<p>Amb a 1 is the major allergen found in ragweed. Our observations have suggested that Amb a 1 may bind lipopolysaccharide (LPS), which would likely contribute to the allergenicity of Amb a 1. In order to assess whether Amb a 1 can bind LPS, peptide sequences from Amb a 1 were assayed for their ability to bind to LPS using an ELISA based LPS binding assay. A 15 amino acid sequence in the β- chain of Amb a 1 demonstrated affinity for biotin labeled <em>E. coli </em>LPS. The sequence also bound to <em>P.</em> <em>aeruginosa</em> LPS, which is structurally disparate in the lipid A region, indicating that the sequence has flexibility in recognizing different lipid A moieties, or that the binding site may not include the lipid A portion of the LPS molecule. An IL-10 ELISA was also used to determine whether the LPS bound to the peptides induced an immunological response in leukocytes. Peptides containing the LPS-binding sequence were able to bind to LPS and induce IL-10 production, suggesting the interaction between Amb a 1 and LPS may have immunological consequences. We have identified a sequence within the major ragweed allergen Amb a 1 that has the potential to bind to LPS. This indicates that the allergen may provide its own adjuvant when encountered by the immune system, leading to an enhanced immunological response to an otherwise innocuous environmental protein.</p> / Master of Science (MSc)
| Identifer | oai:union.ndltd.org:mcmaster.ca/oai:macsphere.mcmaster.ca:11375/12634 |
| Date | 10 1900 |
| Creators | Bysice, Andrew |
| Contributors | Larché, Mark, Biochemistry |
| Source Sets | McMaster University |
| Detected Language | English |
| Type | thesis |
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