Antimicrobial Peptides from Fish

Masso-Silva, Jorge A; Diamond, Gill

doi:10.3390/ph7030265

Cited by 264 publications

(200 citation statements)

References 226 publications

(399 reference statements)

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“…The substitution of Ser 12 with Ala significantly impairs the activity of the native peptide, indicating that a polar residue on the hydrophobic face of the peptide is fundamental for activity. This was a key feature also of other AMPs, as previously reported (35,36).…”

Section: Resultsmentioning

confidence: 99%

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Structural Insights into and Activity Analysis of the Antimicrobial Peptide Myxinidin

Cantisani

Finamore

Mignogna

et al. 2014

Antimicrob Agents Chemother

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eThe marine environment has been poorly explored in terms of potential new molecules possessing antibacterial activity. Antimicrobial peptides (AMPs) offer a new potential class of pharmaceuticals; however, further optimization is needed if AMPs are to find broad use as antibiotics. We focused our studies on a peptide derived from the epidermal mucus of hagfish (Myxine glutinosa L.), which was previously characterized and showed high antimicrobial activity against human and fish pathogens. In the present work, the activities of myxinidin peptide analogues were analyzed with the aim of widening the original spectrum of action of myxinidin by suitable changes in the peptide primary structure. The analysis of key residues by alanine scanning allowed for the design of novel peptides with increased activity. We identified the amino acids that are of the utmost importance for the observed antimicrobial activities against a set of pathogens comprising both Gram-negative and Gram-positive bacteria. Overall, optimized bactericidal potency was achieved by adding a tryptophan residue at the N terminus and by the simultaneous substitution of residues present in positions 3, 4, and 11 with arginine. These results indicate that the myxinidin analogues emerge as an attractive alternative for treating drug-resistant infectious diseases and provide key insights into a rational design for novel agents against these pathogens.

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Section: Resultsmentioning

confidence: 99%

“…The mucus layer provides mechanical protective functions, but the prevention of colonization by parasites, bacteria, and fungi is also complemented by the molecules present in the mucus having antimicrobial characteristics. Thus, fish are a good source of AMPs, including defensins, cathelicidins, hepcidins, histone-derived peptides, and piscidins (12,13).…”

mentioning

confidence: 99%

Structural Insights into and Activity Analysis of the Antimicrobial Peptide Myxinidin

Cantisani

Finamore

Mignogna

et al. 2014

Antimicrob Agents Chemother

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“…Derived from their diversity, fish possess an enormous variety of antimicrobial peptides that provoke a great deal of interest, with many being described (1,2). Among these antimicrobial peptides is hepcidin, a small cysteine-rich molecule discovered at the turn of the twenty-first century, which has been the focus of recent attention.…”

mentioning

confidence: 99%

“…A hepcidin homolog was soon after found in a teleost fish, the hybrid striped bass (Morone saxatilis 3 Morone chrysops) (7), and several others followed (8)(9)(10). However, contrary to mammals, in which a single hepcidin gene exists [with the mouse being the only known exception (11)], the studies performed with other fish species have shown that many teleosts could possess a large number of hepcidin genes (1,12), especially in Perciformes and Pleuronectiformes. This diversity is generally attributed to genome duplications and positive Darwinian selection (13)(14)(15), influenced by host-pathogen interactions, with variations in gene copy number suggested to be lineage-or species-specific.…”

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confidence: 99%

Multiple Hepcidins in a Teleost Fish, Dicentrarchus labrax: Different Hepcidins for Different Roles

