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  • 94
    Millipore chitinase
    B. safensis targets the C. neoformans cell surface and bacterial <t>chitinase</t> activity contributes to the antimelanization effect during the dual-species interaction. (A) Individual coincubation of 154 different C. neoformans transcription factor (TF) mutants with B. safensis identified the fungal cell wall and cell membrane as possible targets. For each TF, two independent mutants were incubated in liquid l -DOPA medium with or without bacteria (308 TF strains in total) at 30°C for 5 days. Growth was determined via OD 405 measurements. Results are plotted relative to the fungus-only control. Each circle represents the mean of the results for two independent mutants of the same TF. The black dotted lines and the gray dotted lines indicate the overall means of all values ± SD, respectively. The experiment (exp.) was performed twice, and TF mutant outliers (in at least one experiment) are indicated and color-coded according to previously published roles of these TFs in cell membrane and cell wall integrity (see scheme on the right). Rel. growth, relative growth of fungal cells in coculture versus monoculture, expressed in percentages. (B) Sorbitol bypassed B. safensis -mediated suppression of fungal melanization, and this effect was not observed in a C. neoformans nrg1 Δ mutant. C. neoformans wild-type strain H99 or the nrg1 Δ mutant was incubated alone or mixed with bacteria on l -DOPA agar with or without sorbitol for 48 h. Ctrl, control; Sorb, sorbitol. Scale bar, 5 mm. The experiment was performed twice, and representative images are shown. (C) Coincubation of C. neoformans nrg1 Δ with B. safensis in YPD for 24 h resulted in fungal cell aggregation and abnormal cell wall chitin staining. White squares in the panels of the middle row indicate regions that are shown in a magnified view in the bottom row. Arrows point to abnormal,
    Chitinase, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/chitinase/product/Millipore
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    chitinase - by Bioz Stars, 2021-09
    94/100 stars
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    93
    R&D Systems chi3l1
    Serum levels of <t>CHI3L1</t> and IGFBP-2 in patients without pulmonary and with liver metastasis. Differences were calculated using a Mann Whitney U with Bonferroni's correction test. (A) CHI3L1 and (B) IGFBP-2 levels in patients with liver metastases ≥100
    Chi3l1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/chi3l1/product/R&D Systems
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    chi3l1 - by Bioz Stars, 2021-09
    93/100 stars
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    93
    Millipore chitinase assay kit
    (a) Bound <t>GFP-chitinase</t> levels and chitin levels of wild-type strain BY4742 and BY4742 Δ ygp1 and BY4742 Δ tus1 ), and equal amounts of cells based on OD measurement at 600 nm were washed and resuspended in PBS buffer before adding GFP-tagged chitinase or before staining with calcofluor white for chitin quantification. Fluorescence intensity is expressed in arbitrary units (a.u.). (b) Fold change of the deletion mutant strains relative to the wild-type strain BY4742. A correlation of 0.98 was obtained between the amount of yeast cell wall chitin and the amount of GFP-chitinase bound to the cell wall.
    Chitinase Assay Kit, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/chitinase assay kit/product/Millipore
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    chitinase assay kit - by Bioz Stars, 2021-09
    93/100 stars
      Buy from Supplier

    Image Search Results


    B. safensis targets the C. neoformans cell surface and bacterial chitinase activity contributes to the antimelanization effect during the dual-species interaction. (A) Individual coincubation of 154 different C. neoformans transcription factor (TF) mutants with B. safensis identified the fungal cell wall and cell membrane as possible targets. For each TF, two independent mutants were incubated in liquid l -DOPA medium with or without bacteria (308 TF strains in total) at 30°C for 5 days. Growth was determined via OD 405 measurements. Results are plotted relative to the fungus-only control. Each circle represents the mean of the results for two independent mutants of the same TF. The black dotted lines and the gray dotted lines indicate the overall means of all values ± SD, respectively. The experiment (exp.) was performed twice, and TF mutant outliers (in at least one experiment) are indicated and color-coded according to previously published roles of these TFs in cell membrane and cell wall integrity (see scheme on the right). Rel. growth, relative growth of fungal cells in coculture versus monoculture, expressed in percentages. (B) Sorbitol bypassed B. safensis -mediated suppression of fungal melanization, and this effect was not observed in a C. neoformans nrg1 Δ mutant. C. neoformans wild-type strain H99 or the nrg1 Δ mutant was incubated alone or mixed with bacteria on l -DOPA agar with or without sorbitol for 48 h. Ctrl, control; Sorb, sorbitol. Scale bar, 5 mm. The experiment was performed twice, and representative images are shown. (C) Coincubation of C. neoformans nrg1 Δ with B. safensis in YPD for 24 h resulted in fungal cell aggregation and abnormal cell wall chitin staining. White squares in the panels of the middle row indicate regions that are shown in a magnified view in the bottom row. Arrows point to abnormal,

