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PubMed2001

Effect of acid resistance of Escherichia coli O157:H7 on efficacy of buffered lactic acid to decontaminate chilled beef tissue and effect of modified atmosphere packaging on survival of Escherichia coli O157:H7 on red meat.

The present study examined the effect of pH-independent acid resistance of Escherichia coli O157:H7 on efficacy of buffered lactic acid to decontaminate chilled beef tissue. A varied level of acid resistance was observed among the 14 strains tested. Eight strains were categorized as acid resistant, four strains as acid sensitive, and two strains demonstrated acid-inducible acid resistance. The survival of an acid-resistant (II/45/4) and acid-sensitive (IX/8/16) E. coli O157:H7 strain on chilled beef tissue treated with 1 and 2% buffered lactic acid, sterile water, or no treatment (control) was followed. A gradual reduction of E. coli O157:H7 was noticed during the 10 days of storage at 4 degrees C for each of the treatments. Decontamination with 1 and 2% buffered lactic acid did not appreciably affect the pathogen. Differences in the pH-independent acid resistance of the strains had no effect on the efficacy of decontamination. The effect of modified atmosphere packaging (MAP) on survival of E. coli O157:H7 in red meat was also studied. MAP (40% CO2/60% N2) or vacuum did not significantly influence survival of E. coli O157:H7 on inoculated sliced beef (retail cuts) meat compared to packing in air. The relative small outgrowth of lactic acid bacteria during storage under vacuum for 28 days did not affect survival of E. coli O157:H7. Neither lactic acid decontamination nor vacuum or MAP packaging could enhance reduction of E. coli O157:H7 on beef, thus underlining the need for preventive measures to control the public health risk of E. coli O157:H7.

Adaptation, Physiological↗
PubMed2002

Effectiveness of spraying with tween 20 and lactic acid in decontaminating inoculated Escherichia coli O157:H7 and indigenous Escherichia coli biotype I on beef.

Beef carcass quarters and fat-covered subprimal cuts were suspended vertically and inoculated with a bovine manure slurry containing a five-strain mixture of Escherichia coli O157:H7 to deliver about 4 to 5 log10 CFU/cm2. To identify treatments that would improve the effectiveness of spraying with lactic acid (LA), the inoculated quarters and cuts were treated as follows: experiment A, (i) not treated (control), (ii) sprayed with 2% (vol/vol) LA, (iii) tempered at 21 degrees C for 4 h, and (iv) tempered and then sprayed with LA; experiment B, (v) sprayed with water, (vi) sprayed with LA, (vii) sprayed with LA containing 0.5% (vol/vol) sodium benzoate (SB), and (viii) sprayed with LA containing SB and 5% (vol/vol) Tween 20 (TW20); and experiment C, (ix) sprayed with water (no prespray), (x) presprayed with TW20 and then sprayed with LA, and (xi) presprayed with TW20 and then sprayed with LA containing SB. In experiment A, spraying carcasses with LA significantly (P < 0.05) reduced the numbers of E. coli Biotype I and serotype O157:H7 after 1 and 3 days of storage, respectively. The tempering process employed did not affect the effectiveness of the LA spray on either type of E. coli. In experiment B, there was no significant difference in the reduction of E. coli O157:H7 on subprimal cuts sprayed with water and that on cuts sprayed with LA alone or with LA in combination with SB and TW20 after 1 or 3 days of storage (total reductions ranged from about 1.6 to 2.8 log10 CFU/cm2). In experiment C, prespraying subprimal cuts with TW20 significantly (P < 0.05) increased the effectiveness of LA (reductions of 2.8 and 3.2 log10 CFU/cm2, respectively) and that of LA with SB (reductions of 2.6 and 3.3 log10 CFU/cm2, respectively) compared with spraying with water alone (reductions of ca. 1.0 and 2.0 log10 CFU/cm2, respectively) after I and 3 days of storage, respectively. In a separate experiment, the incorporation of TW20 (0.1 or 0.25%) into buffered peptone water prior to the maceration of excised carcass surface samples resulted in the recovery of significantly larger numbers (ca. 5.1 to 5.2 log10 CFU/cm2) of E. coli O157:H7 cells than did the control treatment without added TW20 (ca. 3.8 to 4.6 log10 CFU/cm2). These results demonstrate that the treatment of beef carcasses with LA reduces the number of viable E. coli O157:H7 cells and that this inactivation or removal by LA is enhanced by prespraying of the carcass with a 5% solution of TW20.

