scholarly journals φYeO3-12 phage tail fiber Gp17 as a promising high specific tool for recognition of Yersinia enterocolitica pathogenic serotype O:3

AMB Express ◽  
2022 ◽  
Vol 12 (1) ◽  
Author(s):  
Karolina Filik ◽  
Bożena Szermer-Olearnik ◽  
Joanna Niedziółka-Jönson ◽  
Ewa Roźniecka ◽  
Jarosław Ciekot ◽  
...  
Keyword(s):  
Yersinia Enterocolitica ◽  
Yersinia Pseudotuberculosis ◽  
Specific Interaction ◽  
Elisa Test ◽  
Diagnostic Process ◽  
Growth Media ◽  
Tail Fiber ◽  
Serotype O ◽  
Promising Tool ◽  
Contaminated Food

AbstractYersiniosis is an infectious zoonotic disease caused by two enteropathogenic species of Gram-negative genus Yersinia: Yersinia enterocolitica and Yersinia pseudotuberculosis. Pigs and other wild and domestic animals are reservoirs for these bacteria. Infection is usually spread to humans by ingestion of contaminated food. Yersiniosis is considered a rare disease, but recent studies indicate that it is overlooked in the diagnostic process therefore the infections with this bacterium are not often identified. Reliable diagnosis of Yersiniosis by culturing is difficult due to the slow growth of the bacteria easily overgrown by other more rapidly growing microbes unless selec-tive growth media is used. Phage adhesins recognizing bacteria in a specific manner can be an excellent diagnostic tool, es-pecially in the diagnosis of pathogens difficult for culturing. In this study, it was shown that Gp17, the tail fiber protein (TFP) of phage φYeO3-12, specifically recognizes only the pathogenic Yersinia enterocolitica serotype O:3 (YeO:3) bacteria. The ELISA test used in this work confirmed the specific interaction of this protein with YeO:3 and demonstrated a promising tool for developing the pathogen recognition method based on phage adhesins.

scholarly journals New Insights on the Feature and Function of Tail Tubular Protein B and Tail Fiber Protein of the Lytic Bacteriophage φYeO3-12 Specific for Yersinia enterocolitica Serotype O:3

Molecules ◽  
2020 ◽  
Vol 25 (19) ◽  
pp. 4392
Author(s):  
Anna Pyra ◽  
Karolina Filik ◽  
Bożena Szermer-Olearnik ◽  
Anna Czarny ◽  
Ewa Brzozowska
Keyword(s):  
Yersinia Enterocolitica ◽  
3D Structure ◽  
Bioinformatic Analysis ◽  
Thermal Unfolding ◽  
Tail Fiber ◽  
Lytic Bacteriophage ◽  
Serotype O ◽  
Phage T7 ◽  
Domain Protein ◽  
Aggregation Temperature

For the first time, we are introducing TTPBgp12 and TFPgp17 as new members of the tail tubular proteins B (TTPB) and tail fiber proteins (TFP) family, respectively. These proteins originate from Yersinia enterocolitica phage φYeO3-12. It was originally thought that these were structural proteins. However, our results show that they also inhibit bacterial growth and biofilm formation. According to the bioinformatic analysis, TTPBgp12 is functionally and structurally similar to the TTP of Enterobacteria phage T7 and adopts a β-structure. TFPgp17 contains an intramolecular chaperone domain at its C-terminal end. The N-terminus of TFPgp17 is similar to other representatives of the TFP family. Interestingly, the predicted 3D structure of TFPgp17 is similar to other bacterial S-layer proteins. Based on the thermal unfolding experiment, TTPBgp12 seems to be a two-domain protein that aggregates in the presence of sugars such as maltose and N-acetylglucosamine (GlcNAc). These sugars cause two unfolding events to transition into one global event. TFPgp17 is a one-domain protein. Maltose and GlcNAc decrease the aggregation temperature of TFPgp17, while the presence of N-acetylgalactosamine (GalNAc) increases the temperature of its aggregation. The thermal unfolding analysis of the concentration gradient of TTPBgp12 and TFPgp17 indicates that with decreasing concentrations, both proteins increase in stability. However, a decrease in the protein concentration also causes an increase in its aggregation, for both TTPBgp12 and TFPgp17.

scholarly journals Yersinia enterocolitica : Biochemical, Serological, and Gas-Liquid Chromatographic Characterization of Rhamnose-, Raffinose-, Melibiose-, and Citrate-Utilizing Strains

