Andre S. auteur aut IRD Raja Z. auteur aut IRD Humblot V. auteur aut IRD Piesse C. auteur aut IRD Foulon T. auteur aut IRD Sereno Denis auteur aut IRD Oury Bruno auteur aut IRD Ladram A. auteur aut IRD text journalArticle eng text/pdf reformatted digital access Amphibian skin is a promising natural resource for antimicrobial peptides (AMPs), key effectors of innate immunity with attractive therapeutic potential to fight antibiotic-resistant pathogens. Our previous studies showed that the skin of the Sahara Frog (Pelophylax saharicus) contains broad-spectrum AMPs of the temporin family, named temporins-SH. Here, we focused our study on temporin-SHe, a temporin-SHd paralog that we have previously identified in this frog but was never structurally and functionally characterized. We synthesized and determined the structure of temporin-SHe. This non-amphipathic alpha-helical peptide was demonstrated to strongly destabilize the lipid chain packing of anionic multilamellar vesicles mimicking bacterial membranes. Investigation of the antimicrobial activity revealed that temporin-SHe targets Gram-negative and Gram-positive bacteria, including clinical isolates of multi-resistant Staphylococcus aureus strains. Temporin-SHe exhibited also antiparasitic activity toward differentLeishmaniaspecies responsible for visceral leishmaniasis, as well as cutaneous and mucocutaneous forms. Functional assays revealed that temporin-SHe exerts bactericidal effects with membrane depolarization and permeabilization, via a membranolytic mechanism observed by scanning electron microscopy. Temporin-SHe represents a new member of the very limited group of antiparasitic temporins/AMPs. Despite its cytotoxicity, it is nevertheless an interesting tool to study the AMP antiparasitic mechanism and design new antibacterial/antiparasitic agents. specialized frog antimicrobial peptide temporin-SHe broad-spectrum activity bacteria parasites secondary structure membrane disrupting mechanism scanning electron microscopy 020 084 052 080 21 18 6713 [19 p.] 2020 https://www.documentation.ird.fr/hor/PAR00021702 10.3390/ijms21186713 [F B010079861] https://www.documentation.ird.fr/hor/PAR00021702 https://horizon.documentation.ird.fr/exl-doc/pleins_textes/divers20-11/010079861.pdf IRD - Base Horizon / Pleins textes 2020-12-08 2025-02-24 PAR00021702 fre