Alpha-helical domain from IL-8 of salmonids: Mechanism of action and identification of a novel antimicrobial function.
Biochem Biophys Res Commun
; 498(4): 803-809, 2018 04 15.
Article
em En
| MEDLINE
| ID: mdl-29530531
ABSTRACT
In this work, the potential antimicrobial role and mechanism of action of α-helix domain of trout and salmon IL-8 against Eschericia coli, Pseudomonas aeruginosa and Staphylococcus aureus was investigated. By an in silico analysis of the primary structure of IL-8 from Oncorhynchus mykiss and salmo salar, it was evidenced that γ-core motif was present, as in the vast majority of kinocidins. The α-helix domain of IL-8 (αIL-8) was synthesized by solid phase peptide synthesis and showed a tendency to form an α-helix conformation, as revealed by circular dichroism. Additionally, it was demonstrated that αIL-8 from both species showed antimicrobial activity against E. coli, P. aeruginosa and S. aureus. Membrane permeabilization and co-localization assay, as well as scanning electron microscopy, showed that these peptides were accumulated on the cell surface and in the cytoplasm, suggesting that they were capable of permeabilizing and disrupt the bacterial membranes and interact with cytoplasmic components. Our results represent the first analysis on the antimicrobial function of IL-8-derived peptide from salmonids.
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Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Salmonidae
/
Interleucina-8
/
Proteínas de Peixes
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Anti-Infecciosos
Tipo de estudo:
Diagnostic_studies
/
Prognostic_studies
Limite:
Animals
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Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
Chile