1977 ◽  
Vol 6 (5) ◽  
pp. 461-468
Author(s):  
Brent Chester ◽  
Guenther Stotzky ◽  
Edward J. Bottone ◽  
Moises S. Malowany ◽  
Jona Allerhand
Keyword(s):  
Yersinia Enterocolitica ◽  
Yersinia Pseudotuberculosis ◽  
Gas Liquid Chromatography ◽  
Susceptibility Data ◽  
Serotype O ◽  
Chromatographic Characterization ◽  
O 15 ◽  
Liquid Chromatographic ◽  
Lactic Acids

Thirteen atypical Yersinia enterocolitica isolates, all fermenting rhamnose, raffinose, and melibiose and utilizing sodium citrate within 24 to 48 h at 22°C ( Y.e.rh +), were examined biochemically-serologically, and by gas-liquid chromatography. These data, as well as cultural, biochemical, and antibiotic susceptibility data gathered from two previous studies involving (i) these same atypical Y.e.rh + isolates, (ii) Y. enterocolitica serotypes O:1 through O:15 (rhamnose, raffinose, and citrate negative [ Y.e.rh −]), (iii) Y. enterocolitica serotype O:16 (rhamnose positive but raffinose and citrate negative), and (iv) Yersinia pseudotuberculosis serogroups I through V were statistically compared. Both preand postabsorption agglutination studies demonstrated the serological distinctiveness of Y.e.rh + from Y.e.rh − and Y. pseudotuberculosis . At the same time, three immunological groups among the 13 Y.e.rh + strains were seen; 8 corresponded to Y. enterocolitica serotype O:17; 1 to Y. enterocolitica serotype O:16; and the remaining four were nontypable in antisera against known Y. enterocolitica antigen types. Each of the three Yersinia groups tested chromatographically produced acetic and lactic acids. Both Y.e.rh − and Y.e.rh + formed propionic acid, but only Y.e.rh + produced detectable amounts of succinic acid. Based on 49 variables, statistical analysis of the three Yersinia groups studied placed each of the Y.e.rh + strains in a homogeneous group separate from both Y.e.rh − and Y. pseudotuberculosis . These data, coupled with deoxyribonucleic acid homology studies of Brenner and co-workers (D. J. Brenner, A. G. Steigerwalt, D. F. Falcao, R. E. Weaver, and G. R. Fanning, Int. J. Syst. Bacteriol. 26 :180-194, 1976), support the distinctiveness of Y.e.rh + from typical Y. enterocolitica and Y. pseudotuberculosis .

scholarly journals Novel diagnostic ELISA test for discrimination between infections with Yersinia enterocolitica and Yersinia pseudotuberculosis

2018 ◽  
Vol 37 (12) ◽  
pp. 2301-2306 ◽  
Author(s):  
Tomasz Wielkoszynski ◽  
Aliyeh Moghaddam ◽  
Assar Bäckman ◽  
Jessica Broden ◽  
Rafał Piotrowski ◽  
...  
Keyword(s):  
Yersinia Enterocolitica ◽  
Yersinia Pseudotuberculosis ◽  
Elisa Test

scholarly journals Plague virulence antigens from Yersinia enterocolitica

1980 ◽  
Vol 28 (2) ◽  
pp. 638-640 ◽  
Author(s):  
P B Carter ◽  
R J Zahorchak ◽  
R R Brubaker
Keyword(s):  
Yersinia Pestis ◽  
Yersinia Enterocolitica ◽  
Yersinia Pseudotuberculosis ◽  
Serotype O

The virulence of Yersinia enterocolitica, biotype 2, serotype O:8, in mice is related to its ability to produce plague V and W antigens. V and W antigens in Y. enterocolitica are shown to be immunologically identical to the previously described V and W antigens of Yersinia pestis and Yersinia pseudotuberculosis.

Other Yersinia infections: yersiniosis

2010 ◽  
pp. 776-777
Author(s):  
Michael B. Prentice
Keyword(s):  
Abdominal Pain ◽  
Yersinia Enterocolitica ◽  
Erythema Multiforme ◽  
Reactive Arthritis ◽  
Yersinia Pseudotuberculosis ◽  
Systemic Infection ◽  
Late Complications ◽  
Gram Negative ◽  
Contaminated Food ◽  
Gram Negative Organisms

Yersiniosis is caused by the enteropathogenic Gram-negative organisms Yersinia enterocolitica and Yersinia pseudotuberculosis, which are worldwide zoonotic pathogens. Disease is acquired by consumption of contaminated food or water and is commonest in childhood, and in colder climates. Presentation is with diarrhoea, fever and abdominal pain, which may mimic appendicitis. Late complications include reactive arthritis, erythema nodosum, and erythema multiforme. Systemic infection is more likely with ...