    Journal: mBio

    Article Title: Disarming Fungal Pathogens: Bacillus safensis Inhibits Virulence Factor Production and Biofilm Formation by Cryptococcus neoformans and Candida albicans

    doi: 10.1128/mBio.01537-17

    Figure Lengend Snippet: B. safensis targets the C. neoformans cell surface and bacterial chitinase activity contributes to the antimelanization effect during the dual-species interaction. (A) Individual coincubation of 154 different C. neoformans transcription factor (TF) mutants with B. safensis identified the fungal cell wall and cell membrane as possible targets. For each TF, two independent mutants were incubated in liquid l -DOPA medium with or without bacteria (308 TF strains in total) at 30°C for 5 days. Growth was determined via OD 405 measurements. Results are plotted relative to the fungus-only control. Each circle represents the mean of the results for two independent mutants of the same TF. The black dotted lines and the gray dotted lines indicate the overall means of all values ± SD, respectively. The experiment (exp.) was performed twice, and TF mutant outliers (in at least one experiment) are indicated and color-coded according to previously published roles of these TFs in cell membrane and cell wall integrity (see scheme on the right). Rel. growth, relative growth of fungal cells in coculture versus monoculture, expressed in percentages. (B) Sorbitol bypassed B. safensis -mediated suppression of fungal melanization, and this effect was not observed in a C. neoformans nrg1 Δ mutant. C. neoformans wild-type strain H99 or the nrg1 Δ mutant was incubated alone or mixed with bacteria on l -DOPA agar with or without sorbitol for 48 h. Ctrl, control; Sorb, sorbitol. Scale bar, 5 mm. The experiment was performed twice, and representative images are shown. (C) Coincubation of C. neoformans nrg1 Δ with B. safensis in YPD for 24 h resulted in fungal cell aggregation and abnormal cell wall chitin staining. White squares in the panels of the middle row indicate regions that are shown in a magnified view in the bottom row. Arrows point to abnormal, "scratch-like" CFW staining. DIC, differential interference contrast; CFW, calcofluor white. Scale bars indicate 5 µm (middle row) and 2 µm (bottom row). The experiment was performed twice, and representative images are shown. (D) B. safensis and CFW synergistically inhibit cryptococcal growth. CFU-based analysis of C. neoformans growth in YPD in presence of CFW or bacteria or a combination of the two was performed. Results are the means ± SD of two independent experiments, each performed in duplicate. (E) A chitinase inhibitor partially rescues B. safensis -mediated inhibition of fungal melanization on l -DOPA. Strains were incubated at 30°C for 48 h. Ctrl, control; BisC, bisdionine C. Scale bar, 5 mm. The experiment was performed three times, and representative images are shown.

    Article Snippet: To analyze the effects of chitinase on formation of melanin, fungal cells were resuspended in 1 mg ml−1 chitinase (from Streptomyces griseus ; Sigma) solution before being spotted onto l -DOPA agar.

    Techniques: Activity Assay, Incubation, Mutagenesis, Staining, Inhibition

    Exogenous chitinase partially inhibits C. albicans filamentation. (A) C. albicans was grown with or without B. safensis or 100 µg ml −1 chitinase in 10% FCS at 37°C and 5% CO 2 for 24 h. White squares in the upper row panels indicate regions that are shown in a magnified view in the bottom row. Arrows point to abnormally shaped C. albicans cells, and arrowheads point to C. albicans yeast cells, which were not observed in the control sample without chitinase. Scale bar, 50 µm. (B) Semiquantitative evaluation of the impact of chitinase on C. albicans hypha formation. Results are the means + SD of three independent experiments. *, P

