1. Academic Validation
  2. 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)

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. 2022 Mar 11;11(3):342. doi: 10.3390/pathogens11030342.
András Fodor 1 2 Maxime Gualtieri 3 Matthias Zeller 4 Eustachio Tarasco 5 6 Michael G Klein 7 Andrea M Fodor 1 Leroy Haynes 8 Katalin Lengyel 1 9 Steven A Forst 10 Ghazala M Furgani 1 11 Levente Karaffa 12 13 Tibor Vellai 1 14
Affiliations

Affiliations

  • 1 Department of Genetics, Eötvös University, Pázmány Péter Sétány 1/C, H-1117 Budapest, Hungary.
  • 2 Department of Genetics, University of Szeged, Középfasor 52, H-6726 Szeged, Hungary.
  • 3 Nosopharm, 110 Allée Charles Babbage, Espace Innovation 2, 30000 Nîmes, France.
  • 4 Department of Chemistry, Purdue University, 560 Oval Drive, West Lafayette, IN 47906, USA.
  • 5 Department of Soil, Plant and Food Sciences, University of Bari "Aldo Moro", Via Amendola 165/A, 70126 Bari, Italy.
  • 6 Institute for Sustainable Plant Protection of CNR, Via Amendola 122/D, 70126 Bari, Italy.
  • 7 USDA-ARS & Department of Entomology, The Ohio State University, 13416 Claremont Ave, Cleveland, OH 44130, USA.
  • 8 Department of Chemistry, The College of Wooster, Wooster, OH 44691, USA.
  • 9 National Institute of Pharmacy and Nutrition (NIPN), Zrinyi utca 3, H-1051 Budapest, Hungary.
  • 10 Department of Biological Sciences, University of Wisconsin-Milwaukee, P.O. Box 413, Milwaukee, WI 53201, USA.
  • 11 Department of Plant Protection, Faculty of Agriculture, University of Tripoli, Tripoli P.O. Box 13793, Libya.
  • 12 Department of Biochemical Engineering, Faculty of Science and Technology, University of Debrecen, Egyetem Tér 1, H-4032 Debrecen, Hungary.
  • 13 Institute of Metagenomics, University of Debrecen, Egyetem tér 1, H-4032 Debrecen, Hungary.
  • 14 MTA-ELTE Genetics Research Group, Pázmány Péter Sétány 1/C, H-1117 Budapest, Hungary.
Abstract

Antimicrobial multidrug resistance (MDR) is a global challenge, not only for public health, but also for sustainable agriculture. Antibiotics used in humans should be ruled out for use in veterinary or agricultural settings. Applying antimicrobial peptide (AMP) molecules, produced by soil-born organisms for protecting (soil-born) Plants, seems a preferable alternative. The natural role of peptide-antimicrobials, produced by the prokaryotic partner of entomopathogenic-nematode/bacterium (EPN/EPB) symbiotic associations, is to sustain monoxenic conditions for the EPB in the gut of the semi-anabiotic infective dauer juvenile (IJ) EPN. They keep pathobiome conditions balanced for the EPN/EPB complex in polyxenic (soil, vanquished insect cadaver) niches. Xenorhabdus szentirmaii DSM16338(T) (EMC), and X. budapestensis DSM16342(T) (EMA), are the respective natural symbionts of EPN species Steinernema rarum and S. bicornutum. We identified and characterized both of these 15 years ago. The functional annotation of the draft genome of EMC revealed 71 genes encoding non-ribosomal peptide synthases, and polyketide synthases. The large spatial Xenorhabdus AMP (fabclavine), was discovered in EMA, and its biosynthetic pathway in EMC. The AMPs produced by EMA and EMC are promising candidates for controlling MDR prokaryotic and eukaryotic pathogens (bacteria, oomycetes, fungi, protozoa). EMC releases large quantity of iodinin (1,6-dihydroxyphenazine 5,10-dioxide) in a water-soluble form into the media, where it condenses to form spectacular water-insoluble, macroscopic crystals. This review evaluates the scientific impact of international research on EMA and EMC.

Keywords

EPN/EPB cospeciation 10; NRP-AMP 2; PAX-peptides 7; R-type bacteriocins 9; Xenorhabdus 1; exocrystal 5; fabclavine 3; iodinin 4; phenazine 6; szentiamide 8.

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