Skip to main content
ARS Home » Research » Publications at this Location » Publication #212480

Title: Monoclonal antibodies reactive with chicken interleukin-17

item CHANG, H
item Lillehoj, Hyun

Submitted to: Veterinary Immunology and Immunopathology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 8/20/2007
Publication Date: 4/20/2008
Citation: Yoo, J., Chang, H.H., Bae, Y., Seoung, C., Lillehoj, H.S., Min, W. 2008. Monoclonal antibodies reactive with chicken interleukin-17. Veterinary Immunology and Immunopathology. 121:359-363.

Interpretive Summary: Host immune response to microbial pathogens is complex and involves many different types of lymphocytes and their soluble mediators. Lymphokines are soluble hormone-like factors which are locally secreted by lymphocytes upon their interaction with microbes and they mediate various types of immune responses. In this study, ARS scientists developed mouse monoclonal antibodies which detect chicken IL-17 and characterized their binding specificity against recombinant chicken IL-17. Using biochemical and molecular assays, these antibodies showed specificity to recombinant chicken IL-17a. Because IL-17a lymphokine is known to have various biological function during early response to invading pathogens, the development of these antibodies which are specific for IL-17a will be useful for detection of IL-17 production in various tissues. More importantly, IL-17 has been shown to exert an important role in host defense mechanisms against viral, bacterial and parasitic infections. Thus, availability of antibodies that are specific for chicken IL-17 will provide a new important tool that can be used for detailed investigation of IL-17 in many poultry diseases including avian coccidiosis.

Technical Abstract: In our previous study chicken interleukin -17 (chIL-17) gene was cloned from the expressed sequence tag (EST) cDNA library and initially analyzed. To further investigate biological properties of chicken IL-17, six monoclonal antibodies (mAbs) against bacterially expressed protein were produced and characterized their binding specificities. Antibodies were reactive with recombinant chIL-17 by enzyme-linked immunosorbent assay (ELISA). On Western blot analyses, mAbs identified 20 and 21 kDa proteins both in the supernatant and lysate of CU205 cells and in conconavalin A (Con A)-activated splenic lymphocytes, but not normal spenic lymphocytes. Furthermore, mAbs detected a 16 kDa protein in the lysate of CU205 cells treated with tunicamycin. An intracellular protein in CU205 cells was recognized by three mAbs using flow cytometric analysis. These results indicate that mAbs specific for chIL-17 are useful for further structural and immunological studies of chIL-17.