Fig. 13

The most likely binding conformation between the CDR1–3 area on K9RABVscFv16 and the antigenic sites on RABV-G was predicted by the HADDOCK 2.4 web server. (a) Surface display structures of RABV-G with residues on antigenic sites that interact with (b) residues on the CDR of K9RABVscFv1. The numbers in brackets “()” in the RABV-G labels refer to the positions without 19 amino acids in the signal sequence. (c) Interactions between the residues on the CDR of K9RABVscFv1 and the antigenic sites of RABV-G on the basis of the results in Table 3. The sticks display the amino acid residues on the CDR (A chain) that interact with the residues on the antigenic sites of RABV-G (B chain). Significant interactions are shown in panels (c1) and (c2). The VH chain, VL chain, G/S linker, CDR1–3 VH, CDR1–3 VL, antigenic major sites I, II, III, IV, and G5, and minor site G1 (or “a”) are shown in different colors.