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Journal of Clinical Microbiology Oct 1979Yersinia enterocolitica and related Yersinia species share many temperature-dependent biological attributes. The present report documents temperature-dependent...
Yersinia enterocolitica and related Yersinia species share many temperature-dependent biological attributes. The present report documents temperature-dependent production of a bacteriocin-like substance only among Yersinia strains which ferment L-rhamnose, raffinose, and melibiose and which have been tentatively designed Y. intermedia. When tested by the "lawn-spotting" technique at 25 and 37 degrees C, 7 of 15 Y. intermedia strains produced a bacteriocin only at 25 degrees C with a uniform spectrum of activity against 2 strains of Y. enterocolitica, 1 rhamnose-positive, raffinose-negative, melibiose-negative strain tentatively designated Y. frederiksenii, 8 Y. intermedia, and 3 sucrose- and acetylmethylcarbinol-negative yersinial isolates tested. Bacteriocin-like activity was not detected among the Y. enterocolitica, Y. frederiksenii, or sucrose-negative yersinial strains tested. The exclusive activity of the Y. intermedia antibacterial substance only against yersiniae and not against other representative Enterobacteriaceae tested supports the placement of these microorganisms within the genus Yersinia and further establishes the singularity of Y. intermedia.
Topics: Bacteriocins; Drug Resistance, Microbial; Species Specificity; Temperature; Yersinia
PubMed: 528679
DOI: 10.1128/jcm.10.4.433-436.1979 -
Genome Announcements Aug 2017like strains are usually understudied. In this work, we reported the draft genome sequences of two , two , and two strains isolated from humans, animals, food, and the...
like strains are usually understudied. In this work, we reported the draft genome sequences of two , two , and two strains isolated from humans, animals, food, and the environment in Brazil. These draft genomes will provide better molecular characterizations of these species.
PubMed: 28798182
DOI: 10.1128/genomeA.00780-17 -
Antonie Van Leeuwenhoek Jun 2024Yersinia is an important genus comprising foodborne, zoonotic and pathogenic bacteria. On the other hand, species of the so-called group Yersinia enterocolitica-like are...
Yersinia is an important genus comprising foodborne, zoonotic and pathogenic bacteria. On the other hand, species of the so-called group Yersinia enterocolitica-like are understudied and mostly characterized as non-pathogenic, despite of some reports of human infections. The present study aimed to provide genomic insights of Yersinia frederiksenii (YF), Yersinia intermedia (YI) and Yersinia kristensenii (YK) isolated worldwide. A total of 22 YF, 20 YI and 14 YK genomes were searched for antimicrobial resistance genes, plasmids, prophages, and virulence factors. Their phylogenomic relatedness was analyzed by Gegenees and core-genome multi-locus sequence typing. Beta-lactam resistance gene bla and five plasmids replicons (pYE854, ColRNAI, ColE10, Col(pHAD28) and IncN3) were detected in less than five genomes. A total of 59 prophages, 106 virulence markers of the Yersinia genus, associated to adherence, antiphagocytosis, exoenzymes, invasion, iron uptake, proteases, secretion systems and the O-antigen, and virulence factors associated to other 20 bacterial genera were detected. Phylogenomic analysis revealed high inter-species distinction and four highly diverse YF clusters. In conclusion, the results obtained through the analyses of YF, YI and YK genomes suggest the virulence potential of these strains due to the broad diversity and high frequency of prophages and virulence factors found. Phylogenetic analyses were able to correctly distinguish these closely related species and show the presence of different genetic subgroups. These data contributed for a better understanding of YF, YI and YK virulence-associated features and global genetic diversity, and reinforced the need for better characterization of these Y. enterocolitica-like species considered non-pathogenic.
Topics: Yersinia; Phylogeny; Genome, Bacterial; Virulence Factors; Brazil; Yersinia Infections; Humans; Genomics; Prophages; Plasmids; Multilocus Sequence Typing; Virulence
PubMed: 38829455
DOI: 10.1007/s10482-024-01984-8 -
Folia Microbiologica 1986One strain of Yersinia enterocolitica and one strain of Y. intermedia were grown in peptone water at 25 or 37 degrees C, or in ground water at 15 degrees C. Similar...
One strain of Yersinia enterocolitica and one strain of Y. intermedia were grown in peptone water at 25 or 37 degrees C, or in ground water at 15 degrees C. Similar growth rates were observed when these strains were cultivated separately in the same media and at the same temperature. Mixed cultures at 37 degrees C displayed equivalent growth rates. In contrast, mixed cultures incubated at 15 or 25 degrees C were regularly unfavourable to Y. enterocolitica, whereas they did not modify the growth of Y. intermedia. A bacteriophage active on Y. enterocolitica and not on Y. intermedia was characterized from the filtrate of mixed cultures at low temperatures. This phage produced by the lysogenic Y. intermedia strain might be a potential factor responsible for the inhibition of Y. enterocolitica, since no additional antibacterial factor or nutritional competition between Y. intermedia and Y. enterocolitica were found in the mixed cultures.
