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%...

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Bibliographic Details
Published in:Veterinary immunology and immunopathology 2008-10, Vol.125 (3), p.205-215
Main Authors: Wu, Yung Fu, Shien, Jui Huang, Yin, Hsien Hseng, Chiow, Shiou Her, Lee, Long Huw
Format: Article
Language:English
Subjects:
Amino Acid Sequence
amino acid sequences
animal proteins
Animals
antigenic variation
Avian species
Base Sequence
Blotting, Western - veterinary
Chemotaxis
Chemotaxis assay
Chicken IL-8
chickens
Cloning, Molecular
Columbidae - genetics
Columbidae - immunology
DNA - chemistry
DNA - genetics
ducks
Enzyme-Linked Immunosorbent Assay - veterinary
geese
genetic variation
Homology
immune system
immunogenetics
Interleukin (IL)-8
interleukin-8
Interleukin-8 - genetics
Molecular cloning
molecular genetics
Molecular Sequence Data
nucleotide sequences
Phylogenetic analysis
Phylogeny
Polymerase Chain Reaction - veterinary
Poultry - genetics
Poultry - immunology
Recombinant Proteins - genetics
Sequence Alignment
sequence homology
turkeys
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Summary: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.
ISSN:0165-2427
1873-2534
DOI:10.1016/j.vetimm.2008.03.001