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human pro il 1β  (Sino Biological)


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    Structured Review

    Sino Biological human pro il 1β
    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
    Human Pro Il 1β, supplied by Sino Biological, used in various techniques. Bioz Stars score: 95/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+pro+il+1%CE%B2/Human+IL-1+beta+%2F+IL1B+(E6K)+Protein/pmc12909850-519-19-26
    Average 95 stars, based on 20 article reviews
    human pro il 1β - by Bioz Stars, 2026-09
    95/100 stars

    Images

    1) Product Images from "Loss of Fsr quorum sensing promotes biofilm formation and worsens outcomes in enterococcal infective endocarditis"

    Article Title: Loss of Fsr quorum sensing promotes biofilm formation and worsens outcomes in enterococcal infective endocarditis

    Journal: Nature Communications

    doi: 10.1038/s41467-026-68366-8

    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. C Rat pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
    Figure Legend Snippet: A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. C Rat pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.

    Techniques Used: Staining, Western Blot, Control, Two Tailed Test, Mutagenesis, Incubation, Negative Control, Activation Assay, Positive Control

    Related Articles

    Recombinant:

    Article Title: Interleukin-1β Processing Is Dependent on a Calcium-mediated Interaction with Calmodulin
    Article Snippet: LPS from Escherichia coli serotype 055:B5 (Toll like receptors 2/4) and nigericin were purchased from Sigma. .. The recombinant proteins used were human pro-IL-1β, human calmodulin (both from Sino Biological, Philadelphia, PA), and human IL-1β (R&D Systems, Minneapolis, MN). .. The calcium chelator BAPTA-AM was purchased from Life Technologies, and the calmodulin inhibitors E6 berbamine and W7 were purchased from Enzo Life Sciences (Exeter, UK) and Santa Cruz Biotechnology, respectively.

    Article Title: Caspase-4 dimerisation and D289 auto-processing elicit an interleukin-1β-converting enzyme
    Article Snippet: Cell extracts and supernatants were precipitated using methanol/chloroform and analysed by Western blot following previously described methods ( ) and the following reagents: antibodies against the caspase-4 large subunit (mouse monoclonal, 1:1,000; Proteintech), hIL-1β and mIL-1β (goat polyclonal, 1:1,000; R&D Systems), caspase-1 large subunit (Bally-1, mouse monoclonal, 1:1,000; Adipogen), V5 (SV5-Pk1, mouse monoclonal, 1:2000; Abcam), and GAPDH. .. 5 U of full-length human caspase-1 (Abcam) or caspase-4 (Abcam) recombinant proteins were incubated with 2 μg of recombinant human pro-IL-1β (Sino Biological Inc.) in caspase activity buffer (200 mM NaCl, 50 mM HEPES, pH 8.0, 50 mM KCl). .. The protein mix was incubated at 37°C for 0, 6, and 24 h. Cleavage of recombinant proteins was analysed by Western blot using standard methods ( ) and the following reagents: antibodies against the caspase-4 large subunit (4B9, mouse monoclonal antibody, 1:1,000; Santa Cruz Biotechnology), human IL-1β (goat polyclonal antibody, 1:1,000; R&D Systems), caspase-1 (D7F10, rabbit monoclonal, 1:1,000; Cell Signalling Technology).

    Article Title: Caspase-4 dimerisation and D289 auto-processing elicits an interleukin-1β converting enzyme
    Article Snippet: Cell extracts and supernatants were precipitated using methanol/chloroform and analysed by western blot following previously described methods ( ) and the following reagents: antibodies against the caspase-4 large subunit, hIL-1β, caspase-1 large subunit (Bally-1, mouse monoclonal, 1:1000; Adipogen), V5 (SV5-Pk1, mouse monoclonal, 1:2000; Abcam) and GAPDH. .. 5 U of full-length human caspase-1 (Abcam) or caspase-4 (Abcam) recombinant proteins were incubated with 2 μg of recombinant human pro-IL-1β (Sino Biological Inc) in caspase activity buffer (200 mM NaCl, 50 mM HEPES, pH 8.0, 50 mM KCl). .. The protein mix was incubated at 37°C for 0 h, 6 h, and 24 h. Cleavage of recombinant proteins was analysed by western blot using standard methods ( ) and the following reagents: antibodies against the caspase-4 large subunit (4B9, mouse monoclonal antibody, 1:1000; Santa Cruz Biotechnology), human IL-1β (goat polyclonal antibody, 1:1000, R&D Systems), caspase-1 (D7F10, rabbit monoclonal, 1:1000; Cell Signalling Technology).

