A piscidin-like antimicrobial peptide from the icefish Chionodraco hamatus (Perciformes: Channichthyidae): Molecular characterization, localization and bactericidal activity

Buonocore, Francesco; Randelli, Elisa; Casani, Daniela; Picchietti, Simona; Belardinelli, Maria Cristina; Pascale, Donatella de; Santi, Concetta De; Scapigliati, Giuseppe

doi:10.1016/j.fsi.2012.09.005

Cited by 46 publications

(43 citation statements)

References 52 publications

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“…Piscidins are mainly expressed in gill, skin and intestine, although can be also found in head-kidney and spleen [10,43,47,50,58,101,102]. However, in Atlantic cod piscidin was found to be ubiquitous, being detected in chondrocytes, heart, oocytes, exocrine and endocrine glands, swim bladder, and other tissues [103].…”

Section: Piscidinsmentioning

confidence: 99%

“…Nevertheless, the expression profiles vary depending on the isoform [39,78,83]. Moreover, specifically among the cell types where piscidin has shown to be expressed are mast cells, rodlet cells, phagocytic granulocytes and eosinophilic granular cells [43,88,102,104,105]. Interestingly, there is evidence that granulocytes can destroy bacteria in phagosome by intracellular release of piscidin, meaning that piscidin can act against extra and intracellular bacteria [102].…”

Section: Piscidinsmentioning

confidence: 99%

“…Like AMP genes from mammals, piscidin genes can be induced by a variety of stimuli, including Gram-positive and -negative bacteria [78], bacteria cell components like LPS [43,50,58] or the bacterial antigen ASAL [10]. The LPS-mediated induction of epinecidin-1 in zebrafish was shown to require hepatocyte nuclear factor 1 [89].…”

Section: Piscidinsmentioning

confidence: 99%

“…The LPS-mediated induction of epinecidin-1 in zebrafish was shown to require hepatocyte nuclear factor 1 [89]. Furthermore, piscidin genes are induced by parasites [47,104,106], viruses [107], and poly I:C [43,58]. Another study demonstrated that high biomass density ( i.e.…”

Section: Piscidinsmentioning

confidence: 99%

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Antimicrobial Peptides from Fish

2014

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Antimicrobial peptides (AMPs) are found widely distributed through Nature, and participate in the innate host defense of each species. Fish are a great source of these peptides, as they express all of the major classes of AMPs, including defensins, cathelicidins, hepcidins, histone-derived peptides, and a fish-specific class of the cecropin family, called piscidins. As with other species, the fish peptides exhibit broad-spectrum antimicrobial activity, killing both fish and human pathogens. They are also immunomodulatory, and their genes are highly responsive to microbes and innate immuno-stimulatory molecules. Recent research has demonstrated that some of the unique properties of fish peptides, including their ability to act even in very high salt concentrations, make them good potential targets for development as therapeutic antimicrobials. Further, the stimulation of their gene expression by exogenous factors could be useful in preventing pathogenic microbes in aquaculture.

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Section: Piscidinsmentioning

confidence: 99%

Section: Piscidinsmentioning

confidence: 99%

Section: Piscidinsmentioning

confidence: 99%

Section: Piscidinsmentioning

confidence: 99%

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Antimicrobial Peptides from Fish

2014

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“…To date, there have been many AMPs isolated from teleosts [1], [6]–[8], [14], [15]. Among the most common and potent AMP family present in fish is the piscidins, linear cationic α-helical peptides, except for Atlantic Cod piscidin [3], [7], [16].…”

Section: Introductionmentioning

confidence: 99%

The Effect of an Adding Histidine on Biological Activity and Stability of Pc-pis from Pseudosciaena crocea

