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The Generation and Immunogenicity of PP7 Virus-Like Particles Displaying Target Antigens

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Please use this identifier to cite or link to this item: http://hdl.handle.net/1928/10833

The Generation and Immunogenicity of PP7 Virus-Like Particles Displaying Target Antigens

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dc.contributor.author Medford, Alex
dc.date.accessioned 2010-06-25T21:06:06Z
dc.date.available 2010-06-25T21:06:06Z
dc.date.issued 2010-06-25T21:06:06Z
dc.date.submitted May 2010
dc.identifier.uri http://hdl.handle.net/1928/10833
dc.description.abstract The 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.iso en_US en_US
dc.subject VLPs en_US
dc.subject bacteriophage en_US
dc.title The Generation and Immunogenicity of PP7 Virus-Like Particles Displaying Target Antigens en_US
dc.type Thesis en_US
dc.description.degree Biomedical Science en_US
dc.description.level Masters en_US
dc.description.department University of New Mexico. Biomedical Sciences Graduate Program en_US
dc.description.advisor Chackerian, Bryce
dc.description.committee-member Ozbun, Michelle
dc.description.committee-member Peabody, David
dc.description.committee-member Wilson, Bridget


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final master 2.doc 2.150Mb Microsoft Word View/Open Thesis
page 0.doc 11.5Kb Microsoft Word View/Open Committee sign off page
page 1.doc 27.5Kb Microsoft Word View/Open Title page
page 2.doc 12Kb Microsoft Word View/Open Abstract

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