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A, Jäger W, Kalinowski J, Thierbach G, Puhler A: Small mobilizable multi-purpose cloning vectors derived

from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum . Gene 1994, XMU-MP-1 cell line 145:69–73.PubMedCrossRef Competing interests The authors do not declare competing interests. Authors’ contributions All authors contributed to designing the study. SAEH constructed and characterized the recombinant strains. VFW and PPW supervised the experiments. SAEH and PPW were responsible for the draft of the manuscript. All authors contributed to writing and approved the final manuscript.”
“Background The intensive use of chemical pesticides to treat plant diseases has resulted in various problems such as severe environmental pollution, food safety concerns, and emergence of drug resistance. Biological control using microorganisms or their metabolites, a more rational and safer method, has emerged as a 4-Aminobutyrate aminotransferase promising alternative to suppress plant pathogens and reduce the use of agrochemicals [1, 2]. Pelgipeptins, a group of natural

active compounds isolated from Paenibacillus elgii B69, are potential biological control agents [1]. This group of antibiotics has a general structure composed of a cyclic nonapeptide moiety and a β-hydroxy fatty acid. Four analogues of pelgipeptin have been identified and characterised [3]. These analogues are highly similar in structure and differ only in one amino acid unit or in the lipid acid (Figure1A). Pelgipeptin exhibits broad-spectrum antimicrobial activity against pathogenic bacteria and fungi, including Staphylococcus aureus Enterococcus faecalis Escherichia coli Candida albicans Fusarium oxysporum F. graminearum F. moniliforme Rhizoctonia solani, and Colletotrichum lini[1, 3]. This compound effectively inhibited the development of sheath blight caused by R. solani on rice in a preliminary evaluation of the in vivo efficacy of pelgipeptin [1]. Figure 1 Pelgipeptin and the genes responsible for its biosynthesis. (A) Primary structure of pelgipeptin. (B) The plp gene cluster and domain organisation of the NRPS. Similar to polymyxin and fusaricidin from P.