dc.contributor.advisor | Foster, Timothy | |
dc.contributor.author | McCormack, Niamh | |
dc.date.accessioned | 2017-06-01T15:10:41Z | |
dc.date.available | 2017-06-01T15:10:41Z | |
dc.date.issued | 2014 | |
dc.identifier.citation | Niamh McCormack, 'Analysis of the function of the N1 subdomain of MSCRAMMs of Staphylococcus aureus', [thesis], Trinity College (Dublin, Ireland). Department of Microbiology, 2014, pp 250 | |
dc.identifier.other | THESIS 10364 | |
dc.identifier.uri | http://hdl.handle.net/2262/80337 | |
dc.description.abstract | The Microbial Surface Component Recognising Adhesive Matrix Molecules (MSCRAMMs) family of cell wall-associated proteins have recently been reclassified based on structure-function analysis. Under this new regime the MSCRAMM family is defined by the presence of at least two tandemly-linked IgG-like folded domains. Clumping factor A (ClfA) is the archetypal fibrinogen-binding MSCRAMM of Staphylococcus aureus and an important virulence factor. An N-terminal signal sequence directs export by the Sec pathway and the C-terminal cell wall-anchoring domain allows covalent attachment of ClfA to peptidoglycan by sortase. Region A of ClfA comprises three independently folded subdomains N1, N2 and N3. Subdomains N2N3 comprise IgG-like folds and promote fibrinogen binding. However the function of subdomain N1 has, until now, remained elusive. | |
dc.format | 1 volume | |
dc.language.iso | en | |
dc.publisher | Trinity College (Dublin, Ireland). Department of Microbiology | |
dc.relation.isversionof | http://stella.catalogue.tcd.ie/iii/encore/record/C__Rb15662327 | |
dc.subject | Microbiology, Ph.D. | |
dc.subject | Ph.D. Trinity College Dublin | |
dc.title | Analysis of the function of the N1 subdomain of MSCRAMMs of Staphylococcus aureus | |
dc.type | thesis | |
dc.type.supercollection | thesis_dissertations | |
dc.type.supercollection | refereed_publications | |
dc.type.qualificationlevel | Doctoral | |
dc.type.qualificationname | Doctor of Philosophy (Ph.D.) | |
dc.rights.ecaccessrights | openAccess | |
dc.format.extentpagination | pp 250 | |
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