e coli  (ATCC)

Journal: Bioactive Materials

Article Title: Degradation-tunable coating with sustained silver release for spinal implants to prevent postoperative infections

doi: 10.1016/j.bioactmat.2026.02.035

Figure Lengend Snippet: Characterization of Ag, ZIF-8 and AgZ nanoparticles. (a) TEM images of Ag, ZIF-8, and AgZ nanoparticles. (b) TEM and element mapping images of AgZ. (c) Diameter distribution of nanoparticles. (d) Zeta potential measurements of nanoparticles suspended in PBS. (e) X-ray diffraction (XRD) pattern of nanoparticles, with black arrows indicating representative silver peaks in AgZ. (f) Fourier transform infrared (FTIR) spectra of nanoparticles. (g) Mass content of silver and zinc elements in AgZ, as measured by inductively coupled plasma mass spectrometry (ICP-MS). (h) Photograph of nanoparticle dispersions. Nanoparticles were dispersed in PBS (1 mg/mL) by ultrasound and allowed to stand for 10 min at room temperature. The yellow arrow highlights the precipitated Ag nanoparticles. (i) Minimal bactericidal concentration (MBC) of nanoparticles against MRSA and E. coli . AgZ concentration is expressed in terms of silver equivalent to Ag. All data are presented as mean ± standard deviation from three independent samples or experiments.

Article Snippet: Two bacterial strains, methicillin-resistant Staphylococcus aureus ATCC 43300 (MRSA) and Escherichia coli ATCC 25922 ( E. coli ), were used in this study.

Techniques: Zeta Potential Analyzer, Fourier Transform Infrared Spectroscopy, Clinical Proteomics, Mass Spectrometry, Concentration Assay, Standard Deviation

Journal: Bioactive Materials

Article Title: Degradation-tunable coating with sustained silver release for spinal implants to prevent postoperative infections

doi: 10.1016/j.bioactmat.2026.02.035

Figure Lengend Snippet: Transcriptomic analysis of gene expression changes in MRSA and E. coli . (a) Heatmap showing the top 20 differentially expressed genes (DEGs) of between the AgZ-treated and PBS (control) groups, both upregulated and downregulated, from three biologically independent samples. (b) Volcano plot representing the distribution of DEGs, with a significance threshold of p-value <0.05 and |log 2 FC| > 1. (c) Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway analysis highlighting the enriched pathways in the DEGs between AgZ-treated and PBS-treated bacteria. (d) Gene Set Enrichment Analysis (GSEA) depicting enriched gene sets. (e) Gene ontology (GO) analysis of differentially expressed genes between AgZ-treated and PBS-treated bacteria.

Article Snippet: Two bacterial strains, methicillin-resistant Staphylococcus aureus ATCC 43300 (MRSA) and Escherichia coli ATCC 25922 ( E. coli ), were used in this study.

Techniques: Gene Expression, Control, Bacteria

Journal: Journal of Structural Biology: X

Article Title: Salt bridge disruption in colicin Ib channel-forming domain enhances membrane translocation and bactericidal activity

doi: 10.1016/j.yjsbx.2026.100144

Figure Lengend Snippet: E. coli viability after the treatments of full-length ColIb and salt bridge variants using spot assay and CFU analysis. E. coli ATCC8739 treated with full-length WT ColIb or salt bridge variants, in the a, c absence and b, d presence of the iron chelator, 2,2′ bipyridine (100 μM), were 10-fold serially diluted and spotted. The groups treated with the protein buffer were included as a negative control. The bacterial cell viabilities treated with 0.1 nM and 0.01 nM of protein samples are compared in b . Data represent the mean ± S.D. with n = 3 independent experimental replicates. Statistical analyses were assessed using a one-way ANOVA in GraphPad Prism. * p ≤ 0.05, ** p ≤ 0.01, *** p ≤ 0.001, **** p ≤ 0.0001, n.s., not significant.

Article Snippet: Since the above experimental results demonstrated that disrupting the electrostatic interactions in the C-domain leads to a more loosely packed tertiary structure, which may reduce the unfolding energy required for translocation through CirA and facilitate membrane insertion, we sought to characterize the antibacterial activity by monitoring the viability of E. coli ATCC 8739 treated with full-length ColIb and its salt bridge variants ( , ).

Techniques: Spot Test, Negative Control

Journal: Journal of Structural Biology: X

Article Title: Salt bridge disruption in colicin Ib channel-forming domain enhances membrane translocation and bactericidal activity

doi: 10.1016/j.yjsbx.2026.100144

Figure Lengend Snippet: Bactericidal activity of the WT ColIb C-domain and salt bridge variants using the spot-on-lawn antimicrobial assay. Three-fold serially diluted a , b isolated ColIb C-domain and variants, and c , d full-length ColIb were spotted on the lawn of E. coli ATCC8739. The WT ColIb C-domain and variants were purified at pH 6.0 ( a , b left) and pH 4.5 ( a , b right) for spotting. The C-domain-truncated ColIb variant (TR) was pre-spotted on the plate before spotting b the ColIb C-domain and variants, and d full-length ColIb. Refer to Methods for details.

Article Snippet: Since the above experimental results demonstrated that disrupting the electrostatic interactions in the C-domain leads to a more loosely packed tertiary structure, which may reduce the unfolding energy required for translocation through CirA and facilitate membrane insertion, we sought to characterize the antibacterial activity by monitoring the viability of E. coli ATCC 8739 treated with full-length ColIb and its salt bridge variants ( , ).

Techniques: Activity Assay, Isolation, Purification, Variant Assay