Abstract
By searching a chicken EST database, we identified a cDNA clone that appeared to contain the entire open reading frame (ORF) of chicken interleukin-18 (ChIL-18). The encoded protein consists of 198 amino acids and exhibits approximately 30% sequence identity to IL-18 of humans and various others mammals. Sequence comparisons reveals a putative caspase-1 cleavage site at aspartic acid 29 of the primary translation product, indicating that mature ChIL-18 might consist of 169 amino acids. Bacterially expressed ChIL-18 in which the N-terminal 29 amino acids of the putative precursor molecule were replaced by a histidine tag induced the synthesis of interferon-γ (IFN-γ) in cultured primary chicken spleen cells, indicating that the recombinant protein is biologically active.
| Item Type: | Journal article |
|---|---|
| Form of publication: | Publisher's Version |
| Faculties: | Veterinary Medicine |
| Subjects: | 600 Technology > 610 Medicine and health |
| URN: | urn:nbn:de:bvb:19-epub-14787-5 |
| ISSN: | 1557-7465 |
| Language: | English |
| Item ID: | 14787 |
| Date Deposited: | 19. Mar 2013 12:06 |
| Last Modified: | 04. Nov 2020 12:55 |
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