Animals↗
PubMed2002

Polymerase chain reaction assay for detection of Escherichia coli O157: H7 and Escherichia coli O157: H-.

The DNA band patterns generated by polymerase chain reaction (PCR) using the du2 primer and template DNAs from various strains of Escherichia coli and non-E. coli bacteria were compared. Among three to five prominent bands produced, the three bands at about 1.8, 2.7, and 5.0 kb were detected in all of the E. coli O157 strains tested. Some nonpathogenic E. coli and all pathogenic E. coli except E. coli O157 showed bands at 1.8 and 5.0 kb. It seems that the band at 2.7 kb is specific to E. coli O157. Sequence analysis of the 2.7-kb PCR product revealed the presence of a DNA sequence specific to E. coli O157:H- and E. coli O157:H7. Since the DNA sequence from base 15 to base 1,008 of the PCR product seems to be specific to E. coli O157, a PCR assay was carried out with various bacterial genomic DNAs and O157-FHC1 and O157-FHC2 primers that amplified the region between base 23 and base 994 of the 2.7-kb PCR product. A single band at 970 bp was clearly detected in all of the strains of E. coli O157:H- and E. coli O157:H7 tested. However, no band was amplified from template DNAs from other bacteria, including both nonpathogenic and pathogenic E. coli except E. coli O157. All raw meats inoculated with E. coli O157:H7 at 3 x 10(0) to 3.5 x 10(2) CFU/25 g were positive both for our PCR assay after cultivation in mEC-N broth at 42 degrees C for 18 h and for the conventional cultural method.

Animals↗
PubMed2004

Escherichia coli O157 prevalence and enumeration of aerobic bacteria, Enterobacteriaceae, and Escherichia coli O157 at various steps in commercial beef processing plants.

The effectiveness of current antimicrobial interventions used in reducing the prevalence or load of Escherichia coli O157 and indicator organisms on cattle hides and carcasses at two commercial beef processing plants was evaluated. Sponge sampling of beef cattle was performed at five locations from the initial entry of the animals to the slaughter floor to the exit of carcasses from the "hotbox" cooler. For each sample, E. coli O157 prevalence was determined and total aerobic bacteria, Enterobacteriaceae, and E. coli O157 were enumerated. E. coli O157 was found on 76% of animal hides coming into the plants, but no carcasses leaving the cooler were identified as contaminated with E. coli O157. A positive relationship was seen between the incidence of E. coli O157 in hide samples and that in preevisceration samples. Aerobic plate counts and Enterobacteriaceae counts averaged 7.8 and 6.2 log CFU/100 cm2, respectively, on hides, and 1.4 and 0.4 log CFU/100 cm2, respectively, on chilled carcasses. Aerobic plate counts and Enterobacteriaceae counts on preevisceration carcasses were significantly related to the respective levels on the corresponding hides; the carcasses of animals whose hides carried higher numbers of bacteria were more likely to carry higher numbers of bacteria. Implementation of the sampling protocol described here would allow processors to evaluate the efficacy of on-line antimicrobial interventions and allow industrywide benchmarking of hygienic practices.

Animals↗
PubMed1975

The structural basis for the resistance of Escherichia coli formylmethionyl transfer ribonucleic acid to cleavage by Escherichia coli peptidyl transfer ribonucleic acid hydrolase.