    Journal: mBio

    Article Title: Disarming Fungal Pathogens: Bacillus safensis Inhibits Virulence Factor Production and Biofilm Formation by Cryptococcus neoformans and Candida albicans

    doi: 10.1128/mBio.01537-17

    Figure Lengend Snippet: Exogenous chitinase partially inhibits C. albicans filamentation. (A) C. albicans was grown with or without B. safensis or 100 µg ml −1 chitinase in 10% FCS at 37°C and 5% CO 2 for 24 h. White squares in the upper row panels indicate regions that are shown in a magnified view in the bottom row. Arrows point to abnormally shaped C. albicans cells, and arrowheads point to C. albicans yeast cells, which were not observed in the control sample without chitinase. Scale bar, 50 µm. (B) Semiquantitative evaluation of the impact of chitinase on C. albicans hypha formation. Results are the means + SD of three independent experiments. *, P

    Article Snippet: To analyze the effects of chitinase on formation of melanin, fungal cells were resuspended in 1 mg ml−1 chitinase (from Streptomyces griseus ; Sigma) solution before being spotted onto l -DOPA agar.

    Techniques:

    Proposed model depicting the impact of B. safensis on fungal cell walls. (A) Schematic view of the C. neoformans cell membrane and cell wall organization, with attached capsule polysaccharide. α-1,3-glucan is shown in light red, β-1,3-glucan is shown in orange, and β-1,6-glucan is shown in dark red. (B) Following direct cell contact, the environmental bacterium B. safensis produces chitinases and other factors which degrade fungal cell wall chitin and influence the interspecies interaction. The destabilization of the fungal cell wall architecture does not lead to fungal cell death but prevents proper anchoring of melanin and polysaccharide capsule components, thereby disarming the virulence factors of the fungal pathogen.

    Journal: mBio

    Article Title: Disarming Fungal Pathogens: Bacillus safensis Inhibits Virulence Factor Production and Biofilm Formation by Cryptococcus neoformans and Candida albicans

    doi: 10.1128/mBio.01537-17

    Figure Lengend Snippet: Proposed model depicting the impact of B. safensis on fungal cell walls. (A) Schematic view of the C. neoformans cell membrane and cell wall organization, with attached capsule polysaccharide. α-1,3-glucan is shown in light red, β-1,3-glucan is shown in orange, and β-1,6-glucan is shown in dark red. (B) Following direct cell contact, the environmental bacterium B. safensis produces chitinases and other factors which degrade fungal cell wall chitin and influence the interspecies interaction. The destabilization of the fungal cell wall architecture does not lead to fungal cell death but prevents proper anchoring of melanin and polysaccharide capsule components, thereby disarming the virulence factors of the fungal pathogen.

    Article Snippet: To analyze the effects of chitinase on formation of melanin, fungal cells were resuspended in 1 mg ml−1 chitinase (from Streptomyces griseus ; Sigma) solution before being spotted onto l -DOPA agar.

    Techniques:

    Serum levels of CHI3L1 and IGFBP-2 in patients without pulmonary and with liver metastasis. Differences were calculated using a Mann Whitney U with Bonferroni's correction test. (A) CHI3L1 and (B) IGFBP-2 levels in patients with liver metastases ≥100

    Journal: Oncology Letters

    Article Title: Novel serum markers HSP60, CHI3L1, and IGFBP-2 in metastatic colorectal cancer

    doi: 10.3892/ol.2019.10925

    Figure Lengend Snippet: Serum levels of CHI3L1 and IGFBP-2 in patients without pulmonary and with liver metastasis. Differences were calculated using a Mann Whitney U with Bonferroni's correction test. (A) CHI3L1 and (B) IGFBP-2 levels in patients with liver metastases ≥100

    Article Snippet: CHI3L1 (Chitinase 3-like 1, YKL-40), a highly conserved glycoprotein produced by cancer cells (including CRC cells), seems to be a new biomarker in patients with cancer ( , ).

    Techniques: MANN-WHITNEY

    Comparison of HSP60, CHI3L1 and IGFBP-2 levels in patients with CRC and healthy controls. Differences were calculated using a Mann-Whitney U test. (A) HSP60 levels, (B) CHI3L1 levels and (C) IGFBP-2 levels. *P

    Journal: Oncology Letters

    Article Title: Novel serum markers HSP60, CHI3L1, and IGFBP-2 in metastatic colorectal cancer

    doi: 10.3892/ol.2019.10925

    Figure Lengend Snippet: Comparison of HSP60, CHI3L1 and IGFBP-2 levels in patients with CRC and healthy controls. Differences were calculated using a Mann-Whitney U test. (A) HSP60 levels, (B) CHI3L1 levels and (C) IGFBP-2 levels. *P

    Article Snippet: CHI3L1 (Chitinase 3-like 1, YKL-40), a highly conserved glycoprotein produced by cancer cells (including CRC cells), seems to be a new biomarker in patients with cancer ( , ).

    Techniques: MANN-WHITNEY

    Serum levels of HSP60, CHI3L1 and IGFBP-2

    Journal: Oncology Letters

    Article Title: Novel serum markers HSP60, CHI3L1, and IGFBP-2 in metastatic colorectal cancer

    doi: 10.3892/ol.2019.10925

    Figure Lengend Snippet: Serum levels of HSP60, CHI3L1 and IGFBP-2

    Article Snippet: CHI3L1 (Chitinase 3-like 1, YKL-40), a highly conserved glycoprotein produced by cancer cells (including CRC cells), seems to be a new biomarker in patients with cancer ( , ).

    Techniques:

    Overall survival according to HSP60, CHI3L1, IGFBP-2 and CEA levels. Kaplan-Meier curves. Difference between curves was calculated by log-rank test. Kaplan-Meier curves of patient (A) HSPp60, (B) CHI3L1, (C) IGFBP-2 and (D) CEA levels. HSP60, heat shock

    Journal: Oncology Letters

    Article Title: Novel serum markers HSP60, CHI3L1, and IGFBP-2 in metastatic colorectal cancer

    doi: 10.3892/ol.2019.10925

    Figure Lengend Snippet: Overall survival according to HSP60, CHI3L1, IGFBP-2 and CEA levels. Kaplan-Meier curves. Difference between curves was calculated by log-rank test. Kaplan-Meier curves of patient (A) HSPp60, (B) CHI3L1, (C) IGFBP-2 and (D) CEA levels. HSP60, heat shock

    Article Snippet: CHI3L1 (Chitinase 3-like 1, YKL-40), a highly conserved glycoprotein produced by cancer cells (including CRC cells), seems to be a new biomarker in patients with cancer ( , ).

    Techniques:

    Receiver operator curve analysis of HSP60, CHI3L1 and IGFBP-2. The sensitivity and specificity of (A) HSP60, (B) CHI3L1 and (C) IGFBP-2 to distinguish CRC from healthy controls. HSP60, heat shock protein 60; CHI3L1, chitinase-3-like protein 1; IGFBP-2,

    Journal: Oncology Letters

    Article Title: Novel serum markers HSP60, CHI3L1, and IGFBP-2 in metastatic colorectal cancer

    doi: 10.3892/ol.2019.10925

    Figure Lengend Snippet: Receiver operator curve analysis of HSP60, CHI3L1 and IGFBP-2. The sensitivity and specificity of (A) HSP60, (B) CHI3L1 and (C) IGFBP-2 to distinguish CRC from healthy controls. HSP60, heat shock protein 60; CHI3L1, chitinase-3-like protein 1; IGFBP-2,

    Article Snippet: CHI3L1 (Chitinase 3-like 1, YKL-40), a highly conserved glycoprotein produced by cancer cells (including CRC cells), seems to be a new biomarker in patients with cancer ( , ).

    Techniques:

    (a) Bound GFP-chitinase levels and chitin levels of wild-type strain BY4742 and BY4742 Δ ygp1 and BY4742 Δ tus1 ), and equal amounts of cells based on OD measurement at 600 nm were washed and resuspended in PBS buffer before adding GFP-tagged chitinase or before staining with calcofluor white for chitin quantification. Fluorescence intensity is expressed in arbitrary units (a.u.). (b) Fold change of the deletion mutant strains relative to the wild-type strain BY4742. A correlation of 0.98 was obtained between the amount of yeast cell wall chitin and the amount of GFP-chitinase bound to the cell wall.

    Journal: Applied and Environmental Microbiology

    Article Title: Yeast Cell Wall Chitin Reduces Wine Haze Formation

    doi: 10.1128/AEM.00668-18

    Figure Lengend Snippet: (a) Bound GFP-chitinase levels and chitin levels of wild-type strain BY4742 and BY4742 Δ ygp1 and BY4742 Δ tus1 ), and equal amounts of cells based on OD measurement at 600 nm were washed and resuspended in PBS buffer before adding GFP-tagged chitinase or before staining with calcofluor white for chitin quantification. Fluorescence intensity is expressed in arbitrary units (a.u.). (b) Fold change of the deletion mutant strains relative to the wild-type strain BY4742. A correlation of 0.98 was obtained between the amount of yeast cell wall chitin and the amount of GFP-chitinase bound to the cell wall.

    Article Snippet: The chitinase assay kit (catalog no. CS0980; Sigma-Aldrich) was used to assay for the remaining chitinase activity, as per the manufacturer's instructions.

    Techniques: Staining, Fluorescence, Mutagenesis

    GFP-tagged chitinase activity from crude protein concentrate assayed in 3 different substrates suitable for exochitinase (substrate A), endochitinase (substrate B), and chitobiosidase (substrate C) activity detection supplied with the chitinase assay kit (catalog no. CS0980; Sigma-Aldrich), according to the manufacturer's instructions.

    Journal: Applied and Environmental Microbiology

    Article Title: Yeast Cell Wall Chitin Reduces Wine Haze Formation

    doi: 10.1128/AEM.00668-18

    Figure Lengend Snippet: GFP-tagged chitinase activity from crude protein concentrate assayed in 3 different substrates suitable for exochitinase (substrate A), endochitinase (substrate B), and chitobiosidase (substrate C) activity detection supplied with the chitinase assay kit (catalog no. CS0980; Sigma-Aldrich), according to the manufacturer's instructions.

    Article Snippet: The chitinase assay kit (catalog no. CS0980; Sigma-Aldrich) was used to assay for the remaining chitinase activity, as per the manufacturer's instructions.

    Techniques: Activity Assay

    (a) Chitinase activity levels of chitinase remaining in model wine solution (12% ethanol, 4 g/liter tartaric acid [pH 3.3]) not bound to the yeast cell wall after incubation with cells. (b) Chitinase activity levels of chitinase not bound to the yeast cell wall after incubation with live whole cells (L) and boiled cell wall extract (CW) from S. paradoxus and S. cerevisiae cells. Chitinase levels were quantified using the chitinase assay kit, according to the manufacturer's instructions. Commercial chitinase was used for the yeast cell wall binding assay in this experiment.

    Journal: Applied and Environmental Microbiology

    Article Title: Yeast Cell Wall Chitin Reduces Wine Haze Formation

    doi: 10.1128/AEM.00668-18

    Figure Lengend Snippet: (a) Chitinase activity levels of chitinase remaining in model wine solution (12% ethanol, 4 g/liter tartaric acid [pH 3.3]) not bound to the yeast cell wall after incubation with cells. (b) Chitinase activity levels of chitinase not bound to the yeast cell wall after incubation with live whole cells (L) and boiled cell wall extract (CW) from S. paradoxus and S. cerevisiae cells. Chitinase levels were quantified using the chitinase assay kit, according to the manufacturer's instructions. Commercial chitinase was used for the yeast cell wall binding assay in this experiment.

    Article Snippet: The chitinase assay kit (catalog no. CS0980; Sigma-Aldrich) was used to assay for the remaining chitinase activity, as per the manufacturer's instructions.

    Techniques: Activity Assay, Incubation, Binding Assay

    ), and equal amounts of cells based on the OD measurement at 600 nm were washed and resuspended in PBS buffer before adding GFP-tagged chitinase. Cells were further incubated for 2 h at room temperature with shaking before washing and resuspending in PBS buffer in preparation for quantification using a flow cytometer. Fluorescence intensity is expressed in arbitrary units (a.u.).

    Journal: Applied and Environmental Microbiology

    Article Title: Yeast Cell Wall Chitin Reduces Wine Haze Formation

    doi: 10.1128/AEM.00668-18

    Figure Lengend Snippet: ), and equal amounts of cells based on the OD measurement at 600 nm were washed and resuspended in PBS buffer before adding GFP-tagged chitinase. Cells were further incubated for 2 h at room temperature with shaking before washing and resuspending in PBS buffer in preparation for quantification using a flow cytometer. Fluorescence intensity is expressed in arbitrary units (a.u.).

    Article Snippet: The chitinase assay kit (catalog no. CS0980; Sigma-Aldrich) was used to assay for the remaining chitinase activity, as per the manufacturer's instructions.

    Techniques: Incubation, Flow Cytometry, Cytometry, Fluorescence