Fig. 2

Hemolytic activity of the C-terminal (HrpA-C) and middle (HrpA-M) region of HrpA and in silico interaction between HrpA-C and Mn²⁺ ion. A Hemolytic activity of HrpA-C and HrpA-M against human erythrocytes was assayed either in the absence or in the presence of different amounts (0–10 mM) of MgCl₂, MnCl₂, CoCl₂, CuCl₂, ZnCl₂, CaCl₂, FeCl₂, or NiCl₂. All data shown in the histogram plot were normalized with respect to their corresponding negative control. The data in the histogram are presented as means ± S.D. of at least three independent experiments done in triplicates. B In silico interaction between HrpA-C and Mn²⁺ ion was modeled using the Metal Ion-Binding site prediction and docking server (MIB). Binding residues, template proteins, and score are reported. Putative Mn²⁺ binding sites of HrpA-C were mapped and visualized by Chimera (bottom)