{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,20]],"date-time":"2025-10-20T18:50:07Z","timestamp":1760986207826,"version":"build-2065373602"},"reference-count":75,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2023,3,14]],"date-time":"2023-03-14T00:00:00Z","timestamp":1678752000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"the State of Hungary and the EU","award":["T\u00c1MOP-4.2.2\/B-10\/1-2010-0025"],"award-info":[{"award-number":["T\u00c1MOP-4.2.2\/B-10\/1-2010-0025"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Pathogens"],"abstract":"<jats:p>Entomopathogenic bacteria are obligate symbionts of entomopathogenic nematode (EPN) species. These bacteria biosynthesize and release non-ribosomal-templated hybrid peptides (NR-AMPs), with strong, and large-spectral antimicrobial potential, capable of inactivating pathogens belonging to different prokaryote, and eukaryote taxa. The cell-free conditioned culture media (CFCM) of Xenorhabdus\u00a0budapestensis and X. szentirmaii efficiently inactivate poultry pathogens like Clostridium, Histomonas, and Eimeria. To learn whether a bio-preparation containing antimicrobial peptides of Xenorhabdus origin with accompanying (in vitro detectable) cytotoxic effects could be considered a safely applicable preventive feed supplement, we conducted a 42-day feeding experiment on freshly hatched broiler cockerels. XENOFOOD (containing autoclaved X. budapestensis, and X. szentirmaii cultures developed on chicken food) were consumed by the birds. The XENOFOOD exerted detectable gastrointestinal (GI) activity (reducing the numbers of the colony-forming Clostridium perfringens units in the lower jejunum. No animal was lost in the experiment. Neither the body weight, growth rate, feed-conversion ratio, nor organ-weight data differed between the control (C) and treated (T) groups, indicating that the XENOFOOD diet did not result in any detectable adverse effects. We suppose that the parameters indicating a moderate enlargement of bursas of Fabricius (average weight, size, and individual bursa\/spleen weight-ratios) in the XENOFOOD-fed group must be an indirect indication that the bursa-controlled humoral immune system neutralized the cytotoxic ingredients of the XENOFOOD in the blood, not allowing to reach their critical cytotoxic concentration in the sensitive tissues.<\/jats:p>","DOI":"10.3390\/pathogens12030458","type":"journal-article","created":{"date-parts":[[2023,3,15]],"date-time":"2023-03-15T05:22:59Z","timestamp":1678857779000},"page":"458","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":5,"title":["XENOFOOD\u2014An Autoclaved Feed Supplement Containing Autoclavable Antimicrobial Peptides\u2014Exerts Anticoccidial GI Activity, and Causes Bursa Enlargement, but Has No Detectable Harmful Effects in Broiler Cockerels despite In Vitro Detectable Cytotoxicity on LHM Cells"],"prefix":"10.3390","volume":"12","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3495-0154","authenticated-orcid":false,"given":"Andr\u00e1s","family":"Fodor","sequence":"first","affiliation":[{"name":"Department of Genetics, E\u00f6tv\u00f6s Lor\u00e1nd University, P\u00e1zm\u00e1ny P. S\u00e9t\u00e1ny 1C, H-1117 Budapest, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tibor","family":"Vellai","sequence":"additional","affiliation":[{"name":"Department of Genetics, E\u00f6tv\u00f6s Lor\u00e1nd University, P\u00e1zm\u00e1ny P. S\u00e9t\u00e1ny 1C, H-1117 Budapest, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3535-5157","authenticated-orcid":false,"given":"Claudia","family":"Hess","sequence":"additional","affiliation":[{"name":"Clinic for Poultry and Fish Medicine, Department for Farm Animals and Veterinary Public Health, University of Veterinary Medicine (Vetmeduni Vienna), 1210 Vienna, Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L\u00e1szl\u00f3","family":"Makrai","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Infectious Diseases, University of Veterinary Medicine, H-1581 