Discipline: Biological Sciences
Subcategory: Biochemistry (not Cell and Molecular Biology and Genetics)
Alyssa Paparella - Sarah Lawrence College
Co-Author(s): Rebecca DiBona, University of Delaware; Christine Banos, University of Delaware; Zhihao Zhuang, University of Delaware
ISG15 (interferon stimulated gene) is a ubiquitin-like protein that has implications in antiviral immunity and cancer, but much is still unknown regarding its function in cells. The structure consists of two ubiquitin-like domains with approximately 30% sequence homology to ubiquitin and a connecting linker region between the two domains, with the mature and processed form of ISG15 weighing 15 kDa (1). To interact with other proteins, ISG15 can undergo ISGylation, which is accomplished through conjugation with E1, E2, and E3 enzymes or it can act as a free protein. As a free protein, it can be found either intracellularly or extracellularly. Since little is known about the free protein’s function, it is important to explore what cellular pathways include ISG15. To accomplish this task, we hypothesized and developed an ISG15-specific probe to investigate cellular functions. Results confirmed the efficacy and purification of probe generation, facilitating future analysis of ISG15-dependent pathways and functions.
Funder Acknowledgement(s): The research for my participation in the project was funded through the Research Experience for Undergraduates through the National Science Foundation.
Faculty Advisor: Zhihao Zhuang, firstname.lastname@example.org
Role: For the project, I was responsible for making the specific L10 probe, which is the focus of my poster. For this, I did the small scale growth overnight, the large scale growth, sanitation to lyse the cells and confirmed the purity through multiple analyses, such as the using of a Chitin Column, protein gel, FPLC, and Mass Spectrometry.