Membrane fusion is key to organism homeostasis and occurs when a transport vesicle fuses with a target compartment, merging the two membranes into one while releasing the contents of the transport vesicle into the target compartment. This process is controlled by SNARE proteins. Syntaxin-17 protein plays a crucial role in the fusion of the autophagosome membrane with the lysosome membrane, allowing for degradation of misfolded intracellular components and pathogens. Intriguingly, Syntaxin 17 has been identified as a target of herpesvirus tegument proteins, although the pathological significance of the Syntaxin 17 and tegument protein interaction is unclear. As a first step towards characterizing the biochemical and functional interaction between the tegument proteins and the target SNARE, this study aimed to amplify and introduce the Syntaxin 17 cDNA into a model E. coli for production and purification of Syntaxin 17 protein. Amplified insert and vector cDNA of the correct size were obtained and verified via gel electrophoresis. Future research should focus on the transformation of the chimeric plasmid into competent E. coli. If isolates with the correct size insert were obtained, the next steps would be sequencing to confirm absence of mutation and procee