M1 protein affects fibrin clot fibrinolytic potential. Fibrinolytic potential of fibrin clots was measured using (B,D) a microtiter plate assay and (A,C) ROTEM analysis. (C,D) Whole blood was activated with tissue factor, whereas (A,B) purified clots were activated with thrombin. The lysis time was then derived from the (A,C) ROTEM TEMogram or presented as (B,D) time to reach 100% lysis in the microtiter assays. (D) Halo assay; (B) purified turbidity assay. Plasminogen activation activity of (E) bacterial and host, (F) tPA, and (G) uPA plasminogen activators was measured in the presence of rM1 protein (0-30 μg/mL) using a chromogenic solution assay against S2251 (n ≥ 4). Error bars represent standard error of the mean. (∗P < .05, ∗∗P < .01, ∗∗∗P < .001, ∗∗∗∗P < .0001, 1-way ANOVA with Dunnett post hoc test). LT, lysis time; SK, streptokinase; tPA, tissue-type plasminogen activator; uPA, urokinase-type plasminogen activator.
Figure 5.

M1 protein affects fibrin clot fibrinolytic potential. Fibrinolytic potential of fibrin clots was measured using (B,D) a microtiter plate assay and (A,C) ROTEM analysis. (C,D) Whole blood was activated with tissue factor, whereas (A,B) purified clots were activated with thrombin. The lysis time was then derived from the (A,C) ROTEM TEMogram or presented as (B,D) time to reach 100% lysis in the microtiter assays. (D) Halo assay; (B) purified turbidity assay. Plasminogen activation activity of (E) bacterial and host, (F) tPA, and (G) uPA plasminogen activators was measured in the presence of rM1 protein (0-30 μg/mL) using a chromogenic solution assay against S2251 (n ≥ 4). Error bars represent standard error of the mean. (∗P < .05, ∗∗P < .01, ∗∗∗P < .001, ∗∗∗∗P < .0001, 1-way ANOVA with Dunnett post hoc test). LT, lysis time; SK, streptokinase; tPA, tissue-type plasminogen activator; uPA, urokinase-type plasminogen activator.

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