    Article Title: Caspase-4 dimerisation and D289 auto-processing elicit an interleukin-1β-converting enzyme.
    Article Snippet: Cell extracts and supernatants were precipitated using methanol/chloroform and analysed by Western blot following previously described methods (Groß, 2012) and the following reagents: antibodies against the caspase-4 large subunit (mouse monoclonal, 1:1,000; Proteintech), hIL-1β and mIL-1β (goat polyclonal, 1:1,000; R&D Systems), caspase-1 large subunit (Bally-1, mousemonoclonal, 1:1,000; Adipogen), V5 (SV5Pk1, mouse monoclonal, 1:2000; Abcam), and GAPDH. .. 5 U of full-length human caspase-1 (Abcam) or caspase-4 (Abcam) recombinant proteins were incubated with 2 μg of recombinant human pro-IL-1β (Sino Biological Inc.) in caspase activity buffer (200mMNaCl, 50mMHEPES, pH 8.0, 50mM KCl). .. The proteinmix was incubated at 37°C for 0, 6, and 24 h. Cleavage of recombinant proteins was analysed by Western blot using standard methods (Groß, 2012) and the following reagents: antibodies against the caspase-4 large subunit (4B9, mouse monoclonal antibody, 1:1,000; Santa Cruz Biotechnology), human IL-1β (goat polyclonal antibody, 1:1,000; R&D Systems), caspase-1 (D7F10, rabbit monoclonal, 1:1,000; Cell Signalling Technology).

    Western Blot:

    Article Title: Infection with Mycobacterium avium subsp. paratuberculosis Results in Rapid Interleukin-1? Release and Macrophage Transepithelial Migration
    Article Snippet: Supernatants from M. avium subsp. paratuberculosis invasion assays were collected at 10 and 30 min p.i., filtered with a 0.2-μm Millex syringe-driven filter unit (Millipore, Billerica, MA), and concentrated using a Speedvac. .. The following controls were included in Western blot analysis: human pro-IL-1β (Sino Biological Inc., Beijing, China), mouse IL-1β (Abcam, Cambridge, MA), and bovine IL-1β (Pierce, Rockford, IL). .. Twenty μl of each sample was separately combined with 5.0 μl of Laemmli buffer (Bio-Rad, Hercules, CA), denatured at 95°C, and loaded onto a Precise 4-to-20% Tris-HEPES gradient precast gel (Pierce, Rockford, IL).

    Incubation:

    Article Title: Caspase-4 dimerisation and D289 auto-processing elicit an interleukin-1β-converting enzyme
    Article Snippet: Cell extracts and supernatants were precipitated using methanol/chloroform and analysed by Western blot following previously described methods ( ) and the following reagents: antibodies against the caspase-4 large subunit (mouse monoclonal, 1:1,000; Proteintech), hIL-1β and mIL-1β (goat polyclonal, 1:1,000; R&D Systems), caspase-1 large subunit (Bally-1, mouse monoclonal, 1:1,000; Adipogen), V5 (SV5-Pk1, mouse monoclonal, 1:2000; Abcam), and GAPDH. .. 5 U of full-length human caspase-1 (Abcam) or caspase-4 (Abcam) recombinant proteins were incubated with 2 μg of recombinant human pro-IL-1β (Sino Biological Inc.) in caspase activity buffer (200 mM NaCl, 50 mM HEPES, pH 8.0, 50 mM KCl). .. The protein mix was incubated at 37°C for 0, 6, and 24 h. Cleavage of recombinant proteins was analysed by Western blot using standard methods ( ) and the following reagents: antibodies against the caspase-4 large subunit (4B9, mouse monoclonal antibody, 1:1,000; Santa Cruz Biotechnology), human IL-1β (goat polyclonal antibody, 1:1,000; R&D Systems), caspase-1 (D7F10, rabbit monoclonal, 1:1,000; Cell Signalling Technology).

    Article Title: Caspase-4 dimerisation and D289 auto-processing elicits an interleukin-1β converting enzyme
    Article Snippet: Cell extracts and supernatants were precipitated using methanol/chloroform and analysed by western blot following previously described methods ( ) and the following reagents: antibodies against the caspase-4 large subunit, hIL-1β, caspase-1 large subunit (Bally-1, mouse monoclonal, 1:1000; Adipogen), V5 (SV5-Pk1, mouse monoclonal, 1:2000; Abcam) and GAPDH. .. 5 U of full-length human caspase-1 (Abcam) or caspase-4 (Abcam) recombinant proteins were incubated with 2 μg of recombinant human pro-IL-1β (Sino Biological Inc) in caspase activity buffer (200 mM NaCl, 50 mM HEPES, pH 8.0, 50 mM KCl). .. The protein mix was incubated at 37°C for 0 h, 6 h, and 24 h. Cleavage of recombinant proteins was analysed by western blot using standard methods ( ) and the following reagents: antibodies against the caspase-4 large subunit (4B9, mouse monoclonal antibody, 1:1000; Santa Cruz Biotechnology), human IL-1β (goat polyclonal antibody, 1:1000, R&D Systems), caspase-1 (D7F10, rabbit monoclonal, 1:1000; Cell Signalling Technology).

