In the present study, the complete characterization of cDNA and genomic sequences of IL-1b and IL-8, as well as the expression profile of these genes in the South American fish pacu (Piaractus mesopotamicus) is provided. The full-length pmIL-1b cDNA was composed of 1208 nucleotides that would produce a precursor peptide with 273 amino acid residues. A putative caspase-1 cleavage site, similar to what is found in mammalian IL-1b, was identified producing a mature peptide with a theoretical molecular weight of 17.21 kDa. The pmIL-8 cDNA sequence consisted of 1019 nucleotides which encoded a 95-amino acid protein with a theoretical molecular weight of 10.43 kDa that showed all typical CXC chemokine features, including a 20-residue signal peptide and four conserved cysteine residues. Constitutive mRNA expression was detected for both genes in the liver, head kidney, gill, intestine, skin and spleen. After a bacterial challenge, up-regulation was detected for both pmIL-1b and pmIL-8 in the spleen and head kidney at 12 h post-infection. At 24 h post-infection there was a decrease in the expression of both genes, with pmIL-8 showing a significant down-regulation in the liver and head kidney when compared to the control groups.
Imunização de lambaris (Astyanax lacustris) com o gene que codifica o antígeno de imobilização IAG52A de Ichthyophthirius multifiliis associado com a citocina IL-8 de A. lacustris como adjuvante molecular Pirassununga 2022 2 CAROLINE MUNHOZ MEIRA Imunização de lambaris (Astyanax lacustris) com o gene que codifica o antígeno de imobilização IAG52A de Ichthyophthirius multifiliis associado com a citocina IL-8 de A. lacustris como adjuvante molecular
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