Fig. 2

Protein structure and antibody formation pathway of the tetravalent bispecific AFM13 antibody. The CD16A (domain A, diamond shape) and CD30 (domain B, oval shape) peptide domains were linked by a 9-amino acid linker (L) to form a single polypeptide (nonfunctional monomer). A fully functional tetravalent bispecific chimeric antibody construct (TandAb) is formed by homodimerization of the single polypeptide monomer in a head-to-tail fashion through non-covalent interactions (dotted lines) of the domains in the Ig heavy (V _H) and light (V _L) variable chains. The AFM13 TandAb has a molecular weight of approximately 104 kDa. This figure was modified from Rothe et al. and Reusch et al. [22, 27]