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dc.contributor.advisorFoster, Tim
dc.contributor.authorMulcahy, Michelle
dc.date.accessioned2017-02-08T10:26:09Z
dc.date.available2017-02-08T10:26:09Z
dc.date.issued2013
dc.identifier.citationMichelle Mulcahy, 'The interaction of clumping factor B and iron-regulated surface determinant protein A of Staphylococcus aureus with the squamous epithelial cell envelope protein loricrin', [thesis], Trinity College (Dublin, Ireland). Department of Microbiology, 2013, pp 257
dc.identifier.otherTHESIS 10149
dc.identifier.urihttp://hdl.handle.net/2262/79259
dc.description.abstractStaphylococcus aureus permanently colonises the anterior nares of 20% of the human population while the remainder is colonised intermittently. Clumping factor B (ClfB) is a surface-expressed staphylococcal protein that plays a role in nasal colonisation. ClfB promotes bacterial adherence to human desquamated epithelial cells (squames) and ClfB-deficient strains of S. aureus displayed a significantly reduced ability to colonise the nares of rodents and healthy human volunteers. The iron-regulated surface determinant protein A (IsdA) is also involved in nasal colonisation. IsdA promotes bacterial adherence to squames and an interaction between IsdA and loricrin has been suggested. ClfB binds to the aC-region of fibrinogen and to the tail region of the surface- exposed squamous cell protein cytokeratin 10 (K10). The ClfB-binding site within K10 was localised to the glycine serine-rich omega loops in the K10 tail. Unpublished evidence from E. Walsh and T.J. Foster suggested that ClfB binds to loricrin, another structural protein present in the cornified envelope.
dc.format1 volume
dc.language.isoen
dc.publisherTrinity College (Dublin, Ireland). Department of Microbiology
dc.relation.isversionofhttp://stella.catalogue.tcd.ie/iii/encore/record/C__Rb15355663
dc.subjectMicrobiology, Ph.D.
dc.subjectPh.D. Trinity College Dublin
dc.titleThe interaction of clumping factor B and iron-regulated surface determinant protein A of Staphylococcus aureus with the squamous epithelial cell envelope protein loricrin
dc.typethesis
dc.type.supercollectionthesis_dissertations
dc.type.supercollectionrefereed_publications
dc.type.qualificationlevelDoctoral
dc.type.qualificationnameDoctor of Philosophy (Ph.D.)
dc.rights.ecaccessrightsopenAccess
dc.format.extentpaginationpp 257
dc.description.noteTARA (Trinity’s Access to Research Archive) has a robust takedown policy. Please contact us if you have any concerns: rssadmin@tcd.ie


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