Virus Protein Biochemistry - Gyv9/Tu789

Plankey, Eva; Caten, Megan

Student Work

Virus Protein Biochemistry - Gyv9/Tu789

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The protein structure-function paradigm underlines the importance of a protein’s structure in understanding its functional capabilities and mechanisms of interaction. Apoptin, the third viral protein of the gyrovirus chicken anemia virus (CAV), can selectively target and induce apoptosis in cancer cells, yet its mechanisms of interactions are not fully understood. Efforts to characterize the protein have proven difficult due to an apparent lack of stable secondary and tertiary structures present within. This phenomenon--intrinsic disorder-- makes studying proteins like apoptin difficult in the context of conventional characterization methods. Studying homologs is an effective method for understanding how apoptin functions. Two novel homologs, Tu789 and GyV9, were recently identified and are suspected to behave similarly to apoptin. Yet, further characterization is required to assess if their third viral protein regions truly possess functional similarity. Via the input from several artificial intelligence (AI) and homology-based prediction models, robust experiments with a narrow focus were created. The culmination of these prediction results combined with experimental procedures allowed for Tu789 and GyV9 to be characterized as structural homologs to apoptin due to their strong structural similarities but lack of independent functional localization means they cannot be classified as functional homologs.. This has prompted questions regarding apoptin’s ability to aid in multimerization for these proteins and relocalize them with a potential reliance on a beta-sheet structure in the middle regions of the proteins.

This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

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