Mao

Niu

et al. 2013

PLoS ONE

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Pc-pis is a novel piscidin-like antimicrobial polypeptide that was identified in Pseudosciaena crocea. Although active against most bacteria tested, Pc-pis was inactive against Aeromonas hydrophila and Pseudomonas aeruginosa. The Pc-pis analogue Pc-pis-His was designed by adding a histidine residue at the carboxyl terminal. Pc-pis-His demonstrated a more broad-spectrum and stronger antimicrobial activity against a representative set of microorganisms and more potent antiparasitic activity against Cryptocaryon irritans trophonts than Pc-pis. The stability assay revealed that Pc-pis-His was active against Staphylococcus aureus not only in acidic (pH 5.5–7.3) and relatively low concentration monovalent cation (0–160 mM NaCl) environments but also in alkaline (pH 7.5–9.5), divalent cation (1.25–160 mM MgCl2 and 1.25–40 mM CaCl2) and high concentration monovalent cation (320–2560 mM NaCl) environments, which indicates that the added histidine residue conferred better salt-, acid- and alkali-tolerance to Pc-pis-His. Pc-pis-His also possessed the desired heat-tolerance, which was reflected by the antimicrobial activity of the peptide after being boiled for 10–60 minutes. Hemolytic activity analysis revealed that Pc-pis-His at concentrations up to 6 µM exhibited no hemolysis against human erythrocytes, with 6 µM being a concentration that is highly active against most of the microorganisms tested, although the hemolytic activity of Pc-pis-His was enhanced compared to Pc-pis. These results provide a unique, reasonable basis for designing novel piscidins with potent, broad-spectrum and stable antimicrobial activity and new insight into the future development of piscidins as potential therapeutic agents against microbial and external protozoan parasite infections.

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Isalo scorpion cytotoxic peptide‐strengthened immune function through the JAKs/STATs signaling pathway of the immune organ of grass carp (Ctenopharyngodon idella) challenged with Aeromonas hydrophila

He,

Hu,

Zhou

et al. 2024

Animal Research and One Health

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To investigate the impact of Isalo scorpion cytotoxic peptide (IsCT) on the immune function of immune organ (head kidney, spleen, and skin) of grass carp (Ctenopharyngodon idella), 540 fish (136.88 ± 0.72 g) were supplied with a different amount of IsCT (0, 0.6, 1.2, 1.8, 2.4, and 3.0 mg/kg diet) through a period of 60 days. Afterward, 24 fish were randomly selected from each group and were inoculated with Aeromonas hydrophila for a period of 6 days. Our findings suggested that appropriate IsCT complementation: (1) attenuated skin morbidity and histopathological structural changes in the head kidney and spleen (p < 0.05), which ensured the structural integrity of the immune organs; (2) increased the activity and expression of immune substances (p < 0.05), which in turn increased the function of the immune organs, promoting immune responses; (3) through the regulation of the Janus kinase/signal transducers and activators of transcription (JAKs/STATs) signaling pathway, the mRNA expression of anti‐inflammatory cytokines increased and the mRNA expression of pro‐inflammatory cytokines decreased, which in turn increased the function of the immune organs, reducing the inflammatory response (p < 0.05). However, the addition of IsCT did not affect the expression of IL‐12p35, STAT2, and STAT3a in the immune organ. Ultimately, this study provided evidence that IsCT enhanced immune function via the JAKs/STATs signaling pathway in the immune organ in grass carp after challenged with Aeromonas hydrophila.

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A piscidin-like antimicrobial peptide from the icefish Chionodraco hamatus (Perciformes: Channichthyidae): Molecular characterization, localization and bactericidal activity

Cited by 46 publications

References 52 publications

Antimicrobial Peptides from Fish

Antimicrobial Peptides from Fish

The Effect of an Adding Histidine on Biological Activity and Stability of Pc-pis from Pseudosciaena crocea

Isalo scorpion cytotoxic peptide‐strengthened immune function through the JAKs/STATs signaling pathway of the immune organ of grass carp (Ctenopharyngodon idella) challenged with Aeromonas hydrophila

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