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Joanna Shisler Hinthong, Olivia 2015-09-28T15:17:36Z 2015-09-28T15:17:36Z 10000-01-01 2010 2010 This dissertation elaborates on M2's molecular functioning as a viral immunomodulator to inhibit both the ERK1/2 and NF-kappaB pathways, which is reliant on its glycosylation status and proper cellular trafficking within the infected cell. As M2 has no homology to any known viral or cellular protein, this suggests a novel immunoregulatory function. Data contained within this dissertation provides insight into the molecular mechanism of an ER-localized protein, and its impact on cytoplasmic signaling pathways within the context of an anti-viral immune response. Made available in DSpace on 2015-09-28T15:17:36Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3455728.pdf: 63948126 bytes, checksum: edd950183c0aed8399c7cd1992e06ecc (MD5) Previous issue date: 2010 Embargo set by: Seth Robbins for item 87997 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 187 p. Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2010. http://hdl.handle.net/2142/86716 (MiAaPQ)AAI3455728 eng Biology, Virology Characterization of the Glycosylation and Signal Peptide Sequences Within the Vaccinia Virus M2 Protein and Influence on ERK1/2 and Nf-Kappab Activation text Microbiology Microbiology University of Illinois at Urbana-Champaign Dissertation Ph.D.