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Georgia Journal of Science

Article Title

E411k P-body Protein Interactions**

Abstract

Adenoviruses have contributed to significant advancements in both the medical and scientific communities by serving as a model virus to enhance our understanding of cellular biology and other DNA viruses. After entry into the host cell, adenoviruses can manipulate host cell machinery to create an ideal cellular environment to sustain viral replication, such as altering gene expression. One of the viral proteins involved in this process, E411k, facilitates the production of viral proteins over cellular proteins. It has been observed that E411k interferes with cytoplasmic processing bodies, known as p bodies, which are influential in gene expression. Some p body functions include mRNA degradation and the segregation of repressed mRNA sequences. One of the p body proteins, Pat1b, is a scaffolding protein and thus important in the formation of p-bodies. During an adenovirus infection, several p body proteins have been observed to be relocated to aggresomes. We hypothesize that E411k will disrupt the localization pattern of Pat1b during an adenovirus infection. We performed an infection without virus (mock), with wild-type virus, virus with only E411k, and virus with a deletion of E411k to determine the localization of Pat1b using immunofluorescence microscopy. We observed a significant increase in the number of cytoplasmic Pat1b foci for the wild-type and E411K-only viruses when compared to the mock, however, there was no significant difference between the E411k deletion virus and the mock. This demonstrates that E411k is necessary and sufficient for the relocalization of Pat1b to cytoplasmic foci. When observing Pat1b localization across adenovirus serotypes, we observed that Ad 5 E411k was solely capable of redistributing Pat1b. The redistribution of p body proteins observed in this study is important as it may indicate the mechanism by which E4 11k manipulates gene expression to drive viral replication.

Acknowledgements

Georgia College and State University

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