@article{PAR00021702,
  title = {{F}unctional characterization of temporin-she, a new broad-spectrum antibacterial and leishmanicidal temporin-{SH} paralog from the {S}ahara frog ({P}elophylax saharicus)},
  author = {{A}ndre, {S}. and {R}aja, {Z}. and {H}umblot, {V}. and {P}iesse, {C}. and {F}oulon, {T}. and {S}ereno, {D}enis and {O}ury, {B}runo and {L}adram, {A}.},
  editor = {},
  language = {{ENG}},
  abstract = {{A}mphibian skin is a promising natural resource for antimicrobial peptides ({AMP}s), key effectors of innate immunity with attractive therapeutic potential to fight antibiotic-resistant pathogens. {O}ur previous studies showed that the skin of the {S}ahara {F}rog ({P}elophylax saharicus) contains broad-spectrum {AMP}s of the temporin family, named temporins-{SH}. {H}ere, we focused our study on temporin-{SH}e, a temporin-{SH}d paralog that we have previously identified in this frog but was never structurally and functionally characterized. {W}e synthesized and determined the structure of temporin-{SH}e. {T}his non-amphipathic alpha-helical peptide was demonstrated to strongly destabilize the lipid chain packing of anionic multilamellar vesicles mimicking bacterial membranes. {I}nvestigation of the antimicrobial activity revealed that temporin-{SH}e targets {G}ram-negative and {G}ram-positive bacteria, including clinical isolates of multi-resistant {S}taphylococcus aureus strains. {T}emporin-{SH}e exhibited also antiparasitic activity toward different{L}eishmaniaspecies responsible for visceral leishmaniasis, as well as cutaneous and mucocutaneous forms. {F}unctional assays revealed that temporin-{SH}e exerts bactericidal effects with membrane depolarization and permeabilization, via a membranolytic mechanism observed by scanning electron microscopy. {T}emporin-{SH}e represents a new member of the very limited group of antiparasitic temporins/{AMP}s. {D}espite its cytotoxicity, it is nevertheless an interesting tool to study the {AMP} antiparasitic mechanism and design new antibacterial/antiparasitic agents.},
  keywords = {frog antimicrobial peptide ; temporin-{SH}e ; broad-spectrum activity ; bacteria ; parasites ; secondary structure ; membrane disrupting mechanism ; scanning electron microscopy},
  booktitle = {},
  journal = {{I}nternational {J}ournal of {M}olecular {S}ciences},
  volume = {21},
  numero = {18},
  pages = {6713 [19 p.]},
  year = {2020},
  DOI = {10.3390/ijms21186713},
  URL = {https://www.documentation.ird.fr/hor/{PAR}00021702},
}