scholarly journals Pathogenic Yersinia enterocolitica Strains Increase the Outer Membrane Permeability in Response to Environmental Stimuli by Modulating Lipopolysaccharide Fluidity and Lipid A Structure

2003 ◽  
Vol 71 (4) ◽  
pp. 2014-2021 ◽  
Author(s):  
J. A. Bengoechea ◽  
K. Brandenburg ◽  
M. D. Arraiza ◽  
U. Seydel ◽  
M. Skurnik ◽  
...  
Keyword(s):  
Membrane Permeability ◽  
Outer Membrane ◽  
Yersinia Enterocolitica ◽  
Lipid A ◽  
Yersinia Pseudotuberculosis ◽  
Acyl Chain ◽  
Growth Conditions ◽  
Virulence Plasmid ◽  
Serotype O ◽  
Outer Membrane Permeability

ABSTRACT Pathogenic biotypes of Yersinia enterocolitica (serotypes O:3, O:8, O:9, and O:13), but not environmental biotypes (serotypes O:5, O:6, O:7,8, and O:7,8,13,19), increased their permeability to hydrophobic probes when they were grown at pH 5.5 or in EGTA-supplemented (Ca2+-restricted) media at 37°C. A similar observation was also made when representative strains of serotypes O:8 and O:5 were tested after brief contact with human monocytes. The increase in permeability was independent of the virulence plasmid. The role of lipopolysaccharide (LPS) in this phenomenon was examined by using Y. enterocolitica serotype O:8. LPS aggregates of bacteria grown in acidic or EGTA-supplemented broth took up more N-phenylnaphthylamine than LPS aggregates of bacteria grown in standard broth and also showed a marked increase in acyl chain fluidity which correlated with permeability, as determined by measurements obtained in the presence of hydrophobic dyes. No significant changes in O-antigen polymerization were observed, but lipid A acylation changed depending on the growth conditions. In standard medium at 37°C, there were hexa-, penta-, and tetraacyl lipid A forms, and the pentaacyl form was dominant. The amount of tetraacyl lipid A increased in EGTA-supplemented and acidic media, and hexaacyl lipid A almost disappeared under the latter conditions. Our results suggest that pathogenic Y. enterocolitica strains modulate lipid A acylation coordinately with expression of virulence proteins, thus reducing LPS packing and increasing outer membrane permeability. The changes in permeability, LPS acyl chain fluidity, and lipid A acylation in pathogenic Y. enterocolitica strains approximate the characteristics in Yersinia pseudotuberculosis and Yersinia pestis and suggest that there is a common outer membrane pattern associated with pathogenicity.

Arthritis in children as a result of a previous infection caused by Yersinia enterocolitica and Yersinia pseudotuberculosis

2008 ◽  
Vol 63 (2) ◽  
pp. 88-92
Author(s):  
Michał Szczyrek ◽  
Anna Mełges ◽  
Alina Olender ◽  
Konrad Jarząbek ◽  
Jacek Postępski
Keyword(s):  
Yersinia Enterocolitica ◽  
Yersinia Pseudotuberculosis ◽  
Previous Infection

scholarly journals T4-like Bacteriophages Isolated from Pig Stools Infect Yersinia pseudotuberculosis and Yersinia pestis Using LPS and OmpF as Receptors

Viruses ◽  
2021 ◽  
Vol 13 (2) ◽  
pp. 296
Author(s):  
Mabruka Salem ◽  
Maria I. Pajunen ◽  
Jin Woo Jun ◽  
Mikael Skurnik
Keyword(s):  
Yersinia Pseudotuberculosis ◽  
Host Recognition ◽  
Tail Fiber ◽  
Long Tail ◽  
Phage T4 ◽  
One Step ◽  
In Trans ◽  
Step Growth ◽  
Resistant Strains ◽  
Salmonella Phage

The Yersinia bacteriophages fPS-2, fPS-65, and fPS-90, isolated from pig stools, have long contractile tails and elongated heads, and they belong to genus Tequatroviruses in the order Caudovirales. The phages exhibited relatively wide host ranges among Yersinia pseudotuberculosis and related species. One-step growth curve experiments revealed that the phages have latent periods of 50–80 min with burst sizes of 44–65 virions per infected cell. The phage genomes consist of circularly permuted dsDNA of 169,060, 167,058, and 167,132 bp in size, respectively, with a G + C content 35.3%. The number of predicted genes range from 267 to 271. The phage genomes are 84–92% identical to each other and ca 85% identical to phage T4. The phage receptors were identified by whole genome sequencing of spontaneous phage-resistant mutants. The phage-resistant strains had mutations in the ompF, galU, hldD, or hldE genes. OmpF is a porin, and the other genes encode lipopolysaccharide (LPS) biosynthetic enzymes. The ompF, galU, and hldE mutants were successfully complemented in trans with respective wild-type genes. The host recognition was assigned to long tail fiber tip protein Gp38, analogous to that of T-even phages such as Salmonella phage S16, specifically to the distal β-helices connecting loops.

scholarly journals Yersiniosis in New Zealand

Pathogens ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 191
Author(s):  
Lucia Rivas ◽  
Hugo Strydom ◽  
Shevaun Paine ◽  
Jing Wang ◽  
Jackie Wright
Keyword(s):  
New Zealand ◽  
One Health ◽  
Yersinia Pseudotuberculosis ◽  
Developed Countries ◽  
Farm Animals ◽  
Pathogenic Potential ◽  
Targeted Interventions ◽  
Serotype O ◽  
Large Outbreak ◽  
Insufficient Sensitivity

The rate of yersiniosis in New Zealand (NZ) is high compared with other developed countries, and rates have been increasing over recent years. Typically, >99% of human cases in NZ are attributed to Yersinia enterocolitica (YE), although in 2014, a large outbreak of 220 cases was caused by Yersinia pseudotuberculosis. Up until 2012, the most common NZ strain was YE biotype 4. The emergent strain since this time is YE biotype 2/3 serotype O:9. The pathogenic potential of some YE biotypes remains unclear. Most human cases of yersiniosis are considered sporadic without an identifiable source. Key restrictions in previous investigations included insufficient sensitivity for the isolation of Yersinia spp. from foods, although foodborne transmission is the most likely route of infection. In NZ, YE has been isolated from a variety of sick and healthy domestic and farm animals but the pathways from zoonotic reservoir to human remain unproven. Whole-genome sequencing provides unprecedented discriminatory power for typing Yersinia and is now being applied to NZ epidemiological investigations. A “One-Health” approach is necessary to elucidate the routes of transmission of Yersinia and consequently inform targeted interventions for the prevention and management of yersiniosis in NZ

scholarly journals Yersiniophage ϕR1-37 is a tailed bacteriophage having a 270 kb DNA genome with thymidine replaced by deoxyuridine

Microbiology ◽  
2005 ◽  
Vol 151 (12) ◽  
pp. 4093-4102 ◽  
Author(s):  
Saija Kiljunen ◽  
Kristo Hakala ◽  
Elise Pinta ◽  
Suvi Huttunen ◽  
Patrycja Pluta ◽  
...  
Keyword(s):  
Yersinia Pseudotuberculosis ◽  
Burst Size ◽  
Outer Core ◽  
International Committee ◽  
Amino Acid Sequences ◽  
Structural Proteins ◽  
Virulence Plasmid ◽  
O Antigen ◽  
Serotype O ◽  
Phage Receptor

Bacteriophage ϕR1-37 was isolated based on its ability to infect strain YeO3-R1, a virulence-plasmid-cured O antigen-negative derivative of Yersinia enterocolitica serotype O : 3. In this study, the phage receptor was found to be a structure in the outer core hexasaccharide of Y. enterocolitica O : 3 LPS. The phage receptor was present in the outer core of strains of many other Y. enterocolitica serotypes, but also in some Yersinia intermedia strains. Surprisingly, the receptor structure resided in the O antigen of Yersinia pseudotuberculosis O : 9. Electron microscopy demonstrated that ϕR1-37 particles have an icosahedral head of 88 nm, a short neck of 10 nm, a long contractile tail of 236 nm, and tail fibres of at least 86 nm. This implies that the phage belongs to the order Caudovirales and the family Myoviridae in the ICTV (International Committee for Taxonomy of Viruses) classification. ϕR1-37 was found to have a lytic life cycle, with eclipse and latent periods of 40 and 50 min, respectively, and a burst size of ∼80 p.f.u. per infected cell. Restriction digestions and PFGE showed that the ϕR1-37 genome was dsDNA and ∼270 kb in size. Enzymically hydrolysed DNA was subjected to HPLC-MS/MS analysis, which demonstrated that the ϕR1-37 genome is composed of DNA in which thymidine (T) is >99 % replaced by deoxyuridine (dU). The only organisms known to have similar DNA are the Bacillus subtilis-specific bacteriophages PBS1 and PBS2. N-terminal amino acid sequences of four major structural proteins did not show any similarity to (viral) protein sequences in databases, indicating that close relatives of ϕR1-37 have not yet been characterized. Genes for two of the structural proteins, p24 and p46, were identified from the partially sequenced ϕR1-37 genome.

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