Apoptin, Chicken Anemia Virus VP3, selectively induces apoptosis in transformed cells but not primary cells. In all cases, Apoptin undergoes nucleocytoplasmic shuttling, but partitions into the nucleus of transformed cells and the cytoplasm of primary cells. The N-terminal NES of Apoptin and the domain for multimerization overlap and all previous attempts to uncouple these activities have failed. In this study, we successfully uncoupled nuclear export and multimerization through site-directed mutagenesis of ApI37A and ApI40A. Uncoupling these activities and studying them independently could shed insight into basic biochemical differences between transformed and primary cells that could be exploited for targeted therapeutic purposes.
Worcester Polytechnic Institute
Major Qualifying Project
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Chemistry and Biochemistry