Escherichia coli formylmethionly-tRNA-tMet is unique among N-acylaminoacyl-tRNAs in its resistance to cleavage by peptidyl-tRNA hydrolase. Chemical modification of tRNA-fMet with sodium bisulfite converts fMet-tRNA-fMet into a good substrate for the hydrolase. The products of the enzymatic cleavage are free tRNA-fMet and formylmethionine. Bisulfite treatment produces cytidine to uridine base changes at several sites in the tRNA structure. One of these modifications results in formation of a new hydrogen-bonded base pair at the end of the acceptor stem of tRNA-fMet. We have shown that this modification is responsible for the observed change in biological activity. Enzymatic cleavage appears to be facilitated by the presence of a 5-terminal phosphate at the end of a fully base-paired acceptor stem, because removal of the 5-phosphate group from N-acetylphenylalanyl-tRNA-Phe or bisulfite-modified fMet-tRNA-FMet reduced the rate of hydrolysis of these substrates. The unpaired base at the 5 terminus of unmodified fMet-tRNA-fMet appears to reduce susceptibility of the tRNA to hydrolytic attack both by positioning the 5-phosphate in an unfavorable orientation and by directly interfering with enzymatic binding. The unusual structure of the acceptor stem of this E. coli tRNA thus plays a critical role in maintaining the viability of the organism by preventing enzymatic cleavage of the fMet group from the bacterial initiator tRNA.

Amino Acyl-tRNA Synthetases↗
PubMed1990

Modulating the microbial colonization of the gastrointestinal tract by oral administration of defined Escherichia coli strains. I. Influencing the biotope by means of metabolic drift mutants of Escherichia coli.

Through the selection of spontaneous metabolic drift mutants (selection marker RifR) of an Escherichia coli strain (O6:H2 SmR) of known settling capacity in conventional mice, it was attempted to obtain clones with positively optimized in vitro characteristics, which may exert a promotive influence upon the in vivo colonizing behaviour. Using 512 drift mutant strains (E. coli O6:H2 SmR RifR) we were able to establish positive optimizations, at an over-aleatory rate, for each of the in vitro characters tested (haemagglutination capacity of rabbit, guinea pig, and fowl erythrocytes; overgrowing power of mouse-adapted wild-type E. coli strains; formation of biomass with exclusive utilization of dextrose, lactose, fructose, adonitol, salicin, rhamnose, mannose; multiplying power; quantitative motility; and capacity to synthesize mucus). A higher settling rate (larger number of animals in which the test strain shared greater than or equal to 50% of the Enterobacteriaceae population than that obtained with the initial strain) could be established for one out of the 62 clones tested in vivo (a rise from 20% to 55%). The higher settling rate was associated with combinations of various functional parameters and not with an improvement of any of the individual functions. Despite the increase in settling rate relative to the number of experimental animals used in these studies, it was not generally possible to obtain a more than 3 days' dominance of the test strain within the lac+ Enterobacteriaceae. This is considered to be due primarily to the incipient synthesis of secretory IgA.

Administration, Oral↗
PubMed1990

Modulating the microbial colonization of the gastrointestinal tract by oral administration of defined Escherichia coli strains. II. Influencing the biotope by means of geographically unrelated Escherichia coli strains.

An effective increase in the rate of colonization can be accomplished, in analogy with the pathogenetic mechanism of what is known as travelers' disease, through the administration of geographically unrelated strains. As compared to Escherichia coli strains isolated in the GDR, metabolic drift-optimized and Ethiopian strains showed an increase from 20 to 50%. It was not, however, possible to maintain a greater than or equal to 50% share in the population of Enterobacteriaceae over a period of more than up to three days. Immunologic mechanisms are considered to be responsible for this.

Administration, Oral↗
PubMed1986

[Somatic antigens of Shigella and Escherichia coli. Determination of the structure of O-specific polysaccharide from Shigella boydii type 12 and its serological properties compared with the O-specific polysaccharide from Escherichia coli].

The structure of the O-specific polysaccharide of the somatic antigen (lipopolysaccharide) of Shigella boydii, type 12, was established by 1H- and 13C-NMR, methylation analysis and partial acid hydrolysis methods. The polysaccharide consists of pentasaccharide repeating units of the following structure: (formula; see text) The amount of O-acetyl groups was far less than stoichiometric, only about 2 for 3-4 repeating units. Nevertheless, the results of serological studies revealed 3-O-acetyl-alpha-L-rhamnose residue to be the major immunodominant group. In spite of the presence of similar trisaccharide fragments, the lipopolysaccharide and polysaccharide from Shigella boydii type 12 gave no crossreaction with lipopolysaccharide and polysaccharide from Escherichia coli 07. The possible reasons of the absence of serological relatedness between the Sh. boydii, type 12, and E. coli 07 cells were discussed.

