FIG 1.
Biochemical characterization of the MAb 4.2 scFv interaction with LIV E/TBEV E. (A) Analytical gel filtration profile of MAb 4.2 scFv and LIV E. MAb 4.2 scFv and LIV E proteins eluted as single monomer peaks in the gel filtration curves. The complex of MAb 4.2 scFv bound to LIV E displayed a shifted complex peak with an extra MAb 4.2 scFv peak. (B) SPR of MAb 4.2 scFv binding to LIV E. (C) Analytical gel filtration profile of MAb 4.2 scFv and TBEV E. (D) SPR of MAb 4.2 scFv bound to TBEV E. All data show that MAb 4.2 binds to both the LIV and TBEV E proteins. In panels A and C, the protein peaks are pointed out with arrows, red rectangles indicate the lanes with the complex peak, and lanes M contain molecular mass markers. mAU, milli-absorbance units; KD, equilibrium dissociation constant.