Characterization and antimicrobial mechanism of CF-14, a new antimicrobial peptide from the epidermal mucus of catfish. Issue 92 (September 2019)

• Record Type: Journal Article
• Authors: Li, Tingting; Liu, Quanwei; Wang, Dangfeng; Li, Jianrong
• Is Part Of: Fish & shellfish immunology. Issue 92(2019)
• Page Start: 881
• Page End: 888
• Publication Date: 2019-09
• Subjects: CF-14 -- Antimicrobial peptide -- S. putrefaciens -- Characterization -- Mechanism; Fishes -- Immunology -- Periodicals; Shellfish -- Immunology -- Periodicals; Poissons -- Immunologie -- Périodiques; Crustacés -- Immunologie -- Périodiques; 571.9617
• DOI: 10.1016/j.fsi.2019.07.015
• Languages: English
• ISSNs: 1050-4648

Abstract

Abstract: In this study, we identified a novel antibacterial peptide, RIVELTLPRVSVRL-NH2 (named CF-14), derived from the epidermal mucus of catfish and characterized its antimicrobial activity. Analysis of antimicrobial activity and hemolytic activity of CF-14 revealed broad spectrum, high levels of antimicrobial activity and low toxicity to eukaryotic cells. CF-14 remained stable at pH values ranging from 4.0 to 12.0 and remained bioactive when exposed to high temperature. CD analysis indicated that CF-14 forms a random coil in PBS buffer and an α-helical conformation in the membrane-mimetic 2.5% SDS micelle. Additionally, the antibacterial mechanism of CF-14 against Shewanella putrefaciens was investigated. Membrane permeability experiments confirmed that CF-14 could increase cell wall membrane permeability and cause nucleotide leakage. Moreover, observations performed using scanning electron and confocal microscopy indicated that CF-14 could penetrate into the cell membranes of S. putrefaciens and accumulate in bacterial cells, but did not break down cell membranes. Further, electrophoresis analysis demonstrated that CF-14 possesses DNA-binding affinity. The results provide a substantial basis for future application of CF-14, a novel cell-penetrating peptide (CPP) derived from catfish. Graphical abstract: Image 1 Highlights: The antimicrobial activity of a novel 14-residue antimicrobial peptide "CF-14" was investigated. CF-14 can penetrate the S. putrefaciens cell membranes and accumulate in the cytoplasm. CF-14 possesses DNA binding affinity. CF-14 could be suitable for use in seafood preservation as a novel antibiotic.