Antigens, Bacterial↗
PubMed1989

The prevalence of verocytotoxin-producing Escherichia coli and antimicrobial resistance patterns of nonverocytotoxin-producing Escherichia coli and Salmonella in Ontario broiler chickens.

The prevalence of verocytotoxin-producing Escherichia coli and Salmonella in Ontario broiler chickens was determined by culturing cloacal samples from 500 individual birds selected from 50 poultry farms. Resistance to antimicrobials was determined for each of the isolates. In addition, abattoir and farm-level management data were obtained to evaluate variables that may be considered risk factors for infection. The variables selected included: Percentage of birds condemned at slaughter, percentage of birds dead-on-arrival, bird weight, truck number, farm size, hatchery source, litter source and type, feed source, mortality levels, type of water drinker, water sanitization, down time, barn clean out and history of antibiotic treatment. None of the cloacal samples revealed the presence of verocytotoxin-producing E. coli, though 19/500 (3.8%) contained Salmonella organisms. Nine different Salmonella serotypes were isolated; the most common being S. hadar, S. heidelberg and S. mbandaka. Resistance to tetracycline and streptomycin was common among Salmonella (63%) and E. coli (25.2%) isolates. Resistance to two or more antimicrobials occurred in 420/500 (84%) of the E. coli isolates. No statistically significant associations between abattoir or farm-level management variables and the Salmonella-status of farms were demonstrated.

Abattoirs↗
PubMed1988

Effects of an orally administered live Escherichia coli pilus vaccine on duration of lacteal immunity to enterotoxigenic Escherichia coli in swine.

Primigravid swine were vaccinated orally with a live enterotoxigenic Escherichia coli (ETEC) strain that produces pilus antigen K99. The titers of K99 antibody in colostrum and milk of vaccinates remained higher than those of nonvaccinated controls through the first lactation after vaccination (4 weeks). Some control swine had low titers of K99 antibody in colostrum or developed low titers of K99 antibody in milk during lactation. Lacteal K99 antibody titers of vaccinates dropped to control levels during the second lactation, 6 months after vaccination. Pigs suckling vaccinates and controls were equally susceptible to challenge exposure to K99+ ETEC during the second lactation. Orally vaccinated swine given a parenteral booster vaccination (with killed K99+ ETEC) during their second gestation had K99 antibody in milk through their second lactation. During the second lactation, these orally vaccinated parenterally revaccinated swine had higher titers of K99 antibody in postcolostral milk than did nonvaccinated controls, controls given only the parenteral booster injection, or controls vaccinated parenterally during both gestations.

Administration, Oral↗
PubMed1987

Interactions of the bacteriophage T4 gene 55 product with Escherichia coli RNA polymerase. Competition with Escherichia coli sigma 70 and release from late T4 transcription complexes following initiation.

The bacteriophage T4 gene 55 protein endows Escherichia coli RNA polymerase core with the ability to recognize T4 late promoters. In these experiments, we show that T4 gene product (gp) 55, like the major E. coli RNA polymerase initiation subunit sigma 70, is released from elongating transcription complexes and is thus capable of cycling among molecules of RNA polymerase core. We also show that, paradoxically, sigma 70 is able to displace T4 gp55 from its site of binding to E. coli RNA polymerase core. After T4 infection, the core enzyme is ADP-ribosylated in each alpha subunit, and a T4-coded 11.4-kDa protein (rpbA) binds tightly to it; these modifications do not save gp55 from displacement by sigma 70. However, open T4 late promoter complexes, containing gp55, are resistant to attack by sigma 70.

Adenosine Diphosphate Ribose↗
PubMed1977

Characterization of Escherichia coli serogroups causing meningitis, sepsis and enteritis. II. Classification of Escherichia coli O78 strains by phage sensitivity, colicin type and antibiotic resistance.

Escherichia coli O78: K80 strains isolated from an outbreak of meningitis, sepsis and enteritis in infants, were compared with O78: K80 strains from sporadic cases of enteritis, healthy carriers and animals. The strains were uniform in antigenic structure and phage pattern but differed in colicinogenicity. The epidemic strains and calf-pathogenic cultures produced colicin V, the remaining isolates were characterized by other types of colicin or were not colicinogenic. Col V+ strains multiplied in the mouse peritoneal cavity more readily and killed the animals at significantly lower doses than did col V- strains. One half of antibiotic resistant O78: K80 strains carried R factor. The spread of R factor could be followed by phage restriction experiments.

