Background: Interleukin 8 is a chemokine that is produced by several types of cells, like macrophages
and has chemotactic activity in particular on neutrophils, playing a key role during the inflammatory
process. It has been demonstrated at the molecular level that this molecule is present and conserved
in several vertebrate groups, pointing its importance. Analysis of the amino acid sequence of IL-8,
projected from cDNA of
Salmo salar
, presents homology with the sequences of mammals, poultry and
lamprey, indicating the presence of a homologous molecule in higher fish. However, there is no
information at protein level, which allows characterizing the regulatory role of this molecule during the
immune response in fish.
Results: In this work, we designed and synthesized an epitope peptide of 10
residues with a purity of 95% and mass of 1158.7 kDa, which showed a random coil structure. From
this peptide it was able to generate a polyclonal mono-specific antibody which was capable of detecting
the whole molecule of IL-8 in tissue and cellular model of salmonids.
Conclusions: The resulting
antibody is a versatile tool for detecting IL-8 by different immune techniques such as ELISA, dot blot,
western blotting and immunocytofluorescence. Analysis of IL-8 at proteomic level is a useful method for
characterizing immune properties of this molecule in fish.
