Fig. 2

Multiple sequence alignment of M.tb PpiB in biofilm forming bacteria and interaction of PpiB with cyclosporine-A, acarbose and GaNP. a M.tb PpiB (Rv2582) exhibits homology with proteins from other biofilm forming bacteria and possesses similar amino acids Arg and Pro at the binding site of cyclosporine-A (highlighted in green box) and acarbose (highlighted in red box), respectively. A dimer of atomic gallium¹⁷ similarly binds to Gly residue (highlighted in black box), which is conserved within the PpiB binding site of all biofilm-forming bacteria. b, d, f Interaction of cyclosporine-A, acarbose and dimer of atomic gallium with PpiB was tested by molecular docking analysis. b The docked complex of cyclosporine-A and PpiB. The protein (pink) is shown in surface view whereas interacting residues (grey) and ligand (green) is represented in stick model. Hydrogen bond (yellow) is shown in dotted lines. d Interactions of PpiB with acarbose showing various hydrogen and hydrophobic interactions. f The docked complex of dimer of atomic gallium and PpiB. The protein (pink) is shown in surface view whereas interacting residues (green) and ligand (red) is represented in stick model. Hydrogen bond (black) is shown in dotted lines. c, e, g SPR analysis was performed as described in methods. Response units (RU) of the interaction of PpiB with cyclosporine-A (c) or acrabose e, or GaNP g from representative experiment are shown