Affinity Maturation for Antibody Engineering: The Critical Role of Residues on CDR Loops of Antibodies in Antigen Binding.

ABSTRACT: During the course of affinity maturation, antibodies exhibit enhanced antigen-binding affinities by altering the amino acids in their variable regions. Understanding the structural basis of these antibodies can be beneficial for antibody engineering. We determined the crystal structures of single-chain Fv (scFv) antibodies against (4-hydroxy-3-nitrophenyl)acetyl, C6 and E11, which had undergone affinity maturation. Compared with germline-type antibodies, the affinity-matured antibodies with somatic hypermutation from Lys58 to Arg58 of the heavy chain located in the complementarity-determining region 2 (CDR2) seemed to be critical for increasing the antigen-binding affinity. E11 possessed a disulfide bond at the base of CDR3 in the heavy chain, which contributed to a further increase in its

SUBMITTER: Yoshida M 

PROVIDER: S-EPMC11819675 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature