phaidra.vetmeduni.ac.at o:2515 DOI 10.3390/antibiotics12091462 Antimicrobial Peptides (AMP) in the Cell-Free Culture Media of Xenorhabdus budapestensis and X. szentirmaii Exert Anti-Protist Activity against Eukaryotic Vertebrate Pathogens including Histomonas meleagridis and Leishmania donovani Species Anti-microbial peptides provide a powerful toolkit for combating multidrug resistance. Combating eukaryotic pathogens is complicated because the intracellular drug targets in the eukaryotic pathogen are frequently homologs of cellular structures of vital importance in the host organism. The entomopathogenic bacteria (EPB), symbionts of entomopathogenic-nematode species, release a series of non-ribosomal templated anti-microbial peptides. Some may be potential drug candidates. The ability of an entomopathogenic-nematode/entomopathogenic bacterium symbiotic complex to survive in a given polyxenic milieu is a coevolutionary product. This explains that those gene complexes that are responsible for the biosynthesis of different non-ribosomal templated anti-microbial protective peptides (including those that are potently capable of inactivating the protist mammalian pathogen Leishmania donovanii and the gallinaceous bird pathogen Histomonas meleagridis) are co-regulated. Our approach is based on comparative anti-microbial bioassays of the culture media of the wild-type and regulatory mutant strains. We concluded that Xenorhabdus budapestensis and X. szentirmaii are excellent sources of non-ribosomal templated anti-microbial peptides that are efficient antagonists of the mentioned pathogens. Data on selective cytotoxicity of different cell-free culture media encourage us to forecast that the recently discovered "easy-PACId" research strategy is suitable for constructing entomopathogenic-bacterium (EPB) strains producing and releasing single, harmless, non-ribosomal templated anti-microbial peptides with considerable drug, (probiotic)-candidate potential. eng Escherichia-Coli; In-Vitro; Tetratrichomonas-Gallinarum; Bacteria Xenorhabdus; Resistance; Poultry; Disease; Hfq; Establishment; Depsipeptide 2024-02-13T09:05:44.140Z LOMv1.0 Author BEGIN:VCARD VERSION:3.0 N:Fodor;András; FN:András Fodor X-ORCID:https://orcid.org/0000-0003-3495-0154 END:VCARD BEGIN:VCARD VERSION:3.0 N:Hess;Michael; FN:Michael Hess X-ORCID:https://orcid.org/0000-0002-6991-0120 END:VCARD BEGIN:VCARD VERSION:3.0 N:Vellai;Tibor; FN:Tibor Vellai END:VCARD BEGIN:VCARD VERSION:3.0 N:McGwire;Bradford S.; FN:Bradford S. McGwire END:VCARD BEGIN:VCARD VERSION:3.0 N:Kulkarni;Manjusha M.; FN:Manjusha M. Kulkarni END:VCARD BEGIN:VCARD VERSION:3.0 N:Tarasco;Eustachio; FN:Eustachio Tarasco X-ORCID:https://orcid.org/0000-0001-6310-186X END:VCARD BEGIN:VCARD VERSION:3.0 N:Klein;Michael G.; FN:Michael G. Klein END:VCARD BEGIN:VCARD VERSION:3.0 N:Sebestyén;Anna; FN:Anna Sebestyén END:VCARD BEGIN:VCARD VERSION:3.0 N:Fodor;László; FN:László Fodor X-ORCID:https://orcid.org/0000-0003-2711-0229 END:VCARD BEGIN:VCARD VERSION:3.0 N:Pál;László; FN:László Pál X-ORCID:https://orcid.org/0000-0001-9838-6703 END:VCARD BEGIN:VCARD VERSION:3.0 N:Dublecz;Károly; FN:Károly Dublecz X-ORCID:https://orcid.org/0000-0001-6913-219X END:VCARD BEGIN:VCARD VERSION:3.0 N:Makrai;László; FN:László Makrai END:VCARD BEGIN:VCARD VERSION:3.0 N:Kiss;János; FN:János Kiss X-ORCID:https://orcid.org/0000-0002-0506-5474 END:VCARD BEGIN:VCARD VERSION:3.0 N:Boros;Zsófia; FN:Zsófia Boros END:VCARD BEGIN:VCARD VERSION:3.0 N:Hess;Claudia; FN:Claudia Hess X-ORCID:https://orcid.org/0000-0002-3535-5157 END:VCARD BEGIN:VCARD VERSION:3.0 N:Ganas;Petra; FN:Petra Ganas END:VCARD https://w3id.org/kim/hcrt/scheme https://w3id.org/kim/hcrt/text Textdokument Text LOMv1.0 yes https://creativecommons.org/licenses/by/4.0 application/pdf 1030454 https://phaidra.vetmeduni.ac.at/o:2515 https://phaidra.vetmeduni.ac.at/api/object/o:2515/thumbnail LOMv1.0 discipline