7th grader Hannah Karlin received a First Place award at the Northern Regional Science & Engineering Fair in the Behavior and Social Science category.
8th grader Sophia Anderson received a First Place award at the Northern Regional Science & Engineering Fair in the Environmental category.
Biruktawit Assefa, 11th grader, won the Best in Fair Grand Prize at the Northern Regional Science & Engineering Fair for her project Mapping Phosphorylation Sites Necessary for Large T-antigen Stability through PCR-based Mutagenesis. Birdy will compete at the State Science Fair, April 5-6 at Virginia Military Institute and at the International Science and Engineering Fair in Phoenix, AZ, May 12-17. At the Regional Fair, Birdy was also awarded 1st Place, Certificate of Merit & $100 from the Biophysical Society and 1st Place, Certificate of Excellence, $150, & a one-year subscription to Technology Review Magazine from the MIT Club of Washington, DC. Birdy presented her paper at the 2013 Junior Science & Humanities Symposium, held at Georgetown University in January.
Her abstract: In 2008, it was discovered that Merkel cell polyomavirus (MCV) is the main culprit behind 80% of metastatic Merkel cell carcinoma. Evidence has shown that MCV encodes for a protein called large T antigen which is essential for normal viral replication. Thus, large T antigen has been the subject of many studies. This project describes the phosphorylization sites and motifs necessary for large T antigen stability and function. DNA mapping was utilized to gain a relative idea of the locations of said phosphorylation sites. Next,mutagenesis was performed on four different motifs that contain the majority of the phosphorylation sites on the large T-antigen to isolate their functions. A truncation mutation was executed on three different sites on said oncoprotein to locate the motif necessary for large T-antigen stabilization. The resulting truncation were 516 base pairs, 390 base pairs, and 345 base pairs. These inserts were ligated into vectors 1038 and 2956. These were then expressed in kidney tumor cells and in turn, the protein expressions were analyzed through a western blot. Identifying the phosphorylation sites of large T antigen could lead to a better understanding of the viral protein and in turn a better way to combat it. Furthermore, protein stability is essential for protein expression.Instability of proteins can lead to degradation. Therefore, an improved idea of the phosphorylation sites and the motifs responsible for large T antigenstability and correct function could lead to locating a possible target for therapeutic drugs. Additionally, it will help pinpoint weaknesses in the cellular mechanism as whole.