The Role of LbpB in Iron Acquisition and Cellular Defense in Neisseria meningitidis

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atmire.migration.oldid5111
dc.contributor.advisorSchryvers, Anthony
dc.contributor.authorOstan, Nicholas
dc.contributor.committeememberSchriemer, David
dc.contributor.committeememberArmstrong, Glen
dc.contributor.committeememberDeVinney, Rebekah
dc.date.accessioned2016-11-29T17:25:04Z
dc.date.available2016-11-29T17:25:04Z
dc.date.issued2016
dc.date.submitted2016en
dc.description.abstractLactoferrin binding protein B (LbpB) is a bi-lobed outer membrane-bound lipoprotein that comprises part of the lactoferrin (Lf) receptor complex in many Gram-negative pathogens. Recent studies have demonstrated that the LbpB protein expressed by Neisseria meningitidis - a causative agent and major contributor to bacterial meningitis - plays a role in protecting the bacteria from cationic antimicrobial peptides due to large regions rich in anionic residues in the C-terminal lobe. Relative to its homologue, transferrin-binding protein (TbpB), there is little evidence for its role in iron acquisition and relatively little structural and biophysical information on its interaction with Lf. Nevertheless, there have been several published structural models on the LbpB-Lf interaction that are incompatible. In this study I will present comparative experimental data regarding the LbpB-Lf interaction and TbpB-Tf interaction. Using biophysical data to determine tertiary structure information, I have constructed a new model of LbpB that forms the basis for a new LbpB:Lf interaction. Our data suggests a 1:1 complex of LbpB:hLf is consistent with an LbpB-N/hLf-C binding mode, consistent with a role in iron acquisition. A 2:1 complex of LbpB:hLf:LbpB contains both an LbpB-N/hLf-C interaction as well as an LbpB-C/hLf-N interaction directly with the anti-microbial peptide lactoferricin. We thus show a novel way in which the LbpB from N. meningitidis may sequester anti-microbial peptides, or hinder proteolytic derivation of lactoferricin from lactoferrin by forming large cross-linked complexes of lactoferrin.en_US
dc.identifier.citationOstan, N. (2016). The Role of LbpB in Iron Acquisition and Cellular Defense in Neisseria meningitidis (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/28331en_US
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/28331
dc.identifier.urihttp://hdl.handle.net/11023/3461
dc.language.isoeng
dc.publisher.facultyGraduate Studies
dc.publisher.institutionUniversity of Calgaryen
dc.publisher.placeCalgaryen
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.subjectBiology--Cell
dc.subjectImmunology
dc.subjectBiochemistry
dc.subject.classificationNeisseria meningitidisen_US
dc.subject.classificationIron acquisitionen_US
dc.subject.classificationLactoferrin-binding protein Ben_US
dc.subject.classificationAntimicrobial peptidesen_US
dc.subject.classificationLactoferrinen_US
dc.titleThe Role of LbpB in Iron Acquisition and Cellular Defense in Neisseria meningitidis
dc.typemaster thesis
thesis.degree.disciplineMicrobiology & Infectious Diseases
thesis.degree.grantorUniversity of Calgary
thesis.degree.nameMaster of Science (MSc)
ucalgary.item.requestcopytrue
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