Identification of a moronecidin-like antimicrobial peptide in the venomous fish Pterois volitans: Functional and structural study of pteroicidin-α. Issue 72 (January 2018)

• Record Type: Journal Article
• Authors: Houyvet, Baptiste; Bouchon-Navaro, Yolande; Bouchon, Claude; Goux, Didier; Bernay, Benoît; Corre, Erwan; Zatylny-Gaudin, Céline
• Is Part Of: Fish & shellfish immunology. Issue 72(2018)
• Page Start: 318
• Page End: 324
• Publication Date: 2018-01
• Subjects: Pterois volitans -- Antimicrobial peptides -- Amidation -- Piscidin -- Pteroicidin A -- Pteroicidin α; Fishes -- Immunology -- Periodicals; Shellfish -- Immunology -- Periodicals; Poissons -- Immunologie -- Périodiques; Crustacés -- Immunologie -- Périodiques; 571.9617
• DOI: 10.1016/j.fsi.2017.11.003
• Languages: English
• ISSNs: 1050-4648

Abstract

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. Highlights: Characterization of pteroicidin-α, the first piscidin evidenced in lionfish. Identification of amidated and non-amidated pteroicidin-α by MS/MS. Greater antibacterial and hemolytic activity levels with pteroicidin-α-CONH2 . Impact of amidation of pteroicidin-α on structure/function relationship.