{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/106407"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/106407","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Evaluating the contribution of a metal independent aldolase to resisting nutritional immunity","abstract":"The sequestration of essential nutrients from pathogens is a key component in the vertebrate immune response. One aspect of this defense, known as nutritional immunity, is the sequestration of the essential metals manganese and zinc. An important component of this defense is the metal binding host protein calprotectin, which inactivates metal- dependent bacterial enzymes. The ability of Staphylococcus aureus to cause infection suggests that it has mechanisms that enable it to minimize the impact of nutrient metal limitation. The consumption of glucose is critical to the ability of S. aureus to overcome nitrosative stress. Yet at the same time several of the primary glycolytic enzymes utilized by S. aureus are predicted to be dependent on a metal for function, including a putatively zinc-dependent aldolase. S. aureus possesses an additional metal-independent aldolase, which is regulated by the two-component regulator ArlRS. This two-component system has previously been linked to the ability of S. aureus to resist calprotectin-imposed metal limitation. In light of these observations, we evaluated if the metal-independent aldolase contributes to the ability of S. aureus grow in metal restricted environments. These data show that when the metal-independent aldolase is impaired, S. aureus shows greater sensitivity to metal limitation. This is alleviated upon addition of manganese, but not zinc. Increasing manganese limitation by ablating manganese transport exacerbates the phenotype of the aldolase mutant. In addition, the availability of an alternative carbon source can reduce calprotectin sensitivity, provided its entry point in glycolysis is below the metal-dependent blockage. This suggests that a blockage at the aldolase step in glycolysis is important for S. aureus to resolve, either through the use of a metal-independent isozyme or other carbon sources, in order to resist calprotectin-induced metal limitation.","abstract_html":"The sequestration of essential nutrients from pathogens is a key component in the vertebrate immune response. One aspect of this defense, known as nutritional immunity, is the sequestration of the essential metals manganese and zinc. An important component of this defense is the metal binding host protein calprotectin, which inactivates metal- dependent bacterial enzymes. The ability of Staphylococcus aureus to cause infection suggests that it has mechanisms that enable it to minimize the impact of nutrient metal limitation. The consumption of glucose is critical to the ability of S. aureus to overcome nitrosative stress. Yet at the same time several of the primary glycolytic enzymes utilized by S. aureus are predicted to be dependent on a metal for function, including a putatively zinc-dependent aldolase. S. aureus possesses an additional metal-independent aldolase, which is regulated by the two-component regulator ArlRS. This two-component system has previously been linked to the ability of S. aureus to resist calprotectin-imposed metal limitation. In light of these observations, we evaluated if the metal-independent aldolase contributes to the ability of S. aureus grow in metal restricted environments. These data show that when the metal-independent aldolase is impaired, S. aureus shows greater sensitivity to metal limitation. This is alleviated upon addition of manganese, but not zinc. Increasing manganese limitation by ablating manganese transport exacerbates the phenotype of the aldolase mutant. In addition, the availability of an alternative carbon source can reduce calprotectin sensitivity, provided its entry point in glycolysis is below the metal-dependent blockage. This suggests that a blockage at the aldolase step in glycolysis is important for S. aureus to resolve, either through the use of a metal-independent isozyme or other carbon sources, in order to resist calprotectin-induced metal limitation.","abstract_has_math":false,"creators":["Bastille, Talina S."],"institution":"University of Illinois at Urbana-Champaign","degree_name":"M.S.","degree_level":"Thesis","degree_discipline":"Microbiology","degree_department":null,"school":null,"contributors":["Kehl-Fie, Thomas","Slauch, James","Metcalf, William"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2020,"date_issued":"2020-03-02T22:18:21Z","date_published":"2020-03-02T22:18:21Z","updated_at":"2026-07-22T22:24:47Z","subjects":["staphylococcus aureus, nutritional immunity"],"languages":["en"],"rights":["Copyright 2019 Talina Bastille"],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"http://hdl.handle.net/2142/106407","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Kehl-Fie, Thomas","Slauch, James","Metcalf, William"]},{"key":"dc:creator","label":"Author","values":["Bastille, Talina S."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2020-03-02T22:18:21Z","2022-03-03T10:15:25Z","2019-12-13","2019-12"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Microbiology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["M.S."