Animals↗
PubMed1986

Contrasting effects of Escherichia coli single-stranded DNA binding protein on synthesis by T7 DNA polymerase and Escherichia coli DNA polymerase I (large fragment). Evidence that binding protein inhibits trans-lesion synthesis by polymerase I.

The effect of Escherichia coli single-stranded DNA binding protein (SSB) on DNA synthesis by T7 DNA polymerase and E. coli DNA polymerase I (large fragment) using native or aminofluorene-modified M13 templates was evaluated by in vitro DNA synthesis assays and polyacrylamide gel electrophoresis analysis. The two polymerase enzymes displayed differential responses to the addition of SSB. T7 DNA polymerase, a enzyme required for the replication of the T7 chromosome, was stimulated by the addition of SSB whether native or modified templates were used. On the other hand, E. coli DNA polymerase I was slightly stimulated by the addition of SSB to the native template but substantially inhibited on modified templates. This result suggests that DNA polymerase I may be able to synthesize past an aminofluorene adduct but that the presence of SSB inhibited this trans-lesion synthesis. Polyacrylamide gels of the products of DNA synthesis by polymerase I supported this inference since SSB caused a substantial increase in the accumulation of shorter DNA chains induced by blockage at the aminofluorene adduct sites.

DNA Polymerase I↗
PubMed1977

[Intergeneric conjugational hybridization of Escherichia coli and Salmonella typhimurium. 1. Obtaining a salmonella hybrid possessing greater recipient activity in crosses with Escherichia coli].

Intergeneric hybrids were selected from mating HfrH Escherichia coli with F- Salmonella typhimurium. The hybrid obtained from E. coli leu+ and pro+ genes possessed the increased recipient ability in the mating with E. coli HfrR1 (O--ilv--metE--ara). This hybrid lacked the ability to restrict the phage P1 DNA propagated on E. coli K-12. The replacement of mutated uvrA gene of Salmonella for uvrA+ gene of E. coli restore uvr+ phenotype of Salmonella mutant.

Coliphages↗
PubMed1977

[Intergeneric conjugational crossing of Escherichia coli with Salmonella typhimurium. II. Transfer of a polA1 mutation from Escherichia coli to Salmonella typhimurium and its phenotypic expression in the salmonella genome].

The Escherichia coli structural gene for DNA polymerase I was inserted into Salmonella typhimurium chromosome by conjugal transfer. The genetic analysis of P1-mediated transduction of obtained hybrid showed that polA gene is located in it between metE and rha loci and is cotransduced with metE (about 50%) and rha (12%). The phenotypic properties of polA1 hybrid E. coliXS. typhimurium concerning UV-MMS-NG and gamma-ray sensitivity are similar to the polA1 mutants of E. coli.

Conjugation, Genetic↗
PubMed1987

Expression of rat intestinal fatty acid-binding protein in Escherichia coli. Purification and comparison of ligand binding characteristics with that of Escherichia coli-derived rat liver fatty acid-binding protein.

