Novel CH1:CL interfaces that enhance correct light chain pairing in heterodimeric bispecific antibodies.

ABSTRACT: Targeting two unique antigens with a single bispecific antibody is an attractive approach with potential broad therapeutic applicability. However, the production of heterodimeric bispecific antibodies (bsAbs) presents a challenge, requiring the co-expression and accurate pairing of two distinct heavy and light chain units. Several undesirable by-products can be formed in the production process, including heavy chain homodimers and non-cognate light chain pairings. Although additional downstream purification methods exist, they are often time consuming and restrict practical large-scale production. In this study, we identify and validate novel Fab interface mutations that increase cognate light chain pairing efficiencies within heterodimeric bsAbs. Importantly, the variable domains remain u

SUBMITTER: Bonisch M 

PROVIDER: S-EPMC5914326 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature