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A Binding <t>of</t> <t>glu-plasminogen</t> to purified borrelial proteins was determined by ELISA. Chi proteins, HcpA and BBA70 (positive controls) or Vsp1 and BSA (negative control) (5 ng/µl each) were immobilized and incubated with 10 ng/µ glu-plasminogen. Protein-protein complexes were detected by using a polyclonal anti-plasminogen antibody (1:1000). Data of at least ten technical replicates ( n = 10, mean, ±SD) were shown and compared with BSA as negative control. ** p ≤ 0.01, **** p ≤ 0.0001, n.s., no statistical significance, one-way ANOVA with post-hoc Bonferroni multiple comparison test. B – F Dose-dependent binding of glu-plasminogen to three selected Chi proteins. Purified ChiA ( B ), ChiB ( C ), ChiC ( D ), and ChiD ( E ), ChiE ( F ) (5 ng/µl each) were immobilized and incubated with increasing concentrations of glu-plasminogen (0.5 to 2 µM). Binding curve and dissociation constant were calculated via non-linear regression, four-parameter model. Data of three technical replicates ( n = 3, mean, ±SD) are shown. G Degradation of C3b by activated plasminogen bound to Chi proteins. Proteins (10 ng/µl each) immobilized were incubated with plasminogen (10 ng/µl). Thereafter, uPA (25 ng/µl) and C3b (20 ng/µl) were added and C3b degradation products were visualized by Western blotting using a polyclonal anti-C3 antibody (1:1000). n.a., not available. Source data are provided as a Source data file.
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A Binding <t>of</t> <t>glu-plasminogen</t> to purified borrelial proteins was determined by ELISA. Chi proteins, HcpA and BBA70 (positive controls) or Vsp1 and BSA (negative control) (5 ng/µl each) were immobilized and incubated with 10 ng/µ glu-plasminogen. Protein-protein complexes were detected by using a polyclonal anti-plasminogen antibody (1:1000). Data of at least ten technical replicates ( n = 10, mean, ±SD) were shown and compared with BSA as negative control. ** p ≤ 0.01, **** p ≤ 0.0001, n.s., no statistical significance, one-way ANOVA with post-hoc Bonferroni multiple comparison test. B – F Dose-dependent binding of glu-plasminogen to three selected Chi proteins. Purified ChiA ( B ), ChiB ( C ), ChiC ( D ), and ChiD ( E ), ChiE ( F ) (5 ng/µl each) were immobilized and incubated with increasing concentrations of glu-plasminogen (0.5 to 2 µM). Binding curve and dissociation constant were calculated via non-linear regression, four-parameter model. Data of three technical replicates ( n = 3, mean, ±SD) are shown. G Degradation of C3b by activated plasminogen bound to Chi proteins. Proteins (10 ng/µl each) immobilized were incubated with plasminogen (10 ng/µl). Thereafter, uPA (25 ng/µl) and C3b (20 ng/µl) were added and C3b degradation products were visualized by Western blotting using a polyclonal anti-C3 antibody (1:1000). n.a., not available. Source data are provided as a Source data file.
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A Binding <t>of</t> <t>glu-plasminogen</t> to purified borrelial proteins was determined by ELISA. Chi proteins, HcpA and BBA70 (positive controls) or Vsp1 and BSA (negative control) (5 ng/µl each) were immobilized and incubated with 10 ng/µ glu-plasminogen. Protein-protein complexes were detected by using a polyclonal anti-plasminogen antibody (1:1000). Data of at least ten technical replicates ( n = 10, mean, ±SD) were shown and compared with BSA as negative control. ** p ≤ 0.01, **** p ≤ 0.0001, n.s., no statistical significance, one-way ANOVA with post-hoc Bonferroni multiple comparison test. B – F Dose-dependent binding of glu-plasminogen to three selected Chi proteins. Purified ChiA ( B ), ChiB ( C ), ChiC ( D ), and ChiD ( E ), ChiE ( F ) (5 ng/µl each) were immobilized and incubated with increasing concentrations of glu-plasminogen (0.5 to 2 µM). Binding curve and dissociation constant were calculated via non-linear regression, four-parameter model. Data of three technical replicates ( n = 3, mean, ±SD) are shown. G Degradation of C3b by activated plasminogen bound to Chi proteins. Proteins (10 ng/µl each) immobilized were incubated with plasminogen (10 ng/µl). Thereafter, uPA (25 ng/µl) and C3b (20 ng/µl) were added and C3b degradation products were visualized by Western blotting using a polyclonal anti-C3 antibody (1:1000). n.a., not available. Source data are provided as a Source data file.
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A Binding <t>of</t> <t>glu-plasminogen</t> to purified borrelial proteins was determined by ELISA. Chi proteins, HcpA and BBA70 (positive controls) or Vsp1 and BSA (negative control) (5 ng/µl each) were immobilized and incubated with 10 ng/µ glu-plasminogen. Protein-protein complexes were detected by using a polyclonal anti-plasminogen antibody (1:1000). Data of at least ten technical replicates ( n = 10, mean, ±SD) were shown and compared with BSA as negative control. ** p ≤ 0.01, **** p ≤ 0.0001, n.s., no statistical significance, one-way ANOVA with post-hoc Bonferroni multiple comparison test. B – F Dose-dependent binding of glu-plasminogen to three selected Chi proteins. Purified ChiA ( B ), ChiB ( C ), ChiC ( D ), and ChiD ( E ), ChiE ( F ) (5 ng/µl each) were immobilized and incubated with increasing concentrations of glu-plasminogen (0.5 to 2 µM). Binding curve and dissociation constant were calculated via non-linear regression, four-parameter model. Data of three technical replicates ( n = 3, mean, ±SD) are shown. G Degradation of C3b by activated plasminogen bound to Chi proteins. Proteins (10 ng/µl each) immobilized were incubated with plasminogen (10 ng/µl). Thereafter, uPA (25 ng/µl) and C3b (20 ng/µl) were added and C3b degradation products were visualized by Western blotting using a polyclonal anti-C3 antibody (1:1000). n.a., not available. Source data are provided as a Source data file.
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A Binding <t>of</t> <t>glu-plasminogen</t> to purified borrelial proteins was determined by ELISA. Chi proteins, HcpA and BBA70 (positive controls) or Vsp1 and BSA (negative control) (5 ng/µl each) were immobilized and incubated with 10 ng/µ glu-plasminogen. Protein-protein complexes were detected by using a polyclonal anti-plasminogen antibody (1:1000). Data of at least ten technical replicates ( n = 10, mean, ±SD) were shown and compared with BSA as negative control. ** p ≤ 0.01, **** p ≤ 0.0001, n.s., no statistical significance, one-way ANOVA with post-hoc Bonferroni multiple comparison test. B – F Dose-dependent binding of glu-plasminogen to three selected Chi proteins. Purified ChiA ( B ), ChiB ( C ), ChiC ( D ), and ChiD ( E ), ChiE ( F ) (5 ng/µl each) were immobilized and incubated with increasing concentrations of glu-plasminogen (0.5 to 2 µM). Binding curve and dissociation constant were calculated via non-linear regression, four-parameter model. Data of three technical replicates ( n = 3, mean, ±SD) are shown. G Degradation of C3b by activated plasminogen bound to Chi proteins. Proteins (10 ng/µl each) immobilized were incubated with plasminogen (10 ng/µl). Thereafter, uPA (25 ng/µl) and C3b (20 ng/µl) were added and C3b degradation products were visualized by Western blotting using a polyclonal anti-C3 antibody (1:1000). n.a., not available. Source data are provided as a Source data file.
Human Pai 1 Sandwich Elisa Kit, supplied by Elabscience Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


