Mutagenesis of the VP16 protein of the Herpes Simplex Virus

carrollscholars.legacy.contextkey11097391
carrollscholars.legacy.itemurlhttps://scholars.carroll.edu/lifesci_theses/80
carrollscholars.object.degreeBachelor's
carrollscholars.object.departmentLife & Environmental Sciences
carrollscholars.object.disciplinesLife Sciences; Virology
carrollscholars.object.seasonSpring
dc.contributor.advisorMarilyn Schendel
dc.contributor.advisorJohn Addis
dc.contributor.advisorSteven Triezenberg
dc.contributor.authorSpiger, Benjamin
dc.date.accessioned2020-04-30T10:00:31Z
dc.date.available2020-04-30T10:00:31Z
dc.date.embargo12/31/1899 0:00
dc.date.issued2000-04-01
dc.description.abstractThe herpes simplex virus (HSV-1) encodes a trans-activator protein VP16. VP16 activates the immediate early genes (IE) of the viral genome during lytic infection. VP16 has been heavily studied by mutational analysis as a model for transcriptional activation. The goal of this project was to examine two specific aspects of VP16. First, to compare the properties of a previously constructed insertion mutant, in1814, to other mutant strains constructed in our laboratory; this insertion was moved from strain 17 of HSV-1 into the KOS strain, the strain used in our lab. The second aspect of this examination is a mutational analysis of a possible cryptic N-terminal activation domain. To assess whether this region contributes to transcriptional activation of the IE genes, deletion mutants were constructed in the N terminus of VP16, with or without the deletion of the Cterminal activation domain. The constructed viruses will be verified for the proper mutations, before the properties of these viruses are characterized.
dc.identifier.urihttps://scholars.carroll.edu/handle/20.500.12647/2823
dc.subjectherpes simplex, virus
dc.titleMutagenesis of the VP16 protein of the Herpes Simplex Virus
dc.typethesis
Files
Original bundle
Now showing 1 - 1 of 1
Loading...
Thumbnail Image
Name:
2000_SpigerB_THS_000211.pdf
Size:
2.08 MB
Format:
Adobe Portable Document Format