Abstract
Phylloseptin (PS) peptides, derived from South American hylid frogs (subfamily Phyllomedusinae), have been found to have broad-spectrum antimicrobial activities and relatively low haemolytic activities. Although PS peptides have been identified from several well-known and widely-distributed species of the Phyllomedusinae, there remains merit in their study in additional, more obscure and specialised members of this taxon. Here, we report the discovery of two novel PS peptides, named PS-Du and PS-Co, which were respectively identified for the first time and isolated from the skin secretions of Phyllomedusa duellmani and Phyllomedusa coelestis. Their encoding cDNAs were cloned, from which it was possible to deduce the entire primary structures of their biosynthetic precursors. Reversed-phase high-performance liquid chromatography (RP-HPLC) and tandem mass spectrometry (MS/MS) analyses were employed to isolate and structurally-characterise respective encoded PS peptides from skin secretions. The peptides had molecular masses of 2049.7 Da (PS-Du) and 1972.8 Da (PS-Co). They shared typical N-terminal sequences and C-terminal amidation with other known phylloseptins. The two peptides exhibited growth inhibitory activity against E. coli (NCTC 10418), as a standard Gram-negative bacterium, S. aureus (NCTC 10788), as a standard Gram-positive bacterium and C. albicans (NCPF 1467), as a standard pathogenic yeast, all as planktonic cultures. Moreover, both peptides demonstrated the capability of eliminating S. aureus biofilm.
Highlights
Amphibians possess a special innate skin defence system to protect them from being preyed upon by predators and infected by microorganisms in their living environments
Hundreds of antimicrobial peptides have been discovered in amphibian skins and these have been widely-studied in recent decades [1,2,3,4]
More than 80 antimicrobial peptides have been discovered from the skin secretions of species within this subfamily and these peptides have been divided into seven peptide families including
Summary
Amphibians possess a special innate skin defence system to protect them from being preyed upon by predators and infected by microorganisms in their living environments. Hundreds of antimicrobial peptides have been discovered in amphibian skins and these have been widely-studied in recent decades [1,2,3,4]. These amphibian antimicrobial peptides have been divided into different families according to structural similarities and these include the brevinins, esculentins, temporins, dermaseptins, phylloseptins and bombinins [5,6,7,8]. Phyllomedusa duellmani and Phyllomedusa coelestis are members of genus Phyllomedusa Unlike their relatives, Phyllomedusa hypochondrialis, Phyllomedusa sauvagei and other species, which have been widely studied, only a few bioactive peptides have been reported from these two species. After chemical synthesis of replicates of both peptides, their biological activities were investigated in antimicrobial and haemolysis bioassays
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