Helicobacter pylori: comparative genomics and structure-function analysis of the flagellum biogenesis protein HP0958

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dc.contributor.advisor O'Toole, Paul W. en
dc.contributor.author de Lacy Clancy, Ceara A.
dc.date.accessioned 2014-10-06T16:28:16Z
dc.date.available 2015-10-07T04:00:05Z
dc.date.issued 2014
dc.date.submitted 2014
dc.identifier.citation de Lacy Clancy, C. A. 2014. Helicobacter pylori: comparative genomics and structure-function analysis of the flagellum biogenesis protein HP0958. PhD Thesis, University College Cork. en
dc.identifier.endpage 290
dc.identifier.uri http://hdl.handle.net/10468/1684
dc.description.abstract Helicobacter pylori is a gastric pathogen which infects ~50% of the global population and can lead to the development of gastritis, gastric and duodenal ulcers and carcinoma. Genome sequencing of H. pylori revealed high levels of genetic variability; this pathogen is known for its adaptability due to mechanisms including phase variation, recombination and horizontal gene transfer. Motility is essential for efficient colonisation by H. pylori. The flagellum is a complex nanomachine which has been studied in detail in E. coli and Salmonella. In H. pylori, key differences have been identified in the regulation of flagellum biogenesis, warranting further investigation. In this study, the genomes of two H. pylori strains (CCUG 17874 and P79) were sequenced and published as draft genome sequences. Comparative studies identified the potential role of restriction modification systems and the comB locus in transformation efficiency differences between these strains. Core genome analysis of 43 H. pylori strains including 17874 and P79 defined a more refined core genome for the species than previously published. Comparative analysis of the genome sequences of strains isolated from individuals suffering from H. pylori related diseases resulted in the identification of “disease-specific” genes. Structure-function analysis of the essential motility protein HP0958 was performed to elucidate its role during flagellum assembly in H. pylori. The previously reported HP0958-FliH interaction could not be substantiated in this study and appears to be a false positive. Site-directed mutagenesis confirmed that the coiled-coil domain of HP0958 is involved in the interaction with RpoN (74-284), while the Zn-finger domain is required for direct interaction with the full length flaA mRNA transcript. Complementation of a non-motile hp0958-null derivative strain of P79 with site-directed mutant alleles of hp0958 resulted in cells producing flagellar-type extrusions from non-polar positions. Thus, HP0958 may have a novel function in spatial localisation of flagella in H. pylori en
dc.description.sponsorship Irish Research Council (EMBARK initiative); Science Foundation Ireland (Research Frontiers Programme award (09_RFP_GEN2443)) en
dc.format.mimetype application/pdf en
dc.language.iso en en
dc.publisher University College Cork en
dc.rights © 2014, Ceara A. De Lacy Clancy. en
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/3.0/ en
dc.subject Microbiology en
dc.subject Helicobacter pylori en
dc.subject Flagella en
dc.subject Genomics en
dc.title Helicobacter pylori: comparative genomics and structure-function analysis of the flagellum biogenesis protein HP0958 en
dc.type Doctoral thesis en
dc.type.qualificationlevel Doctoral en
dc.type.qualificationname PhD (Science) en
dc.internal.availability Full text available en
dc.description.version Accepted Version
dc.contributor.funder Irish Research Council en
dc.contributor.funder Science Foundation Ireland en
dc.description.status Not peer reviewed en
dc.internal.school Microbiology en
dc.check.reason This thesis is due for publication or the author is actively seeking to publish this material en
dc.check.opt-out Not applicable en
dc.thesis.opt-out false
dc.check.entireThesis Entire Thesis Restricted
dc.check.embargoformat Both hard copy thesis and e-thesis en
ucc.workflow.supervisor pwotoole@ucc.ie
dc.internal.conferring Summer Conferring 2014


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© 2014, Ceara A. De Lacy Clancy. Except where otherwise noted, this item's license is described as © 2014, Ceara A. De Lacy Clancy.
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