Characterization of SE‐P3, P16, P37, and P47 bacteriophages infecting <i>Salmonella</i> Enteritidis

Yıldırım, Zeliha; Sakіn, Tuba; Akçelik, Mustafa; Akçelik, Nesife

doi:10.1002/jobm.201900102

Cited by 10 publications

(6 citation statements)

References 52 publications

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“…Li et al (2019) reported that the optimal MOI for E. coli phages (IME281, IME338, IME339, IME340, and IME341) was 0.001. A low MOI is an advantage in the large-scale application, phage production and can thus effectively reduce the overall cost of a commercial phage preparation (Wong et al, 2014;Bao et al, 2015;Yildirim et al, 2019).…”

Section: Application Of Bacteriophages In Artificially Contaminated Fmentioning

confidence: 99%

Evaluation of Novel Virulent Phages Infecting the Aeromonas Hydrophila and Escherichia coli Isolated from Sewage Water Samples

Nasr-Eldin

Soliman

2020

Egypt. J. Bot.

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M ULTIDRUG-resistant bacteria are now emerging for almost all the present-day antibiotics. Aeromonas hydrophila D2007 and Escherichia coli W102 were isolated from fresh food and drinking water samples and they were resistant to 57.14% and 85.71% of tested common antibiotics respectively. Three bacteriophages (phages) were isolated from sewage samples. Morphological examinations suggested that phage ΦAHP7, which infects A. hydrophila D2007, belongs to the Myoviridae family and other phages ΦECP8 and ΦECP9 capable of lysing E. coil W102 belongs to Siphoviridae and Podoviridae families, respectively. For the three phages, the optimal multiplicity of infection (MOI) was calculated to be 0.001. Phages were characterized by determining their host range and stability in pHs, temperatures, and salinity. The latent periods of phages ΦAHP7, ΦECP8, and ΦECP9 were 10, 20 and 10min with average burst sizes of 53.5±0.5, 26.5±0.5 and 67.5±0.5 phages per infected cell, respectively. The three phages gradually reduced OD 600 and are able to stop the growth of A. hydrophila D2007 and E. coli W102 in vitro at a low MOI of 0.001. Phages ΦAHP7, ΦECP8, and ΦECP9 treatments achieved 1.55, 1.68 and 2.28 log CFU/g (P< 0.01) reduction of viable bacterial number in red cabbage and 1.48, 1.38 and 1.68 log CFU/g (P< 0.01) reduction in tomato after 30 min at room temperature (28°C) respectively. Applications of lytic ΦAHP7, ΦECP8, and ΦECP9 bacteriophages lead to a rapid reduction of A. hydrophila D2007 and E. coli W102 counts in fresh food for human consumption.

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Section: Application Of Bacteriophages In Artificially Contaminated Fmentioning

confidence: 99%

Evaluation of Novel Virulent Phages Infecting the Aeromonas Hydrophila and Escherichia coli Isolated from Sewage Water Samples

Nasr-Eldin

Soliman

2020

Egypt. J. Bot.

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“…The phage was propagated according to the method of Yildirim et al (2019) with some modifications. The phage samples (100 μL) and active bacterial culture (300 μL) were transferred to 4 mL LB soft agar (LB broth +0.7% agar) at 45–50°C and vortexed (Reax top, Heidolph, Germany), and then poured onto empty Petri dishes.…”

Section: Methodsmentioning

confidence: 99%

“…The thermal stabilities of the free (Figure 3a) and encapsulated (Figure 3b The broad pH stability is an important property for evaluating the potential utilization of phages as bio-protective in acidic, neutral, and alkaline foods. Resistance to acidic conditions is also a significant feature in therapeutic applications (Yildirim et al, 2019). The pH stability of free and encapsulated phages was also evaluated in a broad pH range (1-13) for 1 h at 37 C (Figure 3c).…”

Section: Thermal and Ph Stability Of The Free And Encapsulated Phagesmentioning

confidence: 99%

“…The SE-P47 phage, previously isolated and identified in our laboratory, is effective against Salmonella Enteritidis and other Salmonella enterica serovar including Salmonella Typhimurium. It belongs the Siphoviridae family, has wide host ranged and does not contain sefC, pefA, spvC, sopE, and gipA virulence gene regions (Yildirim et al, 2018(Yildirim et al, , 2019. This is the first study reporting the encapsulation of SE-P47 phage.…”

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confidence: 99%

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Encapsulation of SE‐P47 phage specific to SalmonellaEnteritidis and evaluation of its stability

