Mutational analysis of chicken interleukin 2

被引:30
作者
Kolodsick, JE [1 ]
Stepaniak, JA [1 ]
Hu, WP [1 ]
Sundick, RS [1 ]
机构
[1] Wayne State Univ, Sch Med, Dept Immunol & Microbiol, Detroit, MI 48201 USA
关键词
D O I
10.1006/cyto.2001.0846
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 [生物化学与分子生物学]; 081704 [应用化学];
摘要
Chicken interleukin 2 (chlL-2) has low, but significant, homology to both mammalian IL-2 and mammalian IL-15, In vie,v 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 nonmammalian IL-2 mutational analysis and proposes a model for the interaction between chIL-2 and its receptor. (C) 2001 Academic Press.
引用
收藏
页码:317 / 324
页数:8
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