Budapest, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6913-219X","authenticated-orcid":false,"given":"K\u00e1roly","family":"Dublecz","sequence":"additional","affiliation":[{"name":"Institute of Physiology and Nutrition, Georgikon Campus, Hungarian University of Agriculture and Life Sciences (MATE), De\u00e1k Ferenc utca 16, H-8360 Keszthely, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9838-6703","authenticated-orcid":false,"given":"L\u00e1szl\u00f3","family":"P\u00e1l","sequence":"additional","affiliation":[{"name":"Institute of Physiology and Nutrition, Georgikon Campus, Hungarian University of Agriculture and Life Sciences (MATE), De\u00e1k Ferenc utca 16, H-8360 Keszthely, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Andor","family":"Moln\u00e1r","sequence":"additional","affiliation":[{"name":"Institute of Physiology and Nutrition, Georgikon Campus, Hungarian University of Agriculture and Life Sciences (MATE), De\u00e1k Ferenc utca 16, H-8360 Keszthely, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Michael G.","family":"Klein","sequence":"additional","affiliation":[{"name":"USDA-ARS & Department of Entomology, The Ohio State University, 13416 Claremont Ave., Cleveland, OH 44130, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6310-186X","authenticated-orcid":false,"given":"Eustachio","family":"Tarasco","sequence":"additional","affiliation":[{"name":"Department of Soil, Plant and Food Sciences, University of Bari \u201cAldo Moro\u201d, Via Amendola 165\/A, 70126 Bari, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S\u00e1ndor","family":"J\u00f3zsa","sequence":"additional","affiliation":[{"name":"Institute of Physiology and Nutrition, Georgikon Campus, Hungarian University of Agriculture and Life Sciences (MATE), De\u00e1k Ferenc utca 16, H-8360 Keszthely, Hungary"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Petra","family":"Ganas","sequence":"additional","affiliation":[{"name":"Clinic for Poultry and Fish Medicine, Department for Farm Animals and Veterinary Public Health, University of Veterinary Medicine (Vetmeduni Vienna), 1210 Vienna, Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6991-0120","authenticated-orcid":false,"given":"Michael","family":"Hess","sequence":"additional","affiliation":[{"name":"Clinic for Poultry and Fish Medicine, Department for Farm Animals and Veterinary Public Health, University of Veterinary Medicine (Vetmeduni Vienna), 1210 Vienna, Austria"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2023,3,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1379","DOI":"10.1016\/j.molp.2020.08.010","article-title":"Bacterial Vector-Borne Plant Diseases: Unanswered Questions and Future Directions","volume":"13","author":"Huang","year":"2020","journal-title":"Mol. Plant"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1094\/MPMI-08-17-0196-FI","article-title":"Lessons in Effector and NLR Biology of Plant-Microbe Systems","volume":"31","author":"Zess","year":"2018","journal-title":"Mol. Plant-Microbe Interact."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1007\/s10393-020-01504-w","article-title":"Tracking Batrachochytrium dendrobatidis Infection Across the Globe","volume":"17","author":"Monzon","year":"2020","journal-title":"EcoHealth"},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Kol\u00e1\u0159ov\u00e1, I., and Valigurov\u00e1, A. (2021). Hide-and-Seek: A Game Played between Parasitic Protists and Their Hosts. Microorganisms, 9.","DOI":"10.3390\/microorganisms9122434"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"735815","DOI":"10.3389\/fmicb.2021.735815","article-title":"Emerging Parasitic Protists: The Case of Perkinsea","volume":"12","author":"Metz","year":"2022","journal-title":"Front. Microbiol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1016\/j.meegid.2015.06.029","article-title":"A perspective on genomic-guided anthelmintic discovery and repurposing using Haemonchus contortus","volume":"40","author":"Preston","year":"2016","journal-title":"Infect. Genet. Evol."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Zuo, Y., Shi, Y., Zhang, F., Guan, F., Zhang, J., Feyereisen, R., Fabrick, J.A., Yang, Y., and Wu, Y. (2021). Genome mapping coupled with CRISPR gene editing reveals a P450 gene confers avermectin resistance in the beet armyworm. PLoS Genet., 17.","DOI":"10.1371\/journal.pgen.1009680"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"4193","DOI":"10.3382\/ps\/pey296","article-title":"The resistance of Eimeria spp. to toltrazuril in black grouse (Lyrurus tetrix) kept in an aviary","volume":"97","year":"2018","journal-title":"Poult. Sci."},{"key":"ref_9","first-page":"91","article-title":"Comparative effect of papaya (Carica papaya) leaves\u2019 extract and Toltrazuril on growth performance, hematological parameter, and protozoal load in Sonali chickens infected by mixed Eimeria spp.","volume":"8","author":"Akhter","year":"2021","journal-title":"J. Adv. Veter-Anim. Res."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"5318","DOI":"10.1111\/mec.15877","article-title":"Contrasting levels of genetic predictability in the evolution of resistance to major classes of fungicides","volume":"30","author":"Hawkins","year":"2021","journal-title":"Mol. Ecol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1038\/s41467-017-00119-0","article-title":"Early-life disruption of amphibian microbiota decreases later-life resistance to parasites","volume":"8","author":"Knutie","year":"2017","journal-title":"Nat. Commun."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1750","DOI":"10.1016\/j.jiph.2021.10.020","article-title":"Antibiotic resistance in microbes: History, mechanisms, therapeutic strategies and future prospects","volume":"14","author":"Uddin","year":"2021","journal-title":"J. Infect. Public Health"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Fodor, A., Abate, B.A., De\u00e1k, P., Fodor, L., Gyenge, E., Klein, M.G., Koncz, Z., Muvevi, J., \u00d6tv\u00f6s, L., and Sz\u00e9kely, G. (2020). Multidrug Resistance (MDR) and Collateral Sensitivity in Bacteria, with Special Attention to Genetic and Evolutionary Aspects and to the Perspectives of Antimicrobial Peptides\u2014A Review. Pathogens, 9.","DOI":"10.3390\/pathogens9070522"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"62","DOI":"10.3389\/fchem.2014.00062","article-title":"Current challenges in peptide-based drug discovery","volume":"2","author":"Otvos","year":"2014","journal-title":"Front. Chem."},{"key":"ref_15","unstructured":"Ganelin, R., Jefferts, R., and Roberts, S. (2013). Biological and Small Molecule Drug Research and Development, Academic Press."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1038\/s41564-018-0164-0","article-title":"Antibiotic-resistant bacteria show widespread collateral sensitivity to antimicrobial peptides","volume":"3","author":"Martins","year":"2018","journal-title":"Nat. Microbiol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41467-019-13618-z","article-title":"Chemical-genetic profiling reveals limited cross-resistance between antimicrobial peptides with different modes of action","volume":"10","author":"Kintses","year":"2019","journal-title":"Nat. Commun."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"366","DOI":"10.3390\/ph8030366","article-title":"Peptides and Peptidomimetics for Antimicrobial Drug Design","volume":"8","author":"Mojsoska","year":"2015","journal-title":"Pharmaceuticals"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1128\/CMR.00056-05","article-title":"Peptide Antimicrobial Agents","volume":"19","author":"Jenssen","year":"2006","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"359","DOI":"10.3389\/fchem.2018.00359","article-title":"Advantage of a Narrow Spectrum Host Defense (Antimicrobial) Peptide Over a Broad Spectrum Analog in Preclinical Drug Development","volume":"6","author":"Ostorhazi","year":"2018","journal-title":"Front. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"480","DOI":"10.1016\/j.ijantimicag.2011.01.003","article-title":"Broad-spectrum antimicrobial efficacy of peptide A3-APO in mouse models of multidrug-resistant wound and lung infections cannot be explained by in vitro activity against the pathogens involved","volume":"37","author":"Ostorhazi","year":"2011","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1556\/030.63.2016.005","article-title":"Immunomodulatory effects of anti-microbial peptides","volume":"63","year":"2016","journal-title":"Acta Microbiol. Immunol. Hung."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Petkovic, M., Mouritzen, M.V., Mojsoska, B., and Jenssen, H. (2021). Immunomodulatory Properties of Host Defence Peptides in Skin Wound Healing. Biomolecules, 11.","DOI":"10.3390\/biom11070952"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1002\/psc.908","article-title":"QSAR modeling and computer-aided design of antimicrobial peptides","volume":"14","author":"Jenssen","year":"2007","journal-title":"J. Pept. Sci."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"4112","DOI":"10.1128\/AAC.00237-15","article-title":"Structure-Activity Relationship Study of Novel Peptoids That Mimic the Structure of Antimicrobial Peptides","volume":"59","author":"Mojsoska","year":"2015","journal-title":"Antimicrob. Agents Chemother."},{"key":"ref_26","doi-asserted-by":"crossref","unstructured":"Tsakou, F., Jersie-Christensen, R., Jenssen, H., and Mojsoska, B. (2020). The Role of Proteomics in Bacterial Response to Antibiotics. Pharmaceuticals, 13.","DOI":"10.3390\/ph13090214"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1138","DOI":"10.1007\/s00018-002-8493-8","article-title":"The short proline-rich antibacterial peptide family","volume":"59","year":"2002","journal-title":"Cell Mol. Life Sci."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/S0001-706X(02)00238-3","article-title":"Leishmania model for microbial virulence: The relevance of parasite multiplication and pathoantigenicity","volume":"85","author":"Chang","year":"2002","journal-title":"Acta Trop."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.exppara.2010.02.006","article-title":"Interactions of antimicrobial peptides with Leishmania and trypanosomes and their functional role in host parasitism","volume":"126","author":"McGwire","year":"2010","journal-title":"Exp. Parasitol."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"15496","DOI":"10.1074\/jbc.M809079200","article-title":"Antimicrobial Peptide-induced Apoptotic Death of Leishmania Results from Calcium-de pend ent, Caspase-independent Mitochondrial Toxicity","volume":"284","author":"Kulkarni","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_31","first-page":"3061","article-title":"Antibiotic activity of Xenorhabdus spp., bac 190 teria symbiotically associated with insect pathogenic nematodes of the families Heterorhabditidae and Steinernematidae","volume":"128","author":"Akhurst","year":"1982","journal-title":"J. Gen. Microbiol."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s40168-020-00800-5","article-title":"Entomopathogenic nematode-associated microbiota: From monoxenic paradigm to pathobiome","volume":"8","author":"Ogier","year":"2020","journal-title":"Microbiome"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1086\/375747","article-title":"Killing of African Trypanosomes by Antimicrobial Peptides","volume":"188","author":"McGwire","year":"2003","journal-title":"J. Infect. Dis."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1016\/j.syapm.2004.10.004","article-title":"Description of four novel species of Xenorhabdus, family Enterobacteriaceae: Xenorhabdus budapestensis sp. nov., Xenorhabdus ehlersii sp. nov., Xenorhabdus innexi sp. nov., and Xenorhabdus szentirmaii sp. nov","volume":"28","author":"Lengyel","year":"2005","journal-title":"Syst. Appl. Microbiol."