Engineered antibodies used in immunotherapies have been increasingly successful due to their ability to uniquely target cell expressing specific cancer antigens. Thymidine Kinase 1 (TK1) is a DNA salvage enzyme typically found in the cytosol. However, in certain types of cancer, TK1 is surface expressed, making it a unique cancer biomarker. By identifying antibodies with a high binding affinity for TK1, we can target cancer cells expressing TK1 on their surface. Using cell sorting and a yeast display library expressing 109 human single chain antibody fragments, we have isolated ten unique single-chain antibodies (scFvs) that bind to TK1. Flow cytometry affinity characterization of the 10 clones revealed strong binding affinity in the low nM range. Sequencing of the scFvs showed they all had unique complementarity-determining regions (CDRs) with some similarities among the clones. The scFvs were cloned into constructs containing an antibody constant domain and they will be cultured with cancer cell lines expressing TK1 and evaluated for antibody-dependent cellular cytotoxicity. This research has the potential to target TK1+ cancers and maximize cancer cell death while minimizing harm to healthy cells.
University / Institution: Brigham Young University
Format: In Person
SESSION B (10:45AM-12:15PM)
Area of Research: Health & Medicine
Faculty Mentor: Scott Weber
Location: Union Building, PANORAMA EAST (10:45am)