Show simple item record

dc.contributor.advisorChairperson, Graduate Committee: Trevor Douglasen
dc.contributor.authorServid, Amy Eloiseen
dc.contributor.otherLaura E. Richert, Ann L. Harmsen, Agnieszka Rynda-Apple, Soo Han, James A. Wiley, Trevor Douglas and Allen G. Harmsen were co-authors of the article, 'A virus-like particle vaccine platform elicits heightened and hastened local lung mucosal antibody production after a single dose' in the journal 'Vaccine' which is contained within this thesis.en
dc.contributor.otherPaul Jordan, Alison O'Neil, Peter Prevelige and Trevor Douglas were co-authors of the article, 'Location of the bacteriophage P22 coat protein C-terminus provides opportunities for the design of capsid-based materials' in the journal 'Biomacromolecules' which is contained within this thesis.en
dc.date.accessioned2016-01-03T16:12:40Z
dc.date.available2016-01-03T16:12:40Z
dc.date.issued2014en
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/9137en
dc.description.abstractIn nature, protein cages are found within the structures of viruses, heat shock proteins, and ferritins. They assemble from subunits into spherical oligomeric structures, which serve to encapsulate, protect, and/or deliver cargo. The fundamental understanding of protein cage structure is a key component in the design of novel nanomaterials that best exploit and expand upon the natural functions of protein cage architectures. By mimicking the re-occurring design strategies employed by natural systems, the protein cages produced during virus infection and/or stress responses can be modified to yield particles that fight disease and/or serve as the building blocks for materials design. In particular, the work described here highlights the design and characterization of protein cages in an effort to develop and uncover new strategies for immunization of the lung against a variety of pathogens. A combination of genetic and chemical engineering approaches is described here in order to better understand the structure of protein cage architectures and the relationship between the structure and in vivo function. This work describes the chemical cross-linking of large antigens and immunomodulatory molecules to the surface of a protein cages, and it shows that intensified and accelerated immune responses result from the display of antigens on a protein cage surface. Genetic incorporation of point mutations within the capsid structure provided unique attachment points for chemical functionalization. In addition, genetic modifications revealed information about the location of the C-terminus of the bacteriophage P22 capsid. The knowledge that this position was displayed on the capsid exterior prompted its use to promote inter-capsid interactions and target nanoparticles to melanoma cells. This research emphasizes that both the protein cage structural design and the local in vivo environment can influence the outcomes of protein cages when administered to the lung environment. It also lays the foundation for the logical design of biomaterials that offer enhanced protection against influenza and other respiratory diseases. Finally, regions of protein cages that are amendable to chemical and genetic modifications are described herein, and these have paved the way for the continued development of protein cage platforms for nanomedical and material applications.en
dc.language.isoenen
dc.publisherMontana State University - Bozeman, College of Letters & Scienceen
dc.subject.lcshProtein engineeringen
dc.subject.lcshNanomedicineen
dc.subject.lcshLungsen
dc.subject.lcshImmunologyen
dc.titleCharacterization and embellishment of protein cages for nanomedical and nanomaterial applicationsen
dc.typeDissertationen
dc.rights.holderCopyright 2014 by Amy Eloise Serviden
thesis.catalog.ckey2752924en
thesis.degree.committeemembersMembers, Graduate Committee: Allen G. Harmsen; Martin Teintze; Brian Bothner; Mary J. Cloningeren
thesis.degree.departmentChemistry & Biochemistry.en
thesis.degree.genreDissertationen
thesis.degree.namePhDen
thesis.format.extentfirstpage1en
thesis.format.extentlastpage204en


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record


MSU uses DSpace software, copyright © 2002-2017  Duraspace. For library collections that are not accessible, we are committed to providing reasonable accommodations and timely access to users with disabilities. For assistance, please submit an accessibility request for library material.