Rat intestinal fatty acid-binding protein (I-FABP) is an abundant, 15,124-Da polypeptide found in the cytosol of small intestinal epithelial cells (enterocytes). It is homologous to rat liver fatty acid-binding protein (L-FABP), a 14,273-Da cytosolic protein which is found in enterocytes as well as hepatocytes. It is unclear why the small intestinal epithelium contains two abundant fatty acid-binding proteins. A systematic comparative analysis of the ligand binding characteristics of the two FABPs has not been reported. To undertake such a study we expressed the coding region of a full length I-FABP cDNA in Escherichia coli and purified large quantities of the protein. We also purified rat L-FABP from a similar, previously described expression system (Lowe, J. B., Strauss, A. W., and Gordon, J. I. (1984) J. Biol. Chem. 259, 12696-12704). Analysis of fatty acids associated with each of the homogeneous E. coli-derived FABPs suggested that the two proteins differed in their ligand binding specificity and capacity. All of the fatty acids associated with I-FABP were saturated while 30% of the E. coli fatty acids bound to L-FABP were unsaturated (16:1, 18:1, 18:2). We directly analyzed the ability of I- and L-FABP to bind fatty acids of different chain length and degree of saturation using a hydroxyalkoxypropyl dextran-based assay. Scatchard analysis revealed that each mole of L-FABP can bind up to 2 mol of long chain fatty acid while each mole of I-FABP can bind only 1 mole of fatty acid. L-FABP exhibited a relatively higher affinity for unsaturated fatty acids (oleate, arachidonate) than for saturated fatty acid (palmitate). By contrast, we were not able to detect a significant difference in the affinity of I-FABP for palmitate, oleate, and arachidonate. Neither protein exhibited any appreciable affinity for fatty acids whose chain length was less than C16. The observed differences in ligand affinities and capacities suggest that these proteins may have distinct roles in metabolism and/or compartmentalization of fatty acids within enterocytes.

Amino Acid Sequence↗
PubMed1983

Limited proteolysis studies on the Escherichia coli single-stranded DNA binding protein. Evidence for a functionally homologous domain in both the Escherichia coli and T4 DNA binding proteins.

Limited proteolysis can be used to remove either 42 or 62 amino acids at the COOH terminus of the 18,873-dalton Escherichia coli single-stranded DNA binding protein (SSB). Since poly(dT), but not d(pT)16, increases the rate of this reaction, it appears that cooperative SSB binding to single-stranded DNA (ssDNA) is associated with a conformational change that increases the exposure of the COOH terminus to proteolysis. As a result of this DNA-induced conformational change, we presume that the COOH-terminal region of SSB will become more accessible for interacting with other proteins that utilize the SSB:ssDNA complex as a substrate and that are involved in E. coli DNA replication, repair, and recombination. Removal of this COOH-terminal domain from SSB results in a stronger helix-destabilizing protein which suggests this region may be important for controlling the ability of SSB to denature double-stranded DNA. Since similar results have previously been reported for the bacteriophage T4 gene 32 protein (Williams, K.R., and Konigsberg, W. (1978) J. Biol. Chem. 253, 2463-2470; Hosoda, J., and Moise, H. (1978) J. Biol. Chem. 253, 7547-7555), the acidic, COOH-terminal domains of these two single-stranded DNA binding proteins may be functionally homologous. Preliminary evidence is cited that suggests other prokaryotic and eukaryotic DNA binding proteins may contain similar functional domains essential for controlling their ability to invade double helical DNA.

Amino Acid Sequence↗
PubMed1983

The large subunit of the fatty acid oxidation complex from Escherichia coli is a multifunctional polypeptide. Evidence for the existence of a fatty acid oxidation operon (fad AB) in Escherichia coli.

The subunit locations of the five enzymes associated with the fatty acid oxidation complex from Escherichia coli were studied by immunotitration and chemical modification. Antibodies raised against the purified complex caused the parallel inhibitions of enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase, while slightly stimulating 3-ketoacyl-CoA thiolase. All five component enzymes of the complex were inactivated by treatment with iodoacetamide. The inactivation of 3-ketoacyl-CoA thiolase was rapid, whereas the four other enzymes were inactivated at much slower, but almost equal rates. All enzymes except for 3-ketoacyl-CoA thiolase were protected against this inactivation by either NADH or crotonyl-CoA. The reaction of iodo[1-14C]acetamide with the complex in the presence and absence of NADH resulted in the differential labeling of the large subunit only. These observations together with published results (Pawar, S., and Schulz, H. (1981) J. Biol. Chem. 256, 3894-3899) lead to the suggestion that enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, cis-delta 3-trans-delta 2-enoyl-CoA isomerase, and 3-hydroxyacyl-CoA epimerase are located on the 78,000-Da subunit, whereas 3-ketoacyl-CoA thiolase is associated with the 42,000-Da subunit. Additionally, this study provides further evidence for the existence of a fatty acid oxidation (fad AB) operon that codes for the multienzyme complex of fatty acid oxidation and that is located at 85 min on the E. coli chromosome.

3-Hydroxyacyl CoA Dehydrogenases↗