Figure 1. The repeat domain of coagulase contributes to S. aureus bloodstream infections. (A) Structure of Coa with signal sequence (S), variable D1 and D2 (prothrombin binding), linker (L), and repeat (R, fibrinogen binding) domains. The binding sites for mAbs 5D5 (blue) and 3B3 (red) are identified. (B) Secreted proteins of S. aureus Newman (wild-type) and coagulase variants were analyzed by immunoblotting with polyclonal α-Coa or α-vWbp and mAbs 5D5 or 3B3. Molecular weight markers (72 and 95 kD) are indicated. (C) Calcium-chelated mouse blood was inoculated with S. aureus strains (1 × 106 CFU) at room temperature for 24 h and coagulation was analyzed by inversion of tubes. (D and E) Mice (n = 10 per experiment) were challenged by intravenous injection with 8 × 107 CFU of S. aureus wild-type or coagulase variant strains. Data are representative of two independent analyses; (D and E) statistical significance was assessed with the log-rank test.
Figure 1.

The repeat domain of coagulase contributes to S. aureus bloodstream infections. (A) Structure of Coa with signal sequence (S), variable D1 and D2 (prothrombin binding), linker (L), and repeat (R, fibrinogen binding) domains. The binding sites for mAbs 5D5 (blue) and 3B3 (red) are identified. (B) Secreted proteins of S. aureus Newman (wild-type) and coagulase variants were analyzed by immunoblotting with polyclonal α-Coa or α-vWbp and mAbs 5D5 or 3B3. Molecular weight markers (72 and 95 kD) are indicated. (C) Calcium-chelated mouse blood was inoculated with S. aureus strains (1 × 106 CFU) at room temperature for 24 h and coagulation was analyzed by inversion of tubes. (D and E) Mice (n = 10 per experiment) were challenged by intravenous injection with 8 × 107 CFU of S. aureus wild-type or coagulase variant strains. Data are representative of two independent analyses; (D and E) statistical significance was assessed with the log-rank test.

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