{"id":{"repo_id":"uwo","oai_identifier":"oai:uwo.scholaris.ca:20.500.14721/35495"},"canonical_url":"https://search.dev.ndltd.org/etd/uwo/oai:uwo.scholaris.ca:20.500.14721/35495","repository":{"repo_id":"uwo","name":"Western University","base_url":"https://uwo.scholaris.ca/server/oai/request"},"display":{"title":"HcpE, a potential immuno-modulatory protein from Helicobacter pylori that is dependent on the Disulfide bond protein DsbHP","abstract":"H. pylori is a human gastric pathogen that colonizes ~ 50% of the world’s population. It can cause gastritis, gastric or duodenal ulcers and also gastric cancer. H. pylori produces Helicobacter cysteine rich protein HcpE, a secreted protein which may play a role in virulence. In this study we show that HcpE is secreted in the culture supernatant both as a soluble protein and in association with outer membrane vesicles, and may play a role in the modulation of H. pylori inflammatory responses. We identified that DsbHP is necessary for HcpE production and secretion in H. pylori, and demonstrated DsbHP has DiSulfide Bond (Dsb) forming activity on reduced lysozyme. Furthermore, we demonstrated that DsbHP has a DsbA-type of activity when expressed in E. coli, despite its similarity with DsbG, and that DsbHP is involved in maintaining redox homeostasis in H. pylori.","abstract_html":"H. pylori is a human gastric pathogen that colonizes ~ 50% of the world’s population. It can cause gastritis, gastric or duodenal ulcers and also gastric cancer. H. pylori produces Helicobacter cysteine rich protein HcpE, a secreted protein which may play a role in virulence. In this study we show that HcpE is secreted in the culture supernatant both as a soluble protein and in association with outer membrane vesicles, and may play a role in the modulation of H. pylori inflammatory responses. We identified that DsbHP is necessary for HcpE production and secretion in H. pylori, and demonstrated DsbHP has DiSulfide Bond (Dsb) forming activity on reduced lysozyme. Furthermore, we demonstrated that DsbHP has a DsbA-type of activity when expressed in E. coli, despite its similarity with DsbG, and that DsbHP is involved in maintaining redox homeostasis in H. pylori.","abstract_has_math":false,"creators":["Lester, Jeff"],"institution":"The University of Western Ontario","degree_name":"M Sc","degree_level":null,"degree_discipline":"Microbiology and Immunology","degree_department":null,"school":null,"contributors":[],"advisors":["Carole Creuzenet"],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014-12-10","date_published":"2014-12-10","updated_at":"2026-07-27T21:56:11Z","subjects":["Helicobacter pylori","Disulfide bonds","Dsb proteins","Helicobacter Cysteine-rich proteins","Protein secretion"],"languages":["en_ca"],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://hdl.handle.net/20.500.14721/35495","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Carole Creuzenet"]},{"key":"dc:creator","label":"Author","values":["Lester, Jeff"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2025-07-10T20:38:30Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2025-07-10T20:38:30Z"]},{"key":"dc:date.issued","label":"Date","values":["2014-12-10"]},{"key":"dc:publisher","label":"Institution","values":["The University of Western Ontario"]},{"key":"dc:type","label":"Dc Type","values":["thesis"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology and Immunology"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M Sc"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Helicobacter pylori","Disulfide bonds","Dsb proteins","Helicobacter Cysteine-rich proteins","Protein secretion"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language.iso","label":"Language (ISO)","values":["en_ca"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/20.500.14721/35495"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The thesis cover page in the PDF document includes references to Western University’s previous institutional repository platform, known as Scholarship@Western, and links to that platform (beginning with ir.lib.uwo.ca). In citing or referring to this thesis, use the DOI or handle from this page instead. Sample citation: Author name, \"Thesis title.\" (Year). Western University Open Repository. https://doi.org/10.71858/123456."]},{"key":"dc:description.abstract","label":"Abstract","values":["H. pylori is a human gastric pathogen that colonizes ~ 50% of the world’s population. It can cause gastritis, gastric or duodenal ulcers and also gastric cancer. H. pylori produces Helicobacter cysteine rich protein HcpE, a secreted protein which may play a role in virulence. In this study we show that HcpE is secreted in the culture supernatant both as a soluble protein and in association with outer membrane vesicles, and may play a role in the modulation of H. pylori inflammatory responses. We identified that DsbHP is necessary for HcpE production and secretion in H. pylori, and demonstrated DsbHP has DiSulfide Bond (Dsb) forming activity on reduced lysozyme. Furthermore, we demonstrated that DsbHP has a DsbA-type of activity when expressed in E. coli, despite its similarity with DsbG, and that DsbHP is involved in maintaining redox homeostasis in H. pylori."]},{"key":"dc:title","label":"Title","values":["HcpE, a potential immuno-modulatory protein from Helicobacter pylori that is dependent on the Disulfide bond protein DsbHP"]}]}],"canonical_facts":{"dc:contributor.advisor":["Carole Creuzenet"],"dc:creator":["Lester, Jeff"],"dc:date.accessioned":["2025-07-10T20:38:30Z"],"dc:date.available":["2025-07-10T20:38:30Z"],"dc:date.issued":["2014-12-10"],"dc:description":["The thesis cover page in the PDF document includes references to Western University’s previous institutional repository platform, known as Scholarship@Western, and links to that platform (beginning with ir.lib.uwo.ca). In citing or referring to this thesis, use the DOI or handle from this page instead. Sample citation: Author name, \"Thesis title.\" (Year). Western University Open Repository. https://doi.org/10.71858/123456."],"dc:description.abstract":["H. pylori is a human gastric pathogen that colonizes ~ 50% of the world’s population. It can cause gastritis, gastric or duodenal ulcers and also gastric cancer. H. pylori produces Helicobacter cysteine rich protein HcpE, a secreted protein which may play a role in virulence. In this study we show that HcpE is secreted in the culture supernatant both as a soluble protein and in association with outer membrane vesicles, and may play a role in the modulation of H. pylori inflammatory responses. We identified that DsbHP is necessary for HcpE production and secretion in H. pylori, and demonstrated DsbHP has DiSulfide Bond (Dsb) forming activity on reduced lysozyme. Furthermore, we demonstrated that DsbHP has a DsbA-type of activity when expressed in E. coli, despite its similarity with DsbG, and that DsbHP is involved in maintaining redox homeostasis in H. pylori."],"dc:identifier.uri":["https://hdl.handle.net/20.500.14721/35495"],"dc:language.iso":["en_ca"],"dc:publisher":["The University of Western Ontario"],"dc:subject":["Helicobacter pylori","Disulfide bonds","Dsb proteins","Helicobacter Cysteine-rich proteins","Protein secretion"],"dc:title":["HcpE, a potential immuno-modulatory protein from Helicobacter pylori that is dependent on the Disulfide bond protein DsbHP"],"dc:type":["thesis"],"thesis:degree_discipline":["Microbiology and Immunology"],"thesis:degree_name":["M Sc"]},"updated_at":"2026-07-27T21:56:11Z"}