Persistent Link:
http://hdl.handle.net/10150/243893
Title:
The Role of Furin Cleavage in Human Papillomavirus Infection
Author:
Bratton, Kristin
Issue Date:
May-2012
Publisher:
The University of Arizona.
Rights:
Copyright © 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.
Abstract:
The 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.
Type:
text; Electronic Thesis
Degree Name:
B.S.
Degree Level:
bachelors
Degree Program:
Honors College; Biochemistry and Molecular Biophysics
Degree Grantor:
University of Arizona

Full metadata record

DC FieldValue Language
dc.language.isoenen_US
dc.titleThe Role of Furin Cleavage in Human Papillomavirus Infectionen_US
dc.creatorBratton, Kristinen_US
dc.contributor.authorBratton, Kristinen_US
dc.date.issued2012-05-
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.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.en_US
dc.typetexten_US
dc.typeElectronic Thesisen_US
thesis.degree.nameB.S.en_US
thesis.degree.levelbachelorsen_US
thesis.degree.disciplineHonors Collegeen_US
thesis.degree.disciplineBiochemistry and Molecular Biophysicsen_US
thesis.degree.grantorUniversity of Arizonaen_US
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