|JEONG, MI SUN - US Department Of Agriculture (USDA)|
|DEL CACHO, EMILIO - University Of Zaragoza|
|MIN, WONGI MIN - Gyeongsang National University|
|JEOUNG, HYEYOUNG - Animal, Plant And Fisheries Quarantine And Inspection Agency (QIA)|
|AN, DONG JUNE - Animal, Plant And Fisheries Quarantine And Inspection Agency (QIA)|
Submitted to: Poultry Science
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/1/2014
Publication Date: 7/18/2014
Publication URL: http://handle.nal.usda.gov/10113/61084
Citation: Lee, S.H., Lillehoj, H.S., Jeong, M., Del Cacho, E., Min, W., Jeoung, H., An, D. 2014. Development and characterization of mouse monoclonal antibodies reactive with chicken IL-1ß. Poultry Science. 93(9):2193-2198.
Interpretive Summary: Limited availability of diagnostic reagents to assess immune responses in poultry and the lack of information on key molecules that regulate the immune response of poultry hinder rapid progress in poultry immunology and vaccine development. In this study, ARS scientists collaborated with other scientists to produce an immune factor that identifies a chicken protein important for the initiation of the immune response to infectious agents in poultry. Furthermore, this immune factor was used to develop a diagnostic reagent that can be used to assess the level and production of the immune response protein in chicken tissues and serum during various infections in poultry. The results showed that the new diagnostic reagent, not only detects the immune response protein, but also can be used to examine immune response, both which will be important to study the chicken’s immunity further. The availability of this valuable immune reagent for poultry will enhance basic and applied immunology research for scientists worldwide.
Technical Abstract: Two mouse monoclonal antibodies (mAbs) specific for chicken interleukin-1ß (chIL-1ß) were produced and characterized. Both mAbs identified a 66.0 kDa recombinant protein expressed in Escherichia coli by Western blot analysis that corresponded to the expected molecular weight of a recombinant fusion protein containing the full-length 23.0 kDa chIL-1ß protein and a 43.0 kDa maltose binding protein tag. Immunohistochemical analysis identified cells producing endogenous chIL-1ß in the caecal tonsils, bursa of Fabricius, and spleen. Purified recombinant chIL-1ß dose-dependently stimulated the proliferation and nitric oxide production by thymocytes and both activities were inhibited by co-incubation with the two chIL-1ß mAbs. These mAbs will be important immune reagents for future basic and applied poultry research.