Structural and functional homology among chicken, duck, goose, turkey and pigeon interleukin-8 proteins.
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.
Wu
Yung Fu
YF
Graduate Institute of Veterinary Microbiology, College of Veterinary Medicine, National Chung Hsing University, Taichung, Taiwan.
Shien
Jui Huang
JH
Yin
Hsien Hseng
HH
Chiow
Shiou Her
SH
Lee
Long Huw
LH