2026-09-21T10:24:22Z https://www.ideals.illinois.edu/oai-pmh

oai:www.ideals.illinois.edu:2142/86690 2023-07-11 col_2142_5131 col_2142_16338 com_2142_5130 com_2142_16337 com_2142_14793 com_2142_8903

Kranz, David M. Buonpane, Rebecca Ann 2015-09-28T15:17:27Z 2015-09-28T15:17:27Z 10000-01-01 2006 2006 Chapter four describes the engineering of murine Vbeta8.2 for picomolar affinity to staphylococcal enterotoxin B (SEB). As the known contact regions had already been heavily mutagenized, additional engineering of the Vbeta was performed through extension of the CDR1 loop. Soluble forms of the high-affinity Vbeta regions were tested for their ability to inhibit SEB-mediated T cell cytotoxicity in vitro. As the affinity of the Vbeta regions increased, the amount of protein needed to neutralize 50% of the toxin activity correspondingly decreased. These Vbeta regions were also tested in various rabbit models of toxic shock by Patrick Schlievert, and were remarkably effective at protecting rabbits from the lethal effects of the toxin. Made available in DSpace on 2015-09-28T15:17:27Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3250214.pdf: 6331406 bytes, checksum: 8a96c789714dc0aa5867949745b2bfd4 (MD5) Previous issue date: 2006 Embargo set by: Seth Robbins for item 87971 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs U of I Only 212 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2006. http://hdl.handle.net/2142/86690 (MiAaPQ)AAI3250214 eng Health Sciences, Immunology Engineering Soluble, High Affinity Receptor Antagonists for Bacterial Exotoxins text Microbiology Microbiology University of Illinois at Urbana-Champaign Dissertation Ph.D.