    Article Title: Caspase-4 dimerisation and D289 auto-processing elicit an interleukin-1β-converting enzyme.
    Article Snippet: Cell extracts and supernatants were precipitated using methanol/chloroform and analysed by Western blot following previously described methods (Groß, 2012) and the following reagents: antibodies against the caspase-4 large subunit (mouse monoclonal, 1:1,000; Proteintech), hIL-1β and mIL-1β (goat polyclonal, 1:1,000; R&D Systems), caspase-1 large subunit (Bally-1, mousemonoclonal, 1:1,000; Adipogen), V5 (SV5Pk1, mouse monoclonal, 1:2000; Abcam), and GAPDH. .. 5 U of full-length human caspase-1 (Abcam) or caspase-4 (Abcam) recombinant proteins were incubated with 2 μg of recombinant human pro-IL-1β (Sino Biological Inc.) in caspase activity buffer (200mMNaCl, 50mMHEPES, pH 8.0, 50mM KCl). .. The proteinmix was incubated at 37°C for 0, 6, and 24 h. Cleavage of recombinant proteins was analysed by Western blot using standard methods (Groß, 2012) and the following reagents: antibodies against the caspase-4 large subunit (4B9, mouse monoclonal antibody, 1:1,000; Santa Cruz Biotechnology), human IL-1β (goat polyclonal antibody, 1:1,000; R&D Systems), caspase-1 (D7F10, rabbit monoclonal, 1:1,000; Cell Signalling Technology).

    Article Title: Loss of Fsr quorum sensing promotes biofilm formation and worsens outcomes in enterococcal infective endocarditis
    Article Snippet: .. E. faecalis overnight cultures of OG1RF WT and mutants were diluted 1:10 in 200 μl fresh BHI supplemented with human pro-IL-1β (100 ng/mL; Cat. Nr. 10139-H07E, Sino Biological) and incubated for 2, 4, 6 and 24 h, or with rat pro-IL-1β (10 ng/ml, Cat. Nr. 80023-R07E, Sino Biological) and incubated at 2, 4, and 6 h at 37 °C, static conditions. ..

    Activity Assay:

    Article Title: Caspase-4 dimerisation and D289 auto-processing elicit an interleukin-1β-converting enzyme
    Article Snippet: Cell extracts and supernatants were precipitated using methanol/chloroform and analysed by Western blot following previously described methods ( ) and the following reagents: antibodies against the caspase-4 large subunit (mouse monoclonal, 1:1,000; Proteintech), hIL-1β and mIL-1β (goat polyclonal, 1:1,000; R&D Systems), caspase-1 large subunit (Bally-1, mouse monoclonal, 1:1,000; Adipogen), V5 (SV5-Pk1, mouse monoclonal, 1:2000; Abcam), and GAPDH. .. 5 U of full-length human caspase-1 (Abcam) or caspase-4 (Abcam) recombinant proteins were incubated with 2 μg of recombinant human pro-IL-1β (Sino Biological Inc.) in caspase activity buffer (200 mM NaCl, 50 mM HEPES, pH 8.0, 50 mM KCl). .. The protein mix was incubated at 37°C for 0, 6, and 24 h. Cleavage of recombinant proteins was analysed by Western blot using standard methods ( ) and the following reagents: antibodies against the caspase-4 large subunit (4B9, mouse monoclonal antibody, 1:1,000; Santa Cruz Biotechnology), human IL-1β (goat polyclonal antibody, 1:1,000; R&D Systems), caspase-1 (D7F10, rabbit monoclonal, 1:1,000; Cell Signalling Technology).

    Article Title: Caspase-4 dimerisation and D289 auto-processing elicits an interleukin-1β converting enzyme
    Article Snippet: Cell extracts and supernatants were precipitated using methanol/chloroform and analysed by western blot following previously described methods ( ) and the following reagents: antibodies against the caspase-4 large subunit, hIL-1β, caspase-1 large subunit (Bally-1, mouse monoclonal, 1:1000; Adipogen), V5 (SV5-Pk1, mouse monoclonal, 1:2000; Abcam) and GAPDH. .. 5 U of full-length human caspase-1 (Abcam) or caspase-4 (Abcam) recombinant proteins were incubated with 2 μg of recombinant human pro-IL-1β (Sino Biological Inc) in caspase activity buffer (200 mM NaCl, 50 mM HEPES, pH 8.0, 50 mM KCl). .. The protein mix was incubated at 37°C for 0 h, 6 h, and 24 h. Cleavage of recombinant proteins was analysed by western blot using standard methods ( ) and the following reagents: antibodies against the caspase-4 large subunit (4B9, mouse monoclonal antibody, 1:1000; Santa Cruz Biotechnology), human IL-1β (goat polyclonal antibody, 1:1000, R&D Systems), caspase-1 (D7F10, rabbit monoclonal, 1:1000; Cell Signalling Technology).

