Generation of Protease Inhibitory Antibodies by Functional In Vivo Selection

Authors

Ki Baek Lee
Xin Ge

Language

English

Publication Date

1-1-2024

Journal

Methods in Molecular Biology

DOI

10.1007/978-1-0716-3589-6_19

PMID

38038945

PMCID

PMC10732120

PubMedCentral® Posted Date

1-1-2024

PubMedCentral® Full Text Version

Author MSS

Abstract

Targeting dysregulated protease expression and/or abnormal substrate proteolysis, highly selective inhibition of pathogenic proteases by monoclonal antibodies (mAbs) presents an attractive therapeutic approach for the treatment of diseases including cancer. Herein, we report a functional selection method for protease inhibitory mAbs by periplasmic co-expression of three recombinant proteins-a protease of interest, an antibody Fab library, and a modified β-lactamase TEM-1. We validate this approach by isolation of highly selective and potent mAbs inhibiting human matrix metalloproteinase 9 (MMP9).

Keywords

Humans, Peptide Hydrolases, Matrix Metalloproteinase Inhibitors, Antibodies, Monoclonal, Endopeptidases, Proteolysis, : Inhibitory antibody, Functional selection, Matrix metalloproteinase

Published Open-Access

yes

Recommended Citation

Ki Baek Lee and Xin Ge, "Generation of Protease Inhibitory Antibodies by Functional In Vivo Selection" (2024). Faculty, Staff and Student Publications. 3388.
https://digitalcommons.library.tmc.edu/uthmed_docs/3388