},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Fodor, A., Gualtieri, M., Zeller, M., Tarasco, E., Klein, M.G., Fodor, A.M., Haynes, L., Lengyel, K., Forst, S.A., and Furgani, G.M. (2022). Type Strains of Entomopathogenic Nematode-Symbiotic Bacterium Species, Xenorhabdus szentirmaii (EMC) and X. budapestensis (EMA), Are Exceptional Sources of Non-Ribosomal Templated, Large-Target-Spectral, Thermotolerant-Antimicrobial Peptides (by Both), and Iodinin (by EMC). Pathogens, 11.","DOI":"10.3390\/pathogens11030342"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1111\/j.1365-2672.2007.03613.x","article-title":"Xenorhabdus antibiotics: A comparative analysis and potential utility for controlling mastitis caused by bacteria","volume":"104","author":"Furgani","year":"2008","journal-title":"J. Appl. Microbiol."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"746","DOI":"10.1111\/j.1365-2672.2009.04249.x","article-title":"Isolation and activity of Xenorhabdus antimicrobial compounds against the plant pathogens Erwinia amylovora and Phytophthora nicotianae","volume":"107","author":"Fodor","year":"2009","journal-title":"J. Appl. Microbiol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"547","DOI":"10.15835\/nbha4329997","article-title":"Effectiveness of a Peptide-rich Fraction from Xenorhabdus budapestensis Culture against Fire Blight Disease on Apple Blossoms","volume":"43","author":"Vozik","year":"2015","journal-title":"Not. Bot. Horti Agrobot. Cluj-Napoca"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1","DOI":"10.9734\/MRJI\/2017\/38516","article-title":"Anti-Coccidiosis Potential of Autoclaveable Antimicrobial Peptides from Xenorhabdus budapestensis Resistant to Proteolytic (Pepsin, Trypsin) Digestion Based on In vitro Studies","volume":"22","author":"Fodor","year":"2018","journal-title":"Microbiol. Res. J. Int."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Bobbarala, V. (2012). A Search for Antibacterial Agents, IntechOpen.","DOI":"10.5772\/1085"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"18957","DOI":"10.1002\/anie.201910563","article-title":"Promoter Activation in \u0394 hfq Mutants as an Efficient Tool for Specialized Metabolite Production Enabling Direct Bioactivity Testing","volume":"58","author":"Bode","year":"2019","journal-title":"Angew. Chem. Int. Ed."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1782","DOI":"10.1556\/650.2015.30274","article-title":"A Xenorhabdus budapestensis entomopatog\u00e9n bakt\u00e9rium sejtmentes fermentlev\u00e9nek \u00e9s tiszt\u00edtottfeh\u00e9rje-frakci\u00f3j\u00e1nak antimikrobi\u00e1lis hat\u00e1sa n\u00e9h\u00e1ny zoonoticus bakt\u00e9riumra","volume":"156","author":"Barcs","year":"2015","journal-title":"Orvosi Hetil."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"6948","DOI":"10.1021\/ac300372p","article-title":"Neutral Loss Fragmentation Pattern Based Screening for Arginine-Rich Natural Products in Xenorhabdus and Photorhabdus","volume":"84","author":"Fuchs","year":"2012","journal-title":"Anal. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1002\/cbic.201300802","article-title":"Fabclavines: Bioactive Peptide-Polyketide-Polyamino Hybrids from Xenorhabdus","volume":"15","author":"Fuchs","year":"2014","journal-title":"Chembiochem"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1007\/s10295-018-02124-8","article-title":"Fabclavine biosynthesis in X. szentirmaii: Shortened derivatives and characterization of the thioester reductase FclG and the condensation domain-like protein FclL","volume":"46","author":"Wenski","year":"2019","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"956","DOI":"10.3762\/bjoc.16.84","article-title":"Fabclavine diversity in Xenorhabdus bacteria","volume":"16","author":"Wenski","year":"2020","journal-title":"Beilstein J. Org. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.vetpar.2011.11.037","article-title":"Trichomonas gallinae, in comparison to Tetratrichomonas gallinarum, induces distinctive cytopathogenic effects in tissue cultures","volume":"186","author":"Amin","year":"2012","journal-title":"Vet. Parasitol."},{"key":"ref_48","first-page":"4460","article-title":"Establishment and characterization of a chicken hepatocellular carcinoma cell line, LMH","volume":"47","author":"Kawaguchi","year":"1987","journal-title":"Cancer Res."