Journal
PROTEIN ENGINEERING DESIGN & SELECTION
Volume 23, Issue 4, Pages 221-228Publisher
OXFORD UNIV PRESS
DOI: 10.1093/protein/gzp077
Keywords
bispecific antibody; IgG fusion; pretargeted radioimmunotherapy; single chain variable fragment
Funding
- National Institutes of Health [RO1-CA-101830]
- National Science Foundation Graduate Research Fellowship
Ask authors/readers for more resources
Here we present a bispecific antibody (bsAb) format in which a disulfide-stabilized scFv is fused to the C-terminus of the light chain of an IgG to create an IgG-scFv bifunctional antibody. When expressed in mammalian cells and purified by one-step protein A chromatography, the bsAb retains parental affinities of each binding domain, exhibits IgG-like stability and demonstrates in vivo IgG-like tumor targeting and blood clearance. The extension of the C-terminus of the light chain of an IgG with an scFv or even a smaller peptide does appear to disrupt disulfide bond formation between the light and heavy chains; however, this does not appear to affect binding, stability or in vivo properties of the IgG. Thus, we demonstrate here that the light chain of an IgG can be extended with an scFv without affecting IgG function and stability. This format serves as a standardized platform for the construction of functional bsAbs.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available