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Extensive Sequence and Structural Evolution of Inhibitory Antibodies to Arginase2 Enabled by an Unbiased Approach to Affinity Maturation

Stuart describes a novel antibody optimization strategy that seeks to overcome the restrictive nature of existing affinity maturation methods, by rapidly exploring a vast sequence space in an unbiased manner through novel application of PCR techniques and ribosome display. He exemplified the significance of this method by contrasting the crystal structure of the parent and optimized antibodies bound to ARG2, which revealed a striking reorientation of the binding paratope, concurrent with distinct improvements in inhibitory potency and binding properties. The nature and magnitude of the epitope expansion were extraordinary and unlikely to have been produced through conventional affinity maturation methods. This innovative approach demonstrates broad applicability to the optimization