Show simple item record

dc.contributor.authorBratton, Kristin
dc.creatorBratton, Kristinen_US
dc.date.accessioned2012-09-13T18:23:35Z
dc.date.available2012-09-13T18:23:35Z
dc.date.issued2012-05
dc.identifier.urihttp://hdl.handle.net/10150/243893
dc.description.abstractThe early stages of Human Papillomavirus infection proceeds through a series of steps that involve interactions between cell surface molecules and viral capsid proteins. While the role of viral protein L1 in internalization of the virus has been well characterized, the role of minor capsid protein L2 in internalization and infection is less clear. However, cleavage of L2 by furin, a proprotein convertase, and the resulting exposure of an N-terminal region, the RG-1 epitope, has been shown to be a critical step in infection. In this study, we aimed to explicitly show furin cleavage during infection and identify the cellular conditions required for this cleavage event and establishment of infection. An assay to detect furin cleavage of L2 was developed, and for the first time, furin cleavage was directly shown during infection. In vivo data suggests that cyclophilin B, a peptidyl-prolyl isomerase believed to playa role in the conformational changes that occur prior to internalization, may playa less prominent role than previously thought. Understanding the role of L2 in entry and infection provides a more comprehensive picture of the mechanism of papillomavirus infection and exposure of the RG-1 epitope, the major target for next-generation broadly protective pan-HPV vaccines.
dc.language.isoenen_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.titleThe Role of Furin Cleavage in Human Papillomavirus Infectionen_US
dc.typetexten_US
dc.typeElectronic Thesisen_US
thesis.degree.grantorUniversity of Arizonaen_US
thesis.degree.levelbachelorsen_US
thesis.degree.disciplineHonors Collegeen_US
thesis.degree.disciplineBiochemistry and Molecular Biophysicsen_US
thesis.degree.nameB.S.en_US
refterms.dateFOA2018-04-26T16:12:07Z
html.description.abstractThe early stages of Human Papillomavirus infection proceeds through a series of steps that involve interactions between cell surface molecules and viral capsid proteins. While the role of viral protein L1 in internalization of the virus has been well characterized, the role of minor capsid protein L2 in internalization and infection is less clear. However, cleavage of L2 by furin, a proprotein convertase, and the resulting exposure of an N-terminal region, the RG-1 epitope, has been shown to be a critical step in infection. In this study, we aimed to explicitly show furin cleavage during infection and identify the cellular conditions required for this cleavage event and establishment of infection. An assay to detect furin cleavage of L2 was developed, and for the first time, furin cleavage was directly shown during infection. In vivo data suggests that cyclophilin B, a peptidyl-prolyl isomerase believed to playa role in the conformational changes that occur prior to internalization, may playa less prominent role than previously thought. Understanding the role of L2 in entry and infection provides a more comprehensive picture of the mechanism of papillomavirus infection and exposure of the RG-1 epitope, the major target for next-generation broadly protective pan-HPV vaccines.


Files in this item

Thumbnail
Name:
azu_etd_mr_2012_0017_sip1_m.pdf
Size:
7.440Mb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record