{"id":{"repo_id":"calpoly","oai_identifier":"oai:digitalcommons.calpoly.edu:theses-2602"},"canonical_url":"https://search.dev.ndltd.org/etd/calpoly/oai:digitalcommons.calpoly.edu:theses-2602","repository":{"repo_id":"calpoly","name":"Cal Poly","base_url":"https://digitalcommons.calpoly.edu/do/oai/"},"display":{"title":"Exploring the Physiological Role of Vibrio fischeri PepN","abstract":"<p>The primary contributor to Vibrio fischeri aminopeptidase activity is aminopeptidase N, PepN. Colonization assays revealed the pepN mutant strain to be deficient at forming dense aggregates and populating the host’s light organ compared to wildtype within the first 12 hours of colonization; however the mutant competed normally at 24 hours. To address the role of PepN in colonization initiation and establish additional phenotypes for the pepN mutant strain, stress response and other physiological assays were employed. Marked differences were found between pepN mutant and wildtype strain in response to salinity, acidity, and antibiotic tolerance. This study has provided a foundation for future work on identifying a putative role for V. fischeri PepN in regulating stress response.</p>","abstract_html":"&lt;p&gt;The primary contributor to Vibrio fischeri aminopeptidase activity is aminopeptidase N, PepN. Colonization assays revealed the pepN mutant strain to be deficient at forming dense aggregates and populating the host’s light organ compared to wildtype within the first 12 hours of colonization; however the mutant competed normally at 24 hours. To address the role of PepN in colonization initiation and establish additional phenotypes for the pepN mutant strain, stress response and other physiological assays were employed. Marked differences were found between pepN mutant and wildtype strain in response to salinity, acidity, and antibiotic tolerance. This study has provided a foundation for future work on identifying a putative role for V. fischeri PepN in regulating stress response.&lt;/p&gt;","abstract_has_math":false,"creators":["Cello, Sally L"],"institution":null,"degree_name":"MS in Biological Sciences","degree_level":null,"degree_discipline":"Biological Sciences","degree_department":null,"school":null,"contributors":["Pat Fidopiastis"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-04-01T07:00:00Z","date_published":"2015-04-01T07:00:00Z","updated_at":"2026-07-24T01:31:35Z","subjects":["Aminopeptidase N","metalloproteases","Vibrio fischeri","symbiosis","Euprymna scolopes","Bacteriology","Environmental Microbiology and Microbial Ecology","Microbial Physiology","Organismal Biological Physiology","Other Microbiology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["10.15368/theses.2015.36"],"render_values":[{"text":"10.15368/theses.2015.36","href":"https://doi.org/10.15368/theses.2015.36","code":true}]}]},"links":{"outbound_url":"https://digitalcommons.calpoly.edu/theses/1443","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Pat Fidopiastis"]},{"key":"dc:creator","label":"Author","values":["Cello, Sally L"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2015-07-20T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biological Sciences"]},{"key":"thesis:degree_name","label":"Degree Name","values":["MS in Biological Sciences"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Aminopeptidase N","metalloproteases","Vibrio fischeri","symbiosis","Euprymna scolopes","Bacteriology","Environmental Microbiology and Microbial Ecology","Microbial Physiology","Organismal Biological Physiology","Other Microbiology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://digitalcommons.calpoly.edu/theses/1443","10.15368/theses.2015.36"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["<p>The primary contributor to Vibrio fischeri aminopeptidase activity is aminopeptidase N, PepN. Colonization assays revealed the pepN mutant strain to be deficient at forming dense aggregates and populating the host’s light organ compared to wildtype within the first 12 hours of colonization; however the mutant competed normally at 24 hours. To address the role of PepN in colonization initiation and establish additional phenotypes for the pepN mutant strain, stress response and other physiological assays were employed. Marked differences were found between pepN mutant and wildtype strain in response to salinity, acidity, and antibiotic tolerance. This study has provided a foundation for future work on identifying a putative role for V. fischeri PepN in regulating stress response.</p>"]},{"key":"dc:title","label":"Title","values":["Exploring the Physiological Role of Vibrio fischeri PepN"]}]}],"canonical_facts":{"dc:contributor":["Pat Fidopiastis"],"dc:creator":["Cello, Sally L"],"dc:date.available":["2015-07-20T07:00:00Z"],"dc:description.abstract":["<p>The primary contributor to Vibrio fischeri aminopeptidase activity is aminopeptidase N, PepN. Colonization assays revealed the pepN mutant strain to be deficient at forming dense aggregates and populating the host’s light organ compared to wildtype within the first 12 hours of colonization; however the mutant competed normally at 24 hours. To address the role of PepN in colonization initiation and establish additional phenotypes for the pepN mutant strain, stress response and other physiological assays were employed. Marked differences were found between pepN mutant and wildtype strain in response to salinity, acidity, and antibiotic tolerance. This study has provided a foundation for future work on identifying a putative role for V. fischeri PepN in regulating stress response.</p>"],"dc:identifier":["https://digitalcommons.calpoly.edu/theses/1443","10.15368/theses.2015.36"],"dc:subject":["Aminopeptidase N","metalloproteases","Vibrio fischeri","symbiosis","Euprymna scolopes","Bacteriology","Environmental Microbiology and Microbial Ecology","Microbial Physiology","Organismal Biological Physiology","Other Microbiology"],"dc:title":["Exploring the Physiological Role of Vibrio fischeri PepN"],"thesis:degree_discipline":["Biological Sciences"],"thesis:degree_name":["MS in Biological Sciences"]},"updated_at":"2026-07-24T01:31:35Z"}