Using a Chimeric Protein to Explore Conservation in Herpesvirus-1 Protein ICP-27
Abstract Herpesvirus 1 is a common human pathogenic that is estimated to have infected almost half of the world’s population. While it typically manifests as harmless cold sores, it can cause severe symptoms and fatalities in cases involving immunodeficient individuals and in neonates. It also serves as an important model for DNA virus replication. As a DNA virus, HSV-1 DNA enters the nucleus, where mRNA is transcribed. Many HSV-1 mRNAs lack splice sites; as a result, they are not efficiently exported by the host cell machinery. ICP27 is an HSV-1 protein that aids in the export of viral mRNA out of the nucleus and has homologs across the herpesvirus family. This study aims to investigate the function of the C-terminal domain of the protein by studying a chimeric protein that contains the WT N-terminal domain and a C-terminal domain from ORF4, the ICP27 homolog in varicella zoster virus. This has necessitated cloning of a eukaryotic expression plasmid containing a gene encoding this plasmid, which has so far been unsuccessful. This study will therefore summarize the methods used so far to attempt to clone this plasmid, as well as plans for future experiments once cloning is successful.