Neves

Caldas

Vieira

et al. 2015

The Journal of Immunology

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Teleost fish rely heavily on their innate immunity for an adequate response against pathogens and environmental challenges, with the production of antimicrobial peptides being one of their first lines of defense. Among those is hepcidin, a small cysteine-rich antimicrobial peptide that is also the key regulator of iron metabolism. Although most mammals possess a single hepcidin gene, with a dual role in both iron metabolism regulation and antimicrobial response, many teleost fish present multiple copies of hepcidin, most likely because of genome duplications and positive Darwinian selection, suggesting that different hepcidins may perform different functions. To study the roles of hepcidin in teleost fish, we have isolated and characterized several genes in the European sea bass (Dicentrarchus labrax) and evaluated variations in their expression levels in response to different experimental conditions. Although several hepcidin genes were found, after phylogenetic analysis they could be clustered in two groups: hamp1-like, with a single isoform similar to mammalian hepcidins, and hamp2-like, with several isoforms. Under experimental conditions, hamp1 was upregulated in response to iron overload and infection and downregulated during anemia and hypoxic conditions. Hamp2 did not respond to either iron overload or anemia but was highly upregulated during infection and hypoxia. In addition, Hamp2 synthetic peptides exhibited a clear antimicrobial activity against several bacterial strains in vitro. In conclusion, teleost fish that present two hepcidin types show a degree of subfunctionalization of its functions, with hamp1 more involved in the regulation of iron metabolism and hamp2 mostly performing an antimicrobial role.

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“…Several AMPs, such as pleurocidin, daxin, misgurin, piscidin, chrysophsin, morocidin, parasin, defensin, hepcidin and dicentracin have been identified in fish, and the results of these investigations have revealed the AMPs' capability to protect fish from infections. Recently, a study on synthetic hepcidin injected in sea bass has confirmed the capability to potentiate the antimicrobial activity against bacteria by administration of AMPs as a new frontier of therapeutic application in farmed fish species [34]. The aim of this study was to evaluate, through the biomolecular approach, the dynamic of expression of a panel of various …”

Section: Discussionmentioning

confidence: 99%

Antimicrobial Peptides Are Expressed during Early Development of Zebrafish (Danio rerio) and Are Inducible by Immune Challenge

Caccia

Agnello

Ceci

et al. 2017

Fishes

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Antimicrobial peptides (AMPS) are ancestral components in the evolution of immunity from protozoans to metazoans. Their expression can be constitutive or inducible by infectious challenge. Although characterized in detail in their structure and activity, the temporal and spatial expression of AMPS during vertebrate embryogenesis is still poorly understood. In the present study, we identified selected AMPs in zebrafish, and characterized their expression during early development, and upon experimental immune challenge in adult animals, with the goal of establishing this genetically-tractable model system for further AMP studies. By mining available genomic databases, zebrafish AMP sequences homologous to AMPs from other vertebrates were selected for further study. These included parasin I and its enzyme cathepsin D, β-defensin (DB1), liver-expressed antimicrobial peptide 2 (LEAP2), bactericidal permeability-increasing protein (BPI), and chromogranin-A and -B (CgA and CgB). Specific primers were designed for RT-PCR amplification of each AMP gene of interest and amplicons between 242 bp and 504 bp were obtained from RNA extracted from adult zebrafish. Sequencing of the amplicons and alignment of their deduced amino acid sequences with those from AMPs from other vertebrate species confirmed their identity. The temporal expression of AMPs was investigated by RT-PCR analysis in fertilized oocytes, embryos, and adult individuals. Parasin I and chatepsin D transcripts were detectable immediately after fertilization, while the transcripts for CgA and CgB became evident starting at 48 h post fertilization. Mature transcripts of LEAP2 and DB1 were detectable only in the adult zebrafish, while BPI transcripts were detectable starting from the 12th day post fertilization. To explore the possible upregulation of AMP expression by infectious challenge, experiments were carried out in adult zebrafish by intraperitoneal injection of a cocktail of lipopolysaccharide and lipoteichoic acid. Except for CgA and CgB, amplicons corresponding to all tested AMPs showed stronger signals in the experimental animals as compared to the unchallenged controls. This study provided information on the early expression of AMPs in zebrafish from ontogeny to adulthood and their inducibility by microbials. This information could be useful to actuate new prophylactic strategies as an alternative to the use of antibiotics in culture.

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Antimicrobial Peptides from Fish

Cited by 264 publications

References 226 publications

Structural Insights into and Activity Analysis of the Antimicrobial Peptide Myxinidin

Structural Insights into and Activity Analysis of the Antimicrobial Peptide Myxinidin

Multiple Hepcidins in a Teleost Fish, Dicentrarchus labrax: Different Hepcidins for Different Roles

Antimicrobial Peptides Are Expressed during Early Development of Zebrafish (Danio rerio) and Are Inducible by Immune Challenge

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