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2750","DOI":"10.1002\/cbic.202000176","article-title":"Nonribosomal Peptides Produced by Minimal and Engineered Synthetases with Terminal Reductase Domains","volume":"21","author":"Tietze","year":"2020","journal-title":"Chembiochem"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2342","DOI":"10.1002\/chem.201103479","article-title":"Determination of the Absolute Configuration of Peptide Natural Products by Using Stable Isotope Labeling and Mass Spectrometry","volume":"18","author":"Bode","year":"2012","journal-title":"Chem. Eur. J."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"kuab006","DOI":"10.1093\/jimb\/kuab006","article-title":"Structure and biosynthesis of deoxy-polyamine in Xenorhabdus bovienii","volume":"48","author":"Wenski","year":"2021","journal-title":"J. Ind. Microbiol. Biotechnol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/j.peptides.2012.03.027","article-title":"Two novel antimicrobial peptides purified from the symbiotic bacteria Xenorhabdus budapestensis NMC-10","volume":"35","author":"Xiao","year":"2012","journal-title":"Peptides"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1038\/s41429-019-0203-y","article-title":"Two novel cyclic depsipeptides Xenematides F and G from the entomopathogenic bacterium Xenorhabdus budapestensis","volume":"72","author":"Xi","year":"2019","journal-title":"J. Antibiot."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"1830","DOI":"10.1021\/np060409n","article-title":"Xenofuranones A and B: Phenylpyruvate Dimers from Xenorhabdus szentirmaii","volume":"69","author":"Brachmann","year":"2006","journal-title":"J. Nat. Prod."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/s41589-019-0246-1","article-title":"Dual phenazine gene clusters enable diversification during biosynthesis","volume":"15","author":"Shi","year":"2019","journal-title":"Nat. Chem. Biol."},{"key":"ref_56","first-page":"1247","article-title":"Szentiamide, an N-formylated Cyclic Depsipeptide from Xenorhabdus szentirmaii DSM 16338T","volume":"6","author":"Ohlendorf","year":"2011","journal-title":"Nat. Prod. Commun."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"528","DOI":"10.3762\/bjoc.8.60","article-title":"Synthesis of szentiamide, a depsipeptide from entomopathogenic Xenorhabdus szentirmaii with activity against Plasmodium falciparum","volume":"8","author":"Nollmann","year":"2012","journal-title":"Beilstein J. Org. Chem."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"e00190-14","DOI":"10.1128\/genomeA.00190-14","article-title":"Draft Genome Sequence and Annotation of the Entomopathogenic Bacterium Xenorhabdus szentirmaii Strain DSM16338","volume":"2","author":"Gualtieri","year":"2014","journal-title":"Genome Announc."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"390","DOI":"10.2174\/092986709787002628","article-title":"The antibiotics in the chemical space","volume":"16","author":"Gualtieri","year":"2009","journal-title":"Curr. Med. Chem."},{"key":"ref_60","unstructured":"Gualtieri, M., Villain-Guillot, P., Givaudan, A., and Pages, S. (2012). Nemaucin, an Antibiotic Produced by Entomopathogenic Xenorhabdus cabanillasii. (WO2012085177A1), France Patent."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1038\/ja.2013.58","article-title":"Cabanillasin, a new antifungal metabolite, produced by entomopathogenic Xenorhabdus cabanillasii JM26","volume":"66","author":"Houard","year":"2013","journal-title":"J. Antibiot."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/ja.2009.31","article-title":"Identification of a new antimicrobial lysine-rich cyclolipopeptide family from Xenorhabdus nematophila","volume":"62","author":"Gualtieri","year":"2009","journal-title":"J. Antibiot."