In vitro immunomodulatory activities of peptides derived from Salmo salar NK-lysin and cathelicidin in fish cells

Acosta J.; Roa F.; González-Chavarría I.; Astuya A.; Maura R.; Montesino R.; Muñoz C.; Camacho F.; Saavedra P.; Valenzuela A.; Sánchez O.; Toledo J.R.

Abstract

Antimicrobial peptides (AMPs) are amphipathic peptides, which play an important role in innate defence. These peptides are gene-encoded and either constitutively expressed and/or upregulated during an infection. NK-lysins are AMPs with a three-dimensional globular structure. They are larger molecules, which comprise 74-78 amino acid residues and six conserved cysteine residues forming three disulphide bonds. Cathelicidins are a family of antimicrobial peptides that act as important components of the innate immune system with a broad spectrum of antimicrobial activity and immunomodulatory properties. Although they are widely studied in mammals, little is known about their immunomodulatory function. In the present study, we identified and characterized for the first time four NK-lysin-like transcripts from Atlantic salmon (Salmo solar) based on EST reported sequences. In vitro, NK-lysin derived peptides were able to induce the expression of IL-1 beta and IL-8 in Salmo solar head kidney leukocytes. We also tested Salmo solar cathelicidin 1 derived peptide in a similar assay, showing its ability to induce the expression of IFN-gamma. These results indicate that NK-lysin and cathelicidin 1 derived peptides are able to modulated immune response, suggesting their potential use to enhance immune response in fish.

Más información

Título según WOS: In vitro immunomodulatory activities of peptides derived from Salmo salar NK-lysin and cathelicidin in fish cells
Título según SCOPUS: In vitro immunomodulatory activities of peptides derived from Salmo salar NK-lysin and cathelicidin in fish cells
Título de la Revista: FISH & SHELLFISH IMMUNOLOGY
Volumen: 88
Editorial: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Fecha de publicación: 2019
Página de inicio: 587
Página final: 594
Idioma: English
DOI:

10.1016/j.fsi.2019.03.034

Notas: ISI, SCOPUS