Topics: Antibiosis; Bacteriophages; Culture Media; Temperature; Water Microbiology; Yersinia; Yersinia enterocolitica
PubMed: 3710318
DOI: 10.1007/BF02926836 -
Recent Patents on Food, Nutrition &... 2019Phytases are enzymes capable of degrading phytic acid and used in animal feed supplementation in order to improve digestibility through the release of minerals such as...
BACKGROUND
Phytases are enzymes capable of degrading phytic acid and used in animal feed supplementation in order to improve digestibility through the release of minerals such as phosphorus.
OBJECTIVE
The main goal of this study was to express and characterize a Yersinia intermedia phytase expressed in Escherichia coli cells.
METHODS
The Y. intermedia phytase gene was synthesized and overexpressed in Escherichia coli cells. The phytase recombinante (rPHY) was purified to homogeneity using a Ni-NTA column. The biochemical and biophysical properties of the rPHY were measured in order to fully characterize the recombinant enzyme. The following patents database were consulted: Espacenet, USPTO, LATIPAT, Patent Scope, WIPO and Google Patents.
RESULTS
The results showed that the rPHY is active at 37-40ºC and presented an optimal pH and temperature of 8.0 and 40°C, respectively. The phytase rPHY was activated by Cu2+ ion and showed resistance to trypsin and pepsin, retaining 55% of the activity at the ratio of 0.02. Furthermore, the dissociation constant (Kd = 1.1150 ± 0.0087 mM), as estimated by a fluorescence binding assay, suggests a medium affinity of the enzyme with the substrate.
CONCLUSION
The results of this article can be considered as innovative and for this reason, they were protected by Intellectual Property Law in Brazil. Take together, the biochemical properties of the rPHY could be useful in future for its industrial application of this enzyme as an additive in the monogastric feed.
Topics: 6-Phytase; Escherichia coli; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Patents as Topic; Protein Conformation; Yersinia
PubMed: 30516117
DOI: 10.2174/2212798410666181205114153 -
Bioprocess and Biosystems Engineering Oct 2021Phytase is used in poultry diets to hydrolyze and release of phytate-bound phosphorus. Immobilization on nanomaterials optimizes enzyme's thermal stability and...
Phytase is used in poultry diets to hydrolyze and release of phytate-bound phosphorus. Immobilization on nanomaterials optimizes enzyme's thermal stability and reusability. This study aimed to immobilize the recombinant phytase from Yersinia intermedia on the surface of amino-multi-walled carbon nanotubes (amino-MWCNTs) by physical adsorption. For this, zeta potential measurement, FTIR spectroscopic analysis, scanning electron microscope (SEM), kinetic as well as thermodynamic parameters were used to characterize immobilized phytase on amino-MWCNTs. According to results, the optimum temperature of the immobilized phytase increased from 50 to 70 °C and also thermal and pH stability improved considerably. Moreover, immobilization led to an increase in the value of K and k from 0.13 to 0.33 mM and 2220 to 2776 s, respectively. In addition, the changes in activation energy of thermal inactivation (ΔE), the free energy of thermal inactivation (ΔG) and the enthalpy of thermal inactivation (ΔH) for immobilized phytase increased by +11.05, +24.7 and +11.4 kj/mole, respectively, while the value of the change in the entropy of thermal inactivation (ΔS) decreased by - 0.04 kj/mole.K. Overall, our results showed that adsorption immobilization of phytase on amino-MWCNTs increases thermal, pH and storage stability as well as some of kinetic parameters.
Topics: 6-Phytase; Adsorption; Enzyme Stability; Kinetics; Microscopy, Electron, Scanning; Nanotubes, Carbon; Recombinant Proteins; Spectroscopy, Fourier Transform Infrared; Temperature; Thermodynamics; Yersinia
PubMed: 34142205
DOI: 10.1007/s00449-021-02598-4 -
Journal of Clinical Microbiology Mar 1983Yersinia intermedia produces a temperature-dependent (25 degrees C) bactericidal substance that is active against other Yersinia species. Crude preparations of the...
Yersinia intermedia produces a temperature-dependent (25 degrees C) bactericidal substance that is active against other Yersinia species. Crude preparations of the inhibitory substance were inactivated by chymotrypsin, trypsin, pronase, and heating but were not affected by lipolytic enzymes, chloroform, or other organic solvents. These data suggest that the active molecule is a bacteriocin of a proteinaceous nature. The molecular weight of the bacteriocin was estimated to be greater than 14,000. Exposure of agar fragments containing the active component to a pH range of 3 to 11 did not affect bactericidal activity. Bactericidal activity against the Y. frederiksenii indicator strain was shown by simultaneous and deferred antagonism and by the associative culture technique. The liquor from cell-free macerated agar fragments and broth cultures, however, were devoid of antibacterial activity.
Topics: Bacteriocins; Hydrogen-Ion Concentration; Molecular Weight; Peptide Hydrolases; Yersinia
PubMed: 6341403
DOI: 10.1128/jcm.17.3.511-515.1983 -
Iranian Journal of Biotechnology Mar 2016Bacterial resistance to the commonly used antibacterial agents is an increasing challenge in the medicine, and a major problem for the health care systems; the control...
