Cloning and expression of the bovine papillomavirus major capsid gene.

Persistent Link:
http://hdl.handle.net/10150/184475
Title:
Cloning and expression of the bovine papillomavirus major capsid gene.
Author:
Driscoll, Barbara.
Issue Date:
1988
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:
In order to characterize the protein product of the major capsid protein gene of Bovine Papillomavirus Type 2, 93% of the L1 open reading frame was cloned into two different expression vectors. This coding sequence produced a hybrid product when cloned into the expression vector pKK233-2, which interacted weakly with anti-BPV antisera and proved unable to elicit neutralizing antibodies. When the sequence was cloned into the expression vector pRA10, a more native form of the major capsid protein was produced, which interacted well with anti-BPV sera. Antisera raised against this cloned product was able to neutralize BPV in a tissue culture transformation assay. The 3' end of the L1 open reading frame was cloned into pBA10 in order to characterize the immunogenic potential of the carboxy terminus of the major capsid gene. The carboxy terminus proved to have no greater ability to interact with anti-BPV antisera, showing that the immunogenic epitopes of the protein are probably evenly distributed along the linear sequence.
Type:
text; Dissertation-Reproduction (electronic)
Keywords:
Papillomaviruses.; Molecular cloning.; Gene expression.
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Molecular and Cellular Biology; Graduate College
Degree Grantor:
University of Arizona

Full metadata record

DC FieldValue Language
dc.language.isoenen_US
dc.titleCloning and expression of the bovine papillomavirus major capsid gene.en_US
dc.creatorDriscoll, Barbara.en_US
dc.contributor.authorDriscoll, Barbara.en_US
dc.date.issued1988en_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.description.abstractIn order to characterize the protein product of the major capsid protein gene of Bovine Papillomavirus Type 2, 93% of the L1 open reading frame was cloned into two different expression vectors. This coding sequence produced a hybrid product when cloned into the expression vector pKK233-2, which interacted weakly with anti-BPV antisera and proved unable to elicit neutralizing antibodies. When the sequence was cloned into the expression vector pRA10, a more native form of the major capsid protein was produced, which interacted well with anti-BPV sera. Antisera raised against this cloned product was able to neutralize BPV in a tissue culture transformation assay. The 3' end of the L1 open reading frame was cloned into pBA10 in order to characterize the immunogenic potential of the carboxy terminus of the major capsid gene. The carboxy terminus proved to have no greater ability to interact with anti-BPV antisera, showing that the immunogenic epitopes of the protein are probably evenly distributed along the linear sequence.en_US
dc.typetexten_US
dc.typeDissertation-Reproduction (electronic)en_US
dc.subjectPapillomaviruses.en_US
dc.subjectMolecular cloning.en_US
dc.subjectGene expression.en_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineMolecular and Cellular Biologyen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.identifier.proquest8824268en_US
dc.identifier.oclc701363218en_US
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