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["staphylococcus aureus, nutritional immunity"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 2019 Talina Bastille"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/106407"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The sequestration of essential nutrients from pathogens is a key component in the vertebrate immune response. One aspect of this defense, known as nutritional immunity, is the sequestration of the essential metals manganese and zinc. An important component of this defense is the metal binding host protein calprotectin, which inactivates metal- dependent bacterial enzymes. The ability of Staphylococcus aureus to cause infection suggests that it has mechanisms that enable it to minimize the impact of nutrient metal limitation. The consumption of glucose is critical to the ability of S. aureus to overcome nitrosative stress. Yet at the same time several of the primary glycolytic enzymes utilized by S. aureus are predicted to be dependent on a metal for function, including a putatively zinc-dependent aldolase. S. aureus possesses an additional metal-independent aldolase, which is regulated by the two-component regulator ArlRS. This two-component system has previously been linked to the ability of S. aureus to resist calprotectin-imposed metal limitation. In light of these observations, we evaluated if the metal-independent aldolase contributes to the ability of S. aureus grow in metal restricted environments. These data show that when the metal-independent aldolase is impaired, S. aureus shows greater sensitivity to metal limitation. This is alleviated upon addition of manganese, but not zinc. Increasing manganese limitation by ablating manganese transport exacerbates the phenotype of the aldolase mutant. In addition, the availability of an alternative carbon source can reduce calprotectin sensitivity, provided its entry point in glycolysis is below the metal-dependent blockage. This suggests that a blockage at the aldolase step in glycolysis is important for S. aureus to resolve, either through the use of a metal-independent isozyme or other carbon sources, in order to resist calprotectin-induced metal limitation.","Submission published under a 24 month embargo labeled 'U of I Access', the embargo will last until 2021-12-01","The student, Talina Bastille, accepted the attached license on 2019-12-13 at 10:51.","The student, Talina Bastille, submitted this Thesis for approval on 2019-12-13 at 10:57.","This Thesis was approved for publication on 2019-12-13 at 11:17.","DSpace SAF Submission Ingestion Package generated from Vireo submission #14825 on 2020-02-28 at 17:24:35","Made available in DSpace on 2020-03-02T22:18:21Z (GMT). No. of bitstreams: 2 BASTILLE-THESIS-2019.pdf: 1407143 bytes, checksum: 534dfd301ef47c01951d44ef29c81ab0 (MD5) LICENSE.txt: 4212 bytes, checksum: c3b37348b21d45dea02c885eebf6f7ff (MD5) Previous issue date: 2019-12-13","Embargo set by: Seth Robbins for item 113950 Lift date: 2022-03-02T22:18:25Z Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system","U of I Only Restriction Lifted for Item 113950 on 2022-03-03T10:15:25Z."]},{"key":"dc:format","label":"Dc Format","values":["application/pdf"]},{"key":"dc:title","label":"Title","values":["Evaluating the contribution of a metal independent aldolase to resisting nutritional immunity"]}]}],"canonical_facts":{"dc:contributor":["Kehl-Fie, Thomas","Slauch, James","Metcalf, William"],"dc:creator":["Bastille, Talina S."],"dc:date":["2020-03-02T22:18:21Z","2022-03-03T10:15:25Z","2019-12-13","2019-12"],"dc:description":["The sequestration of essential nutrients from pathogens is a key component in the vertebrate immune response. One aspect of this defense, known as nutritional immunity, is the sequestration of the essential metals manganese and zinc. An important component of this defense is the metal binding host protein calprotectin, which inactivates metal- dependent bacterial enzymes. The ability of Staphylococcus aureus to cause infection suggests that it has mechanisms that enable it to minimize the impact of nutrient metal limitation. The consumption of glucose is critical to the ability of S. aureus to overcome nitrosative stress. Yet at the same time several of the primary glycolytic enzymes utilized by S. aureus are predicted to be dependent on a metal for function, including a putatively zinc-dependent aldolase. S. aureus possesses an additional metal-independent aldolase, which is regulated by the two-component regulator ArlRS. This two-component system has previously been linked to the ability of S. aureus to resist calprotectin-imposed metal limitation. In light of these observations, we evaluated if the metal-independent aldolase contributes to the ability of S. aureus grow in metal restricted environments. These data show that when the metal-independent aldolase is impaired, S. aureus shows greater sensitivity to metal limitation. This is alleviated upon addition of manganese, but not zinc. Increasing manganese limitation by ablating manganese transport exacerbates the phenotype of the aldolase mutant. In addition, the availability of an alternative carbon source can reduce calprotectin sensitivity, provided its entry point in glycolysis is below the metal-dependent blockage. This suggests that a blockage at the aldolase step in glycolysis is important for S. aureus to resolve, either through the use of a metal-independent isozyme or other carbon sources, in order to resist calprotectin-induced metal limitation.","Submission published under a 24 month embargo labeled 'U of I Access', the embargo will last until 2021-12-01","The student, Talina Bastille, accepted the attached license on 2019-12-13 at 10:51.","The student, Talina Bastille, submitted this Thesis for approval on 2019-12-13 at 10:57.","This Thesis was approved for publication on 2019-12-13 at 11:17.","DSpace SAF Submission Ingestion Package generated from Vireo submission #14825 on 2020-02-28 at 17:24:35","Made available in DSpace on 2020-03-02T22:18:21Z (GMT). No. of bitstreams: 2 BASTILLE-THESIS-2019.pdf: 1407143 bytes, checksum: 534dfd301ef47c01951d44ef29c81ab0 (MD5) LICENSE.txt: 4212 bytes, checksum: c3b37348b21d45dea02c885eebf6f7ff (MD5) Previous issue date: 2019-12-13","Embargo set by: Seth Robbins for item 113950 Lift date: 2022-03-02T22:18:25Z Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system","U of I Only Restriction Lifted for Item 113950 on 2022-03-03T10:15:25Z."],"dc:format":["application/pdf"],"dc:identifier":["http://hdl.handle.net/2142/106407"],"dc:language":["en"],"dc:rights":["Copyright 2019 Talina Bastille"],"dc:subject":["staphylococcus aureus, nutritional immunity"],"dc:title":["Evaluating the contribution of a metal independent aldolase to resisting nutritional immunity"],"dc:type":["text"],"thesis:degree_discipline":["Microbiology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["M.S."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:24:47Z"}