high productive infection against generic e coli atcc 13706  (ATCC)

Journal: Frontiers in Microbiology

Article Title: Penetrating the biofilm barrier: characterization of Escherichia phage vB_EcoS-TPF103dw and harnessing depolymerase to combat Shiga toxin-producing Escherichia coli O103 biofilm

doi: 10.3389/fmicb.2025.1715907

Figure Lengend Snippet: Circular genome map of E. coli phage vB_EcoS-TPF103dw (length = 113,080 bp), annotated using Prokka and Bakta pipelines via Proksee. Predicted coding sequences (CDS), structural RNAs (tRNA/rRNA), and open reading frames (ORFs) are represented as colored blocks (red, blue, and green, respectively) across concentric rings. Functional annotations include structural phage components, lytic enzymes (e.g., endolysins, holins), and putative host-interaction proteins. Notable features include the terminase large subunit, tail fiber proteins, and chaperones indicative of complex host recognition mechanisms.

Article Snippet: In contrast, generic E. coli ATCC 13706, the isolation host, produced significantly larger plaques than O103 strains, while some O103 isolates formed pin-sized plaques that complicated titer enumeration ( ).

Techniques: Functional Assay

Journal: Frontiers in Microbiology

Article Title: Penetrating the biofilm barrier: characterization of Escherichia phage vB_EcoS-TPF103dw and harnessing depolymerase to combat Shiga toxin-producing Escherichia coli O103 biofilm

doi: 10.3389/fmicb.2025.1715907

Figure Lengend Snippet: Stability of phage: biological characteristics of phage TPF103dw, including various pH stability at 25°C for 24 h (A) , temperature stability for 24 h (B) , and a one-step growth curve of generic E. coli ATCC 13706 (C) . Error bars indicate 95% confidence intervals for pH and temperature, and standard error bars for one-step growth curve. Asteriks indicated statistically significant differences among groups and p < 0.05.

Article Snippet: In contrast, generic E. coli ATCC 13706, the isolation host, produced significantly larger plaques than O103 strains, while some O103 isolates formed pin-sized plaques that complicated titer enumeration ( ).

Techniques:

Journal: Frontiers in Microbiology

Article Title: Penetrating the biofilm barrier: characterization of Escherichia phage vB_EcoS-TPF103dw and harnessing depolymerase to combat Shiga toxin-producing Escherichia coli O103 biofilm

doi: 10.3389/fmicb.2025.1715907

Figure Lengend Snippet: Bacterial challenge assay for E. coli O103, five E. coli O103 treated with phage TPF103dw at MOI 10,000 at 25 °C for 24 h based on the bacterial optical density at wavelength 600 nm (OD 600 ). The control group only contains bacterial culture.

Article Snippet: In contrast, generic E. coli ATCC 13706, the isolation host, produced significantly larger plaques than O103 strains, while some O103 isolates formed pin-sized plaques that complicated titer enumeration ( ).

Techniques: Control

Journal: Frontiers in Microbiology

Article Title: Penetrating the biofilm barrier: characterization of Escherichia phage vB_EcoS-TPF103dw and harnessing depolymerase to combat Shiga toxin-producing Escherichia coli O103 biofilm

doi: 10.3389/fmicb.2025.1715907

Figure Lengend Snippet: Scanning electron micrographs of E. coli O103 biofilms on stainless steel surfaces. Planktonic E. coli O103 cells were allowed to settle on sterile stainless steel coupons and visualized using SEM at 5,000 × magnification (A) , Day 2 untreated control biofilm at 800 × magnification, showing a thick, dense matrix with extensive extracellular material characteristic of mature biofilm (B) . Corresponding phage-treated biofilm at 800 × magnification, exhibiting visibly reduced biomass and a disrupted matrix structure (C) . Higher magnification (10,000×) view of the control biofilm, revealing dense cellular packing and abundant extracellular polymeric substances (EPS) (D) . Phage-treated biofilm at 10,000 × magnification, displaying isolated bacterial cells with visibly reduced EPS and disrupted aggregation (E) . Biofilm treated filtrate containing soluble phage-derived enzymes (850 × magnification) reveals compact cell stacking with a complete absence of visible EPS (F) . Biofilm treated with filtrate containing soluble phage-derived enzymes (10,000 × magnification) reveals compact cell stacking with a complete absence of visible EPS (G) . These images highlight phage-derived enzymatic activity that may degrade biofilm matrix, supporting potential anti-biofilm mechanisms. Images demonstrate the structural impact of phage treatment on biofilm integrity.

Article Snippet: In contrast, generic E. coli ATCC 13706, the isolation host, produced significantly larger plaques than O103 strains, while some O103 isolates formed pin-sized plaques that complicated titer enumeration ( ).

Techniques: Sterility, Control, Isolation, Derivative Assay, Activity Assay