL ◽  
STEVEN C. RICKE
Keyword(s):  
Escherichia Coli ◽  
Foodborne Pathogens ◽  
Salmonella Enteritidis ◽  
Antioxidant Properties ◽  
Inhibitory Effects ◽  
Natural Antimicrobials ◽  
E Coli ◽  
Liquid Smoke ◽  
Water Based ◽  
Smoke Sample

Liquid smoke extracts have traditionally been used as flavoring agents, are known to possess antioxidant properties, and serve as natural alternatives to conventional antimicrobials. The antimicrobial efficacies of commercial liquid smoke samples may vary depending on their source and composition and the methods used to extract and concentrate the smoke. We investigated the MICs of eight commercial liquid smoke samples against Salmonella Enteritidis, Staphylococcus aureus, and Escherichia coli. The commercial liquid smoke samples purchased were supplied by the manufacturer as water-based or concentrated extracts of smoke from different wood sources. The MICs of the commercial smokes to inhibit the growth of foodborne pathogens ranged from 0.5 to 6.0% for E. coli, 0.5 to 8.0% for Salmonella, and 0.38 to 6% for S. aureus. The MIC for each liquid smoke sample was similar in its effect on both E. coli and Salmonella. Solvent-extracted antimicrobials prepared using pecan shells displayed significant differences between their inhibitory concentrations depending on the type of solvent used for extraction. The results indicated that the liquid smoke samples tested in this study could serve as effective natural antimicrobials and that their inhibitory effects depended more on the solvents used for extraction than the wood source.

Comparison of colony and stool blots for detection of enteropathogens by DNA probes

1991 ◽  
Vol 37 (5) ◽  
pp. 407-410
Author(s):  
Mônica A. M. Vieira ◽  
Beatriz E. C. Guth ◽  
Tânia A. T. Gomes
Keyword(s):  
Escherichia Coli ◽  
Key Words ◽  
Sensitivity And Specificity ◽  
Dna Probes ◽  
Type I ◽  
Enteropathogenic Escherichia Coli ◽  
Key Words Dna ◽  
E Coli ◽  
Heat Stable

DNA probes that identify genes coding for heat-labile type I (LT-I) and heat-stable type 1 (ST-I) enterotoxins, enteropathogenic Escherichia coli adherence factor (EAF), and Shigella-like, invasiveness (INV) are used to evaluate the sensitivity and specificity of stool blots in comparison with the sensitivity and specificity of colony blots in detecting enteropathoghens. The sensitivities of the probes in stool blots are 91.7% for the LT-I probe, 76.9% for the ST-I probes, 78.9% for the EAF probe, and 45.5% for the INV probe. The specificity of all probes is higher than 95%. In general, the stool blot method identifies as many if not more LT-I-, ST-I-, and EAF-producing E. coli infections than the colony blots. Key words: DNA probes, stool blots, enteropathogens, diagnosis.

scholarly journals Fnr-, NarP- and NarL-Dependent Regulation of Transcription Initiation from the Haemophilus influenzae Rd napF (Periplasmic Nitrate Reductase) Promoter in Escherichia coli K-12

2005 ◽  
Vol 187 (20) ◽  
pp. 6928-6935 ◽  
Author(s):  
Valley Stewart ◽  
Peggy J. Bledsoe
Keyword(s):  
Escherichia Coli ◽  
Nitrate Reductase ◽  
Haemophilus Influenzae ◽  
Control Region ◽  
Binding Sites ◽  
Transcription Initiation ◽  
Transcriptional Control ◽  
Class I ◽  
E Coli ◽  
Fnr Protein

ABSTRACT Periplasmic nitrate reductase (napFDAGHBC operon product) functions in anaerobic respiration. Transcription initiation from the Escherichia coli napF operon control region is activated by the Fnr protein in response to anaerobiosis and by the NarQ-NarP two-component regulatory system in response to nitrate or nitrite. The binding sites for the Fnr and phospho-NarP proteins are centered at positions −64.5 and −44.5, respectively, with respect to the major transcription initiation point. The E. coli napF operon is a rare example of a class I Fnr-activated transcriptional control region, in which the Fnr protein binding site is located upstream of position −60. To broaden our understanding of napF operon transcriptional control, we studied the Haemophilus influenzae Rd napF operon control region, expressed as a napF-lacZ operon fusion in the surrogate host E. coli. Mutational analysis demonstrated that expression required binding sites for the Fnr and phospho-NarP proteins centered at positions −81.5 and −42.5, respectively. Transcription from the E. coli napF operon control region is activated by phospho-NarP but antagonized by the orthologous protein, phospho-NarL. By contrast, expression from the H. influenzae napF-lacZ operon fusion in E. coli was stimulated equally well by nitrate in both narP and narL null mutants, indicating that phospho-NarL and -NarP are equally effective regulators of this promoter. Overall, the H. influenzae napF operon control region provides a relatively simple model for studying synergistic transcription by the Fnr and phospho-NarP proteins acting from class I and class II locations, respectively.

scholarly journals Erratum

2003 ◽  
Vol 130 (3) ◽  
pp. 573-573
Author(s):  
Z. ZHOU ◽  
J. OGASAWARA ◽  
Y. NISHIKAWA
Keyword(s):  
Escherichia Coli ◽  
E Coli ◽  
Heat Stable ◽  
Epidemiol Infect

Epidemiol. Infect. 128 (2002), 363–371An outbreak of gastroenteritis in Osaka, Japan due toEscherichia coliserogroup O166[ratio ]H15 that had a coding gene for enteroaggregativeE. coliheat-stable enterotoxin 1 (EAST1)Tables 1 and 2 were omitted

scholarly journals Effects of Essential Oils on Escherichia coli Inactivation in Cheese as Described by Meta-Regression Modelling

Foods ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 716
Author(s):  
Beatriz Nunes Silva ◽  
Vasco Cadavez ◽  
José António Teixeira ◽  
Ursula Gonzales-Barron
Keyword(s):  
Escherichia Coli ◽  
Essential Oils ◽  
Meta Analysis ◽  
Inhibitory Effects ◽  
Food Preservatives ◽  
E Coli ◽  
Log Reduction ◽  
Bactericidal Properties ◽  
Study Characteristics ◽  
Meta Regression

The growing intention to replace chemical food preservatives with plant-based antimicrobials that pose lower risks to human health has produced numerous studies describing the bactericidal properties of biopreservatives such as essential oils (EOs) in a variety of products, including cheese. This study aimed to perform a meta-analysis of literature data that could summarize the inactivation of Escherichia coli in cheese achieved by added EOs; and compare its inhibitory effectiveness by application method, antimicrobial concentration, and specific antimicrobials. After a systematic review, 362 observations on log reduction data and study characteristics were extracted from 16 studies. The meta-regression model suggested that pathogenic E. coli is more resistant to EO action than the non-pathogenic type (p < 0.0001), although in both cases the higher the EO dose, the greater the mean log reduction achieved (p < 0.0001). It also showed that, among the factual application methods, EOs’ incorporation in films render a steadier inactivation (p < 0.0001) than when directly applied to milk or smeared on cheese surface. Lemon balm, sage, shallot, and anise EOs showed the best inhibitory outcomes against the pathogen. The model also revealed the inadequacy of inoculating antimicrobials in cheese purposely grated for performing challenge studies, as this non-realistic application overestimates (p < 0.0001) the inhibitory effects of EOs.

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