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dc.contributor.authorMedford, Alex
dc.date.accessioned2010-06-25T21:06:06Z
dc.date.available2010-06-25T21:06:06Z
dc.date.issued2010-06-25T21:06:06Z
dc.date.submittedMay 2010
dc.identifier.urihttp://hdl.handle.net/1928/10833
dc.description.abstractThe immunogenicity of an antigen can be increased by displaying it in a highly dense, multivalent context, such as on the surface of a virus or virus-like particle (VLP). However, for many viruses, the ability to display diverse antigens on viral surfaces through the construction of recombinant virus particles is limited because peptide insertions are not compatible with virus or VLP assembly. In this thesis, I examined the ability of VLPs of bacteriophage PP7 to have target peptides inserted into a single-chain dimer of its coat protein and form VLP that display the epitope of interest on the particle surface in an immunogenic manner. We found that bacteriophage PP7 is highly tolerant to defined peptide insertions, and a semi-random sequence library. Peptides were displayed on the surface of the VLPs and the recombinant PP7 VLPs were highly immunogenic. Moreover, a PP7 VLP displaying a neutralizing epitope from human papillomavirus (HPV) protein induced a strong antibody response that could protect animals in a mouse genital HPV infection model.en_US
dc.language.isoen_USen_US
dc.subjectVLPsen_US
dc.subjectbacteriophageen_US
dc.titleThe Generation and Immunogenicity of PP7 Virus-Like Particles Displaying Target Antigensen_US
dc.typeThesisen_US
dc.description.degreeBiomedical Scienceen_US
dc.description.levelMastersen_US
dc.description.departmentUniversity of New Mexico. Biomedical Sciences Graduate Programen_US
dc.description.advisorChackerian, Bryce
dc.description.committee-memberOzbun, Michelle
dc.description.committee-memberPeabody, David
dc.description.committee-memberWilson, Bridget


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