A Binding of glu-plasminogen to purified borrelial proteins was determined by ELISA. Chi proteins, HcpA and BBA70 (positive controls) or Vsp1 and BSA (negative control) (5 ng/µl each) were immobilized and incubated with 10 ng/µ glu-plasminogen. Protein-protein complexes were detected by using a polyclonal anti-plasminogen antibody (1:1000). Data of at least ten technical replicates ( n = 10, mean, ±SD) were shown and compared with BSA as negative control. ** p ≤ 0.01, **** p ≤ 0.0001, n.s., no statistical significance, one-way ANOVA with post-hoc Bonferroni multiple comparison test. B – F Dose-dependent binding of glu-plasminogen to three selected Chi proteins. Purified ChiA ( B ), ChiB ( C ), ChiC ( D ), and ChiD ( E ), ChiE ( F ) (5 ng/µl each) were immobilized and incubated with increasing concentrations of glu-plasminogen (0.5 to 2 µM). Binding curve and dissociation constant were calculated via non-linear regression, four-parameter model. Data of three technical replicates ( n = 3, mean, ±SD) are shown. G Degradation of C3b by activated plasminogen bound to Chi proteins. Proteins (10 ng/µl each) immobilized were incubated with plasminogen (10 ng/µl). Thereafter, uPA (25 ng/µl) and C3b (20 ng/µl) were added and C3b degradation products were visualized by Western blotting using a polyclonal anti-C3 antibody (1:1000). n.a., not available. Source data are provided as a Source data file.

Journal: Nature Communications

Article Title: Complement inhibition by a unique cluster of immunomodulatory outer surface proteins of Borrelia recurrentis

doi: 10.1038/s41467-026-72359-y

Figure Lengend Snippet: A Binding of glu-plasminogen to purified borrelial proteins was determined by ELISA. Chi proteins, HcpA and BBA70 (positive controls) or Vsp1 and BSA (negative control) (5 ng/µl each) were immobilized and incubated with 10 ng/µ glu-plasminogen. Protein-protein complexes were detected by using a polyclonal anti-plasminogen antibody (1:1000). Data of at least ten technical replicates ( n = 10, mean, ±SD) were shown and compared with BSA as negative control. ** p ≤ 0.01, **** p ≤ 0.0001, n.s., no statistical significance, one-way ANOVA with post-hoc Bonferroni multiple comparison test. B – F Dose-dependent binding of glu-plasminogen to three selected Chi proteins. Purified ChiA ( B ), ChiB ( C ), ChiC ( D ), and ChiD ( E ), ChiE ( F ) (5 ng/µl each) were immobilized and incubated with increasing concentrations of glu-plasminogen (0.5 to 2 µM). Binding curve and dissociation constant were calculated via non-linear regression, four-parameter model. Data of three technical replicates ( n = 3, mean, ±SD) are shown. G Degradation of C3b by activated plasminogen bound to Chi proteins. Proteins (10 ng/µl each) immobilized were incubated with plasminogen (10 ng/µl). Thereafter, uPA (25 ng/µl) and C3b (20 ng/µl) were added and C3b degradation products were visualized by Western blotting using a polyclonal anti-C3 antibody (1:1000). n.a., not available. Source data are provided as a Source data file.

Article Snippet: Human glu-plasminogen was purchased from Prolytix (Essex Junction, VT, USA).

Techniques: Binding Assay, Purification, Enzyme-linked Immunosorbent Assay, Negative Control, Incubation, Comparison, Western Blot