BACKGROUND
Bacterial resistance to the commonly used antibacterial agents is an increasing challenge in the medicine, and a major problem for the health care systems; the control of their spread is a constant challenge for the hospitals.
OBJECTIVES
In this study, we have investigated the antimicrobial activity of the Zinc Oxide nanoparticles against clinical sample; bacteria.
MATERIALS AND METHODS
Nanoparticle susceptibility constants and death kinetic were used to evaluate the antimicrobial characteristics of the Zinc Oxide (ZnO) against the bacteria. Antimicrobial tests were performed with 10 cfu.mL at baseline. At first, Minimum Inhibitory Concentration (MIC) of ZnO was determined and then nanoparticle suspension at one and two times of the MIC was used for death kinetic and susceptibility constant assay at 0 to 360 min treatment time.
RESULTS
ZnO nanoparticles with size ranging from 10 to 30 nm showed the highest susceptibility reaction against (Z=39.06 mL.μg). The process of death in ZnO suspension was assumed to follow the first-order kinetics and the survival ratio of bacteria decreased with the increasing treatment time. An increased concentration of the nanoparticle was seen to enhance the bactericidal action of the nanoparticle. Then we performed the best ratio of the nanoparticles on semi-sensitive and resistance antibiotic for the bacteria. However, based on experimental results, synergy of ZnO nanoparticles and Oxacilin was determined and showed a higher sensitivity compared to the ZnO nanoparticles alone.
CONCLUSIONS
The results of the present study illustrates that ZnO has a strong antimicrobial effect and could potentially be employed to aid the bacterial control. It could also improve- antibacterial effects in combination with the antibiotics.
PubMed: 28959316
DOI: 10.15171/ijb.1184 -
Environmental Science and Pollution... May 2022Heat- and pH-stable phytase efficiently hydrolyzes phytic acid. In this research, heat- and pH-stable mutant phytases, TR, LR, and TR/LR were generated by site-directed...
Heat- and pH-stable phytase efficiently hydrolyzes phytic acid. In this research, heat- and pH-stable mutant phytases, TR, LR, and TR/LR were generated by site-directed mutagenesis from Yersinia intermedia. After the induction and expression of recombinant wild-type and mutant phytases in E. coli BL21, the enzymes were purified using nickel sepharose affinity chromatography, and characterized kinetically and thermodynamically using spectroscopy methods. The mutants showed optimum activity at pH 5.15 and 55-61 °C. The catalytic efficiencies of TR, LR, TR/LR, and wild-type phytases were calculated to be 2941, 29346, 4906, and 6917 mmol/Ls, respectively. Moreover, after the incubation of TR, LR, wild-type, and TR/ LR phytases at 100 °C for 1 h, the enzymes retained 22, 5, 4, and 2% of their initial activities, respectively. In addition, TR, TR/LR, LR, and wild-type phytases retained 82, 44, 16 as well as 11% of their initial activities after 1 h at pH 5.15, respectively. Among these mutants, TR mutant showed 18% increase in thermal stability, 71% increase in pH stability, and +0.103 KJ/mole increase in ΔΔG, while the catalytic efficiency and ΔΔG value of LR mutant increased by 4 times and +0.0903 KJ/mole, respectively. Thus, the mutants have the potential to be used in feed industries to increase the bioavailability of minerals while decreasing soil and water pollution.
Topics: 6-Phytase; Enzyme Stability; Escherichia coli; Hydrogen-Ion Concentration; Yersinia
PubMed: 35029822
DOI: 10.1007/s11356-022-18578-4 -
Applied and Environmental Microbiology Jun 2006In this study, 231 strains of Yersinia enterocolitica, 25 strains of Y. intermedia, and 10 strains of Y. bercovieri from human and porcine sources (including reference...
Genotyping of human and porcine Yersinia enterocolitica, Yersinia intermedia, and Yersinia bercovieri strains from Switzerland by amplified fragment length polymorphism analysis.
In this study, 231 strains of Yersinia enterocolitica, 25 strains of Y. intermedia, and 10 strains of Y. bercovieri from human and porcine sources (including reference strains) were analyzed using amplified fragment length polymorphism (AFLP), a whole-genome fingerprinting method for subtyping bacterial isolates. AFLP typing distinguished the different Yersinia species examined. Representatives of Y. enterocolitica biotypes 1A, 1B, 2, 3, and 4 belonged to biotype-related AFLP clusters and were clearly distinguished from each other. Y. enterocolitica biotypes 2, 3, and 4 appeared to be more closely related to each other (83% similarity) than to biotypes 1A (11%) and 1B (47%). Biotype 1A strains exhibited the greatest genetic heterogeneity of the biotypes studied. The biotype 1A genotypes were distributed among four major clusters, each containing strains from both human and porcine sources, confirming the zoonotic potential of this organism. The AFLP technique is a valuable genotypic method for identification and typing of Y. enterocolitica and other Yersinia spp.
Topics: Animals; Chromosome Banding; Chromosomes, Bacterial; Genotype; Humans; Polymorphism, Genetic; Swine; Switzerland; Yersinia; Yersinia enterocolitica
PubMed: 16751516
DOI: 10.1128/AEM.01996-05