Mutational analysis of chicken interleukin 2.
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.
Kolodsick
J E
JE
Department of Immunology and Microbiology, Wayne State University, Detroit, Michigan 48201, USA.
Stepaniak
J A
JA
Hu
W
W
Sundick
R S
RS
D000409:Alanine / Q000737:chemistry; D000595:Amino Acid Sequence; D000818:Animals; D001224:Aspartic Acid / Q000737:chemistry; D001665:Binding Sites; D002455:Cell Division; D002645:Chickens; D003208:Concanavalin A / Q000494:pharmacology; D004252:DNA Mutational Analysis; D018076:DNA, Complementary / Q000378:metabolism; D017353:Gene Deletion; D006801:Humans; D019409:Interleukin-15 / Q000737:chemistry; D007376:Interleukin-2 / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D010802:Phylogeny; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013154:Spleen / Q000166:cytology
D018076:DNA, Complementary; D019409:Interleukin-15; D007376:Interleukin-2; D011994:Recombinant Proteins; D003208:Concanavalin A; D001224:Aspartic Acid; D000409:Alanine