The porcine circovirus type 2 viral protein 3 (VP3) and its homolog, the chicken anemia virus protein Apoptin, have been shown to induce p53 independent apoptosis in transformed cells. The present study investigated VP3’s ability to multimerize and associate with the anaphase promoting complex/cylcosome’s (APC/C) subunit 1 similar to Apoptin. A novel FRET technique involving GFP and DsRed fluorophores was successful in demonstrating Apoptin multimerization and provides way to explore VP3’s multimeric capability. In addition, FLAG-tagged VP3 2A and 2B constructs were created for future immunoprecipitation studies of VP3 multimerization and association with the APC/C subunit 1. Understanding such mechanisms may have implications for VP3's candidacy as a cancer therapeutic.
Worcester Polytechnic Institute
Major Qualifying Project
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Chemistry and Biochemistry