Identification of a moronecidin-like antimicrobial peptide in the venomous fish Pterois volitans: Functional and structural study of pteroicidin-α.
Fish Shellfish Immunol
; 72: 318-324, 2018 Jan.
Article
en En
| MEDLINE
| ID: mdl-29108968
ABSTRACT
The present study characterizes for the first time an antimicrobial peptide in lionfish (Pterois volitans), a venomous fish. Using a peptidomic approach, we identified a mature piscidin in lionfish and called it pteroicidin-α. We detected an amidated form (pteroicidin-α- CONH2) and a non-amidated form (pteroicidin-α-COOH), and then performed their functional and structural study. Interestingly, the two peptides displayed different antibacterial and hemolytic activity levels. Pteroicidin-α-CONH2 was bactericidal on human pathogens like Staphylococcus aureus or Escherichia coli, as well as on the fish pathogen Aeromonas salmonicida, while pteroicidin-α-COOH only inhibited their growth. Furthermore, the two peptides induced hemolysis of red blood cells from different vertebrates, namely humans, sea bass and lesser-spotted dogfish. Hemolysis occurred with low concentrations of pteroicidin-α-CONH2, indicating greater toxicity of the amidated form. Circular dichroism analysis showed that both peptides adopted a helical conformation, yet with a greater α-helix content in pteroicidin-α-CONH2. Overall, these results suggest that amidation strongly influences pteroicidin-α by modifying its structure and its physico-chemical characteristics and by increasing its hemolytic activity.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Staphylococcus aureus
/
Péptidos Catiónicos Antimicrobianos
/
Proteínas de Peces
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Aeromonas salmonicida
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Escherichia coli
/
Peces
/
Antibacterianos
Tipo de estudio:
Diagnostic_studies
/
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Fish Shellfish Immunol
Asunto de la revista:
BIOLOGIA
/
MEDICINA VETERINARIA
Año:
2018
Tipo del documento:
Article
País de afiliación:
Francia