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"3130","DOI":"10.1039\/c1ob05097d","article-title":"Structure elucidation and biosynthesis of lysine-rich cyclic peptides in Xenorhabdus nematophila","volume":"9","author":"Fuchs","year":"2011","journal-title":"Org. Biomol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","unstructured":"Dreyer, J., Rautenbach, M., Booysen, E., Van Staden, A.D., Deane, S.M., and Dicks, L.M.T. (2019). Xenorhabdus khoisanae SB10 produces Lys-rich PAX lipopeptides and a Xenocoumacin in its antimicrobial complex. BMC Microbiol., 19.","DOI":"10.1186\/s12866-019-1503-x"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/S0022-2011(02)00019-8","article-title":"Antimicrobial activity of Xenorhabdus sp. RIO (Enterobacteriaceae), symbiont of the entomopathogenic nematode, Steinernema riobrave (Rhabditida: Steinernematidae)","volume":"79","author":"Isaacson","year":"2002","journal-title":"J. Invertebr. Pathol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.molcel.2018.03.001","article-title":"Odilorhabdins, Antibacterial Agents that Cause Miscoding by Binding at a New Ribosomal Site","volume":"70","author":"Pantel","year":"2018","journal-title":"Mol. Cell"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"7814","DOI":"10.1021\/acs.jmedchem.8b00790","article-title":"Total Synthesis and Structure\u2013Activity Relationships Study of Odilorhabdins, a New Class of Peptides Showing Potent Antibacterial Activity","volume":"61","author":"Sarciaux","year":"2018","journal-title":"J. Med. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"2893","DOI":"10.3389\/fmicb.2019.02893","article-title":"From Worms to Drug Candidate: The Story of Odilorhabdins, a New Class of Antimicrobial Agents","volume":"10","author":"Racine","year":"2019","journal-title":"Front. Microbiol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"e0282621","DOI":"10.1128\/mbio.02826-21","article-title":"The Odilorhabdin Antibiotic Biosynthetic Cluster and Acetyltransferase Self-Resistance Locus Are Niche and Species Specific","volume":"13","author":"Pantel","year":"2022","journal-title":"Mbio"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"1976","DOI":"10.1021\/np500390b","article-title":"Xenortide Biosynthesis by Entomopathogenic Xenorhabdus nematophila","volume":"77","author":"Reimer","year":"2014","journal-title":"J. Nat. Prod."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"5332","DOI":"10.1039\/C8OB00452H","article-title":"Efficient syntheses and anti-cancer activity of xenortides A\u2013D including ent\/epi-stereoisomers","volume":"16","author":"Esmati","year":"2018","journal-title":"Org. Biomol. Chem."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1991","DOI":"10.1002\/cbic.201300205","article-title":"Rhabdopeptides as Insect-Specific Virulence Factors from Entomopathogenic Bacteria","volume":"14","author":"Reimer","year":"2013","journal-title":"ChemBioChem"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"3833","DOI":"10.1021\/acs.jafc.8b00253","article-title":"Rhabdopeptides from Xenorhabdus budapestensis SN84 and Their Nematicidal Activities against Meloidogyne incognita","volume":"66","author":"Bi","year":"2018","journal-title":"J. Agric. Food Chem."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"5116","DOI":"10.1021\/acs.orglett.8b01975","article-title":"Rhabdopeptide\/Xenortide-like Peptides from Xenorhabdus innexi with Terminal Amines Showing Potent Antiprotozoal Activity","volume":"20","author":"Zhao","year":"2018","journal-title":"Org. Lett."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1038\/nbt886","article-title":"The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens","volume":"21","author":"Duchaud","year":"2003","journal-title":"Nat. Biotechnol."}],"container-title":["Pathogens"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2076-0817\/12\/3\/458\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T18:55:09Z","timestamp":1760122509000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2076-0817\/12\/3\/458"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,3,14]]},"references-count":75,"journal-issue":{"issue":"3","published-online":{"date-parts":[[2023,3]]}},"alternative-id":["pathogens12030458"],"URL":"https:\/\/doi.org\/10.3390\/pathogens12030458","relation":{},"ISSN":["2076-0817"],"issn-type":[{"type":"electronic","value":"2076-0817"}],"subject":[],"published":{"date-parts":[[2023,3,14]]}}}