Koçer Alaşalvar,

Yıldırım

2024

Journal of Food Safety

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This study was conducted to encapsulate the bacteriophage SE‐P47 target to Salmonella Enteritidis by extrusion method and to examine its stability. Screening and optimization of effective factors in the encapsulation process were performed using fractional factorial design and face‐centered central composite design, respectively. The optimum Na‐alginate concentration and the ratio of coating material to phage for the encapsulation of SE‐P47 phage were 1.5% (v/v) and 2:1, respectively. At the optimum encapsulation point, the highest encapsulation efficiency (98.52%), smallest capsule size (1.28 mm), and highest phage titer were achieved. When exposed to heat treatment at 80°C for 30 min, pH 2 and simulated gastric fluid (pH 2.0) for 120 min, the encapsulated phage maintained almost its stability, but the free (non‐encapsulated) phage almost lost its activity. Phage release from beads in simulated intestinal fluid reached 100% in 4 h. In addition, free and encapsulated phage completely maintained their activity for 12 months at 4 and 25°C. The Salmonella phage encapsulated in this study exhibits high stability in harsh conditions. Thus, this encapsulated phage has the potential to be used as a biocontrol agent or therapeutic purposes in the food chain.

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“…Modern proteomics needs immense powers of resolution, sensitivity, and speed of identifi cation, which so far can be reached through One and/or Two Dimension (1D, 2D) gels in combination with advanced analysis of complex protein distributions in automated fashions considering the large number of diff erent protein interaction domains to provide important data sets [4,5]. Usually, the common technique used to investigate cell protein profi les is Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), which contains separating proteins by isoelectric charge or molecular weight [6][7][8][9]. For a deep understanding of the relevant bacteriophages' proteins biology, this information must be integrated with analytical data from various ' bioinformatics levels' including DNA sequence, mRNA profi les, protein expression and metabolite concentrations as well as information about dynamic spatio-temporal changes in these molecules [10].…”

Section: The Assembly Of Bacteriophage Functional Enzymatic Models Inmentioning

confidence: 99%

The Assembly of Bacteriophage Functional Enzymatic Models in Association with E. coli Proteins’ Profiles

Elshayeb¹,

Elfatih²,

Salih³

et al. 2020

J Biomed Res Environ Sci

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Introduction: The invasion of bacteriophage on the associated host bacterium depends on their receptors' orientation that adsorb them to cell surface. During phage replication a valuable number of proteins acts as lytic enzymes for host puncher at the beginning of the infection and other for burst after lytic cycle compilation. Accordingly, the proteomic relationship among phage and bacterium proteins could easily be studied by their protein profiles analysis. Objective: To detect bacteriophages functional enzymes during lytic cycle. Methods: The isolation and identification of Escherichia coli and their parasitic T7 phage group was done using bacterial culture and common plaque assay techniques. The investigations and protein-protein interactions' assays were inveterate by proteins profile of phage and bacterium using Sodium Dodecyl Sulphate Poly Acrylamide Gel Electrophoresis (SDS-PAGE) to find out their molecular weights, where the scaled location of each mobile band was compared to the standards of identified proteins weights in the molecular ladder. Thereafter, Protein model's assembly and bands migration was done by computer analytical software. Results: Mobilization of the phage' proteins inside the Two Dimensions (2D) gel ranged between 60 and 12 kDa where a model of 4 main bands with molecular weights of (46, 35, 24 and 14 kDa) is corresponded to the host ones, where pure 9 bands with molecular weight ranged between 96-24 kDa. The computational model analysis showed common shared molecular masses of 47, 34 and 16 kDa on plot area of the phage and the bacterium. Model interpretation confirmed that proteins ranged from 47.7 to 34.3 kDa resembles 43.3% of whole phage's proteins that assembled the capsid head and the coil, while the molecular weight mass of 22.5 formed the tail's proteins. The lytic enzymes' molecular weight was ranged between 18-14 kDa according to the function of the enzyme. The study revealed that the 34 kDa band has the common shared peak between T7 phage group and associated Escherichia coli host. Conclusion: Functional models of analysed proteins during phage assembly, ensures lytic enzymes are built in the capsid head and the lysozyme in the tail, they facilitate the enzymatic decay for bacterial host. This enzymatic function is related to the lytic cycle of the bacteriophages and their phenomenon in employing the bacterial DNA in proteins manufacturing during their replication inside host.

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Characterization of SE‐P3, P16, P37, and P47 bacteriophages infecting Salmonella Enteritidis

Cited by 10 publications

References 52 publications

Evaluation of Novel Virulent Phages Infecting the Aeromonas Hydrophila and Escherichia coli Isolated from Sewage Water Samples

Evaluation of Novel Virulent Phages Infecting the Aeromonas Hydrophila and Escherichia coli Isolated from Sewage Water Samples

Encapsulation of SE‐P47 phage specific to SalmonellaEnteritidis and evaluation of its stability

The Assembly of Bacteriophage Functional Enzymatic Models in Association with E. coli Proteins’ Profiles

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