    Article Title: Caspase-4 dimerisation and D289 auto-processing elicit an interleukin-1β-converting enzyme.
    Article Snippet: Cell extracts and supernatants were precipitated using methanol/chloroform and analysed by Western blot following previously described methods (Groß, 2012) and the following reagents: antibodies against the caspase-4 large subunit (mouse monoclonal, 1:1,000; Proteintech), hIL-1β and mIL-1β (goat polyclonal, 1:1,000; R&D Systems), caspase-1 large subunit (Bally-1, mousemonoclonal, 1:1,000; Adipogen), V5 (SV5Pk1, mouse monoclonal, 1:2000; Abcam), and GAPDH. .. 5 U of full-length human caspase-1 (Abcam) or caspase-4 (Abcam) recombinant proteins were incubated with 2 μg of recombinant human pro-IL-1β (Sino Biological Inc.) in caspase activity buffer (200mMNaCl, 50mMHEPES, pH 8.0, 50mM KCl). .. The proteinmix was incubated at 37°C for 0, 6, and 24 h. Cleavage of recombinant proteins was analysed by Western blot using standard methods (Groß, 2012) and the following reagents: antibodies against the caspase-4 large subunit (4B9, mouse monoclonal antibody, 1:1,000; Santa Cruz Biotechnology), human IL-1β (goat polyclonal antibody, 1:1,000; R&D Systems), caspase-1 (D7F10, rabbit monoclonal, 1:1,000; Cell Signalling Technology).



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    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
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    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
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    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
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    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
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    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. <t>C</t> <t>Rat</t> <t>pro-IL-1β</t> and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.
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    Image Search Results


    A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. C Rat pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Loss of Fsr quorum sensing promotes biofilm formation and worsens outcomes in enterococcal infective endocarditis

    doi: 10.1038/s41467-026-68366-8

    Figure Lengend Snippet: A Z-projections of WT and Δ gelE vegetations at 72 hpi, captured with LSCM and stained for DNA, myeloperoxidase (MPO), and IL-1β. Cyan insets are highlighting the presence of IL-1β between the NETs-biofilm interface. Orange inset is shown in Fig. S4B, highlighting the colocalization of IL-1β with neutrophils. Representative images shown from n = 3, N = 1. Bf = biofilm, scale = 20 µm. B Detection and quantification of IL-1β in WT and Δ gelE vegetations at 72 hpi with western blotting. Loading control = β-actin. Mean ± SEM, n = 5 from N = 2, A.U. = arbitrary units. Statistical significance was assessed with a two-tailed t-test. C Rat pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Rat pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6 h. BHI = Negative control with only media and pro-IL 1β. Representative blot shown from N = 2. D Human pro-IL-1β and its cleaved fragments in supernatants from OG1RF WT and mutant strains detected by western blotting. Human pro-IL-1β was incubated in BHI with indicated OG1RF strains for 2, 4, 6, and 24 h. Gelatinase presence was also determined in these supernatants. Δ gelE :: gelE E352A expresses proteolytically inactive gelatinase. Representative blot shown from N = 2. BHI = Negative control with only media and pro-IL 1β. E Mean activation of HEK-Blue IL-1R reporter cells by supernatants harvested from OG1RF WT and Δ gelE :: gelE E352A cultures with or without human pro-IL-1β at 18 h. Stimulation of cells with mature human IL-1β was used as a positive control. N = 3, Error = SEM. Statistical significance was determined with one-way ANOVA. F Schematic representation of gelatinase (blue) and caspase-1 cleavage sites (red) across human, rat, and mouse pro-IL-1β; n = animals per group, N = independent experiments, ns not significant (p ≥ 0.05), Red arrowhead = pro-IL-1β, blue arrowhead = mature IL-1β. Exact p values are reported in the figure. Source data are provided as a Source Data file.

    Article Snippet: E. faecalis overnight cultures of OG1RF WT and mutants were diluted 1:10 in 200 μl fresh BHI supplemented with human pro-IL-1β (100 ng/mL; Cat. Nr. 10139-H07E, Sino Biological) and incubated for 2, 4, 6 and 24 h, or with rat pro-IL-1β (10 ng/ml, Cat. Nr. 80023-R07E, Sino Biological) and incubated at 2, 4, and 6 h at 37 °C, static conditions.

    Techniques: Staining, Western Blot, Control, Two Tailed Test, Mutagenesis, Incubation, Negative Control, Activation Assay, Positive Control