Chicken interleukin 2 (chlL-2) has low, but significant, homology to both m
ammalian IL-2 and mammalian IL-15, In vie,v of its unique phylogenetic posi
tion and potential use as a vaccine adjuvant, a detailed mutational analysi
s 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 recep
tor, which is similar to results obtained for mammalian IL-2 and IL-15, Ana
lysis of the C terminus did not reveal a single critical amino acid. Howeve
r, deletion mutant studies demonstrated that removal of C terminal amino ac
ids 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 i
nteraction between chIL-2 and its receptor. (C) 2001 Academic Press.