2026-09-22T02:22:10Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/44445 2023-07-11 col_2142_14789 col_2142_5131 com_2142_14788 com_2142_8903 com_2142_5130

Hergenrother, Paul J. Larson, Amy 2013-05-24T22:16:25Z 2013-05-24T22:16:25Z 2015-05-24T10:01:42Z 2013-05 2013-05-24T22:16:25Z 2013-05 The rise and spread of drug-resistant pathogens has created a critical need for the continued discovery and development of new antibacterial compounds. Bacterial toxin-antitoxin (TA) systems consist of a toxin capable of arresting cell growth and an antitoxin that binds to and inhibits the toxin under normal circumstances. Cellular stress causes a shift in the toxin/antitoxin ratio to favor the free toxin, which is released to act on its cellular target and arrest growth. TA systems therefore present potential targets for novel antibiotics, as a molecule with the capacity to artificially induce toxin activation could have an antibacterial effect. Described herein is the investigation of the Staphylococcus aureus YefM-YoeBSa1 and YefM-YoeBSa2 TA systems as targets for this artificial activation strategy. Following establishment of the prevalence, conservation, and transcription of the yefM-yoeBSa1 and yefM-yoeBSa2 genes in clinical isolates of methicillin-resistant S. aureus, a peptide activator of the YefM-YoeBSa1 TA system was sought by screening phage-displayed peptide libraries against the YefMSa1 antitoxin. Additionally, a novel strategy was devised to express the YoeBSa1 toxin in an inactive, non-toxic form. Characterization of the activity of YoeBSa1 led to the design of a fluorogenic substrate that can be used to screen for activators of this toxin in a high-throughput manner. Item withdrawn by Mark Zulauf (zulauf@illinois.edu) on 2013-04-22T15:37:24Z Item was in collections: University of Illinois Theses & Dissertations (ID: 1) No. of bitstreams: 2 Larson_Amy.docx: 5124480 bytes, checksum: 4df59701a40f872b27b042d9b6da0aa0 (MD5) Larson_Amy.pdf: 3212970 bytes, checksum: ff9f72f2f0c3c5aca7d4f8e20edd66c3 (MD5) Made available in DSpace on 2013-05-24T22:16:25Z (GMT). No. of bitstreams: 3 Amy_Larson.pdf: 3072816 bytes, checksum: 6a2219dd33f2ff2a28303c04cf46344a (MD5) Larson_Amy.docx: 5133113 bytes, checksum: 0a6c09ceb067d7e07645532b2a12eaa6 (MD5) license.txt: 4060 bytes, checksum: 3e2e8457cc08f37d535e2cd06fe861a0 (MD5) Restriction data tranferred 2014-07-01T11:36:11-05:00 Original Data Group with Access UIUC Users [automated] Release Date: 2015-05-24 17:18:31 UTC Reason: Author requested U of Illinois access only (OA after 2yrs) in Vireo ETD system Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Seth Robbins (srobbins@illinois.edu) on 2013-05-24T22:18:59Z Item is restricted until 2015-05-24T22:18:31Z U of I Only Restriction Lifted for Item 44418 on 2015-05-24T10:01:42Z. http://hdl.handle.net/2142/44445 en Copyright 2013 Amy Susanne Larson toxin-antitoxin system antibacterial Investigation of the YefM-YoeBSa toxin-antitoxin systems as novel antibacterial targets text Chemistry 1413 Chemistry 0335 University of Illinois at Urbana-Champaign Thesis M.S. MS:Chemistry -UIUC 10KS0335MS