title: Symbiotic plant peptides eliminate Candida albicans both in vitro and in an epithelial infection model and inhibit the proliferation of immortalized human cells.
abstract: The increasing number of multidrug-resistant microbes now emerging necessitates the identification of novel antimicrobial agents. Plants produce a great variety of antimicrobial peptides including hundreds of small, nodule-specific cysteine-rich NCR peptides that, in the legume Medicago truncatula, govern the differentiation of endosymbiotic nitrogen fixing bacteria and, in vitro, can display potent antibacterial activities. In this study, the potential candidacidal activity of 19 NCR peptides was investigated. Cationic NCR peptides having an isoelectric point above 9 were efficient in killing Candida albicans, one of the most common fungal pathogens of humans. None of the tested NCR peptides were toxic for immortalized human epithelial cells at concentrations that effectively killed the fungus; however, at higher concentrations, some of them inhibited the division of the cells. Furthermore, the cationic peptides successfully inhibited C. albicans induced human epithelial cell death in an in vitro coculture model. These results highlight the therapeutic potential of cationic NCR peptides in the treatment of candidiasis.
authors.affiliation: Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Korut 62, Szeged 6726, Hungary.
authors.forename: Lilla
authors.initials: L
authors.lastname: Ordögh
authors.affiliation: Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Korut 62, Szeged 6726, Hungary.
authors.forename: Andrea
authors.initials: A
authors.lastname: Vörös
authors.affiliation: Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Korut 62, Szeged 6726, Hungary.
authors.forename: István
authors.initials: I
authors.lastname: Nagy
authors.affiliation: Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Korut 62, Szeged 6726, Hungary ; Institut des Sciences du Végétal, CNRS, Batiment 23, avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France.
authors.forename: Eva
authors.initials: E
authors.lastname: Kondorosi
authors.affiliation: Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences, Temesvari Korut 62, Szeged 6726, Hungary.
authors.forename: Attila
authors.identifier: 0000-0002-4421-6554
authors.initials: A
authors.lastname: Kereszt
mesh_terms: D000935:Antifungal Agents / Q000494:pharmacology; D002176:Candida albicans / Q000166:cytology / Q000187:drug effects*; D002177:Candidiasis / Q000382:microbiology* / Q000473:pathology; D002412:Cations / Q000494:pharmacology; D016923:Cell Death / Q000187:drug effects; D002460:Cell Line; D002461:Cell Line, Transformed; D002463:Cell Membrane Permeability / Q000187:drug effects; D049109:Cell Proliferation / Q000187:drug effects; D002470:Cell Survival / Q000187:drug effects; D004847:Epithelial Cells / Q000187:drug effects / Q000382:microbiology* / Q000473:pathology; D005260:Female; D006801:Humans; D046913:Medicago truncatula / Q000737:chemistry*; D008826:Microbial Sensitivity Tests; D010455:Peptides / Q000494:pharmacology*; D013559:Symbiosis; D013997:Time Factors
chemical_list: D000935:Antifungal Agents; D002412:Cations; D010455:Peptides