Fig. 1

Isolation of crossreactive antibodies toward multiple ELR⁺ CXC chemokines. a Heat map displaying the sequence identity among multiple human and murine ELR⁺ CXC chemokines. The color of each element in the heat map indicates the sequence identity percentage, ranging from 10% (white) to 100% (dark blue). “h” and “m” indicates human and murine CXC chemokines, respectively. b Schematic representation of the iterative selection pathways applied to isolate crossreactive molecules from a naïve library of synthetic antibodies displayed on the surface of yeast. Two cycles of magnetic bead screening followed by four cycles of flow cytometry sorting were applied. c Plot of the binding affinities of 18 unique yeast-displayed synthetic antibody protein binders (CK) selected using six diverse human (hCXCL1, hCXCL5, and hCXCL8) and murine (mCXCL1, mCXCL2, and mCXCL5) ELR⁺ CXC chemokine ligands. Each chemokine and its corresponding binding affinity values are reported as differently colored filled circles and indicate the means of at least three independent experiments. Data are presented as inverse equilibrium binding constants (1/K_D; M⁻¹)