Efficient Labeling of Native Human IgG by Proximity-Based Sortase-Mediated Isopeptide Ligation.

ABSTRACT: Antibody-drug conjugates (ADCs) have demonstrated great therapeutic potential due to their ability to target the delivery of potent cytotoxins. However, the heterogeneous nature of conventional drug conjugation strategies can affect the safety, efficacy, and stability of ADCs. Site-specific conjugations can resolve these issues, but often require genetic modification of Immunoglobulin G (IgG), which can impact yield or cost of production, or require undesirable chemical linkages. Here, we describe a near-traceless conjugation method that enables the efficient modification of native IgG, without the need for genetic engineering or glycan modification. This method utilizes engineered variants of sortase A to catalyze noncanonical isopeptide ligation. Sortase A was fused to an antibody-bindin

SUBMITTER: Yu W 

PROVIDER: S-EPMC8643073 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature