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dc.contributor.advisorSchryvers, Anthony
dc.contributor.authorTang, Alexander
dc.date.accessioned2013-12-13T22:28:20Z
dc.date.available2014-03-15T07:00:16Z
dc.date.issued2013-12-13
dc.date.submitted2013en
dc.identifier.citationTang, A. (2013). The development of a new reporter system to study the interaction between FbpA and FbpBC (Unpublished master's thesis). University of Calgary, Calgary, AB. doi:10.11575/PRISM/28055en_US
dc.identifier.urihttp://hdl.handle.net/11023/1200
dc.description.abstractBacteria require efficient iron acquisition systems to infect and colonize the mammalian host. Neisseriaceae and Pasteurellaceae have developed an iron uptake system that involves iron removal from host glycoproteins. The human pathogen, Haemophilus influenzae, has a surface receptor complex containing transferrin binding proteins (TbpA and TbpB). This complex facilitates the release of iron from host transferrin and into the periplasm, where it binds to a periplasmic binding protein, ferric binding protein (FbpA). FbpA is part of the ABC transporter, FbpABC that transports iron from the periplasm into the cytoplasm. The interaction between FbpA and FbpBC is currently unknown. A series of site directed mutants were created to study this interaction based on models of other ABC transporters. We have developed a new novel reporter system to study this interaction. The results of this study have shown the lux reporter system to be more advantageous than past methods that evaluated iron uptake systems.en_US
dc.language.isoeng
dc.rightsUniversity of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.
dc.subjectMicrobiology
dc.subjectBiology--Molecular
dc.titleThe development of a new reporter system to study the interaction between FbpA and FbpBC
dc.typemaster thesis
dc.publisher.facultyGraduate Studies
dc.publisher.institutionUniversity of Calgaryen
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/28055
thesis.degree.nameMaster of Science
thesis.degree.nameMS
thesis.degree.nameMSc
thesis.degree.disciplineBiochemistry and Molecular Biology
thesis.degree.grantorUniversity of Calgary
atmire.migration.oldid1669
dc.publisher.placeCalgaryen


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