Abstract
Interleukin (IL)-8-encoding regions of five avian species were cloned, sequenced and characterized. Each IL-8-encoding region is 312 nucleotides long and encodes IL-8 which is 103 amino acids. Pairwise sequence analysis showed that sequence identities of IL-8-encoding regions ranged from 87% to 100%. The IL-8 protein identities varied from 84% to 100%. Phylogenetic analysis indicated that IL-8-encoding regions and encoded proteins of chicken, duck, goose and turkey clustered together and evolved into a distinct phylogenetic lineage from that of pigeon which evolved into a second lineage. The results from binding reactivities of antiserum against each recombinant IL-8 (rIL-8) protein to homologous or heterologous rIL-8 proteins, chemotactic activities of each rIL-8 protein or reduction levels of the chemotactic activity of rIL-8 protein which was pretreated with homologous or heterlogous antiserum have suggested that all five IL-8 proteins were functionally active, and shared structural and functional identity with each other.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
