Biomedical Sciences ETDs


Alex Medford

Publication Date



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.


VLPs, bacteriophage, Virus like particles, PP7

Document Type




Degree Name

Biomedical Sciences

Level of Degree


Department Name

Biomedical Sciences Graduate Program

First Committee Member (Chair)

Ozbun, Michelle

Second Committee Member

Peabody, David

Third Committee Member

Wilson, Bridget

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