Mutational analysis of chicken interleukin 2 |
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Authors: | Kolodsick J E Stepaniak J A Hu W Sundick R S |
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Affiliation: | Department of Immunology and Microbiology, Wayne State University, Detroit, Michigan 48201, USA. |
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Abstract: | Chicken interleukin 2 (chIL-2) has low, but significant, homology to both mammalian IL-2 and mammalian IL-15. In view of its unique phylogenetic position and potential use as a vaccine adjuvant, a detailed mutational analysis for critical functional sites was undertaken. It was found that Asp17 is a critical N terminal contact site for binding to the putative chIL-2 receptor, which is similar to results obtained for mammalian IL-2 and IL-15. Analysis of the C terminus did not reveal a single critical amino acid. However, deletion mutant studies demonstrated that removal of C terminal amino acids yielded proteins with decreased bioactivity and that this decrease was a function of the number and kind of amino acids removed. This study is the first non-mammalian IL-2 mutational analysis and proposes a model for the interaction between chIL-2 and its receptor. |
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Keywords: | IL-2/mutagenesis/structure– function/T cell |
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