Host-defense peptides in skin secretions of the tetraploid frog Silurana epitropicalis with potent activity against methicillin-resistant Staphylococcus aureus (MRSA)

Conlon, J. Michael; Mechkarska, Milena; Prajeep, Manju; Sonnevend, Ágnes; Coquet, Laurent; Leprince, Jérôme; Jouenne, Thierry; Vaudry, Hubert; King, Jay D.

doi:10.1016/j.peptides.2012.07.005

Cited by 29 publications

(21 citation statements)

References 36 publications

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“…The C-terminal region of prepro-CPF-St6 shows sequence similarity to the HLP caerulein, as previously reported for prepro-CPF-St7 [30]. Prepro-XPF-St4 and prepro-XPF-St5 share a C-terminal region with similarity to the X. laevis peptide levitide [25], and prepro-XPF-St7, prepro-XPF-St7p and prepro-XPF-St8 show similarity to peptide phenylalanine-glutamine-amide (pFQa), a 14-AA-long peptide of Silurana epitropicalis [16].…”

Section: Resultssupporting

confidence: 57%

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Origin and Functional Diversification of an Amphibian Defense Peptide Arsenal

Roelants

Fry

et al. 2013

PLoS Genet

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The skin secretion of many amphibians contains an arsenal of bioactive molecules, including hormone-like peptides (HLPs) acting as defense toxins against predators, and antimicrobial peptides (AMPs) providing protection against infectious microorganisms. Several amphibian taxa seem to have independently acquired the genes to produce skin-secreted peptide arsenals, but it remains unknown how these originated from a non-defensive ancestral gene and evolved diverse defense functions against predators and pathogens. We conducted transcriptome, genome, peptidome and phylogenetic analyses to chart the full gene repertoire underlying the defense peptide arsenal of the frog Silurana tropicalis and reconstruct its evolutionary history. Our study uncovers a cluster of 13 transcriptionally active genes, together encoding up to 19 peptides, including diverse HLP homologues and AMPs. This gene cluster arose from a duplicated gastrointestinal hormone gene that attained a HLP-like defense function after major remodeling of its promoter region. Instead, new defense functions, including antimicrobial activity, arose by mutation of the precursor proteins, resulting in the proteolytic processing of secondary peptides alongside the original ones.Although gene duplication did not trigger functional innovation, it may have subsequently facilitated the convergent loss of the original function in multiple gene lineages (subfunctionalization), completing their transformation from HLP gene to AMP gene. The processing of multiple peptides from a single precursor entails a mechanism through which peptide-encoding genes may establish new functions without the need for gene duplication to avoid adaptive conflicts with older ones.

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Section: Resultssupporting

confidence: 57%

“…Several authors have recently questioned the singular role of amphibian AMPs as first-line antimicrobials [12]–[16]. The weak activity of some AMPs compared to others has been interpreted as an indication that they evolved another, yet unknown function [17], [20].…”

Section: Discussionmentioning

confidence: 99%

Origin and Functional Diversification of an Amphibian Defense Peptide Arsenal

Roelants

Fry

et al. 2013

PLoS Genet

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“…However, secondary reactions such as hemolytic activity, [36] limit their use as systemic anti-infective drugs. Until recently, no such reaction was reported for the antimicrobial Cgs-derived peptides in the literature.…”

Section: Discussionmentioning

confidence: 99%

Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases

et al. 2013

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Innate immunity involving antimicrobial peptides represents an integrated and highly effective system of molecular and cellular mechanisms that protects host against infections. One of the most frequent hospital-acquired pathogens, Staphylococcus aureus, capable of producing proteolytic enzymes, which can degrade the host defence agents and tissue components. Numerous antimicrobial peptides derived from chromogranins, are secreted by nervous, endocrine and immune cells during stress conditions. These kill microorganisms by their lytic effect at micromolar range, using a pore-forming mechanism against Gram-positive bacteria, filamentous fungi and yeasts. In this study, we tested antimicrobial activity of chromogranin A-derived peptides (catestatin and cateslytin) against S. aureus and analysed S. aureus-mediated proteolysis of these peptides using HPLC, sequencing and MALDI-TOF mass spectrometry. Interestingly, this study is the first to demonstrate that cateslytin, the active domain of catestatin, is active against S. aureus and is interestingly resistant to degradation by S. aureus proteases.

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“…Magainin-2 shows tumoricidal activity against human small cell lung cancer cell lines [45], some bladder cancer cells [46], and against a wide range of hematopoietic cell lines [47]. Some peptides secreted by frog skin with a high activity against multiresistant Staphylococcus aureus did not succeed as anti-infective agents due to their high hemolytic activities against human red blood cells and their rapid clearance from the circulation [48]. Thus, the therapeutic potential of frog skin peptides as anti-infective agents has not been realized so that alternative clinical applications as anti-cancer [43,44,45,46,47,48,49,50,51] or antiviral [44,49] drugs are being explored.…”

Section: Structure and Function Of Antimicrobial Peptidesmentioning

confidence: 99%

Novel Formulations for Antimicrobial Peptides

Carmona-Ribeiro

Carrasco

2014

IJMS

117

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Peptides in general hold much promise as a major ingredient in novel supramolecular assemblies. They may become essential in vaccine design, antimicrobial chemotherapy, cancer immunotherapy, food preservation, organs transplants, design of novel materials for dentistry, formulations against diabetes and other important strategical applications. This review discusses how novel formulations may improve the therapeutic index of antimicrobial peptides by protecting their activity and improving their bioavailability. The diversity of novel formulations using lipids, liposomes, nanoparticles, polymers, micelles, etc., within the limits of nanotechnology may also provide novel applications going beyond antimicrobial chemotherapy.

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Host-defense peptides in skin secretions of the tetraploid frog Silurana epitropicalis with potent activity against methicillin-resistant Staphylococcus aureus (MRSA)

Cited by 29 publications

References 36 publications

Origin and Functional Diversification of an Amphibian Defense Peptide Arsenal

Origin and Functional Diversification of an Amphibian Defense Peptide Arsenal

Cateslytin, a Chromogranin A Derived Peptide Is Active against Staphylococcus aureus and Resistant to Degradation by Its Proteases

Novel Formulations for Antimicrobial Peptides

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