ChemInform Abstract: LI‐F Antibiotics, a Family of Antifungal Cyclic Depsipeptides Produced by Bacillus polymyxa L‐1129

Kuroda, Jun; Fukai, Toshio; Konishi, Masataka; Uno, Jun; Kurusu, Keiji; Nomura, Taro

doi:10.1002/chin.200042217

Cited by 8 publications

(17 citation statements)

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“…From our results, the sequence of fusaricidins could be determined efficiently. They are in excellent agreement with previous structure analysis of fusaricidins performed by other authors [5][6][7][8][9][10][11]. However, in our MALDI-TOF-MS study of the fusaricidins, it was not possible to discriminate between Leu, Ile, and allo-Ile in positions 2 and 3 of the fusaricidin sequence because the corresponding w-ions were missing in the product ion spectra.…”

Section: Structural Characterization Of Fusaricidins From Lift-maldi-supporting

confidence: 91%

“…The main components of the fusaricidin complex, which have already been investigated by other authors, are indicated in Table 1. They are fusaricidins A-D, which have been characterized in detail by Kajimura et al [6,7] and those designated by the LI-F-nomenclature introduced by Kurusu et al [5] and Kuroda et al [8,9]. All other fusaricidin variants in Table 1 were detected and characterized by us for the first time.…”

Section: Demonstration Of the Fusaricidin Complex By Maldi-tof-msmentioning

confidence: 75%

“…The most frequent products are lipopeptides [2][3][4][5][6][7][8][9][10][11][12][13][14][15][16], peptide/polyketide hybrids [17,18], as well as lantibiotics [19,20]. Such products qualify Paenibacillus strains for applications in agriculture, medicine, and biotechnology.…”

Section: Introductionmentioning

confidence: 99%

“…Fusaricidins are a class of cyclic lipohexapeptides with potent antifungal activities [5][6][7][8][9][10][11]. They contain 15-guanidino-3-hydroxypentadecanoic acid (GHPD) integrated in a ring of six amino acids.…”

Section: Introductionmentioning

confidence: 99%

“…The biosynthesis of fusaricidin is catalyzed by a multifunctional enzyme FusA comprising six modules, which are equipped with the domains for activation, modification, and condensation of the amino acid substrates [32,33]. Fusaricidins and the related LI-F-antibiotics were discovered and investigated by Kurusu et al [5], Kajimura et al [6,7], and Kuroda et al [8,9]. Their structure has been elucidated mainly by two-dimensional-NMR methodology.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of Novel Fusaricidins Produced by Paenibacillus polymyxa-M1 Using MALDI-TOF Mass Spectrometry

Vater

Niu

Dietel³

et al. 2015

J. Am. Soc. Mass Spectrom.

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Abstract. Paenibacillus polymyxa-M1 is a potent producer of bioactive compounds, such as lipopeptides, polyketides, and lantibiotics of biotechnological and medical interest. Genome sequencing revealed nine gene clusters for nonribosomal biosynthesis of such agents. Here we report on the investigation of the fusaricidins, a complex of cyclic lipopeptides containing 15-guanidino-3-hydroxypentadecanoic acid (GHPD) as fatty acid component by matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS). More than 20 variants of these compounds were detected and characterized in detail. Mass spectrometric sequence analysis was performed by MALDI-LIFT-TOF/TOF fragment analysis. The obtained product ion spectra show a specific processing in the fatty acid part. GHPD is cleaved between the α-and ß-position yielding two fragments a and b, one bearing the end-standing guanidine group and another one comprising the residual two C-atoms of GHPD with the attached peptide moiety. The complete sequence of all fusaricidins was derived from sets of b n -and y n -ions. The fusaricidin complex can be divided into four lipopeptide families, three of them showing variations of the amino acid in position 3, Val or Ile for the first and Tyr or Phe for families 2 and 3, respectively. A collection of novel fusaricidins was detected differing from those of families 1-3 by an additional residue of 71 Da (family 4). LIFT-TOF/TOF fragment spectra of these species imply that in their peptide moiety, an Ala-residue is attached by an ester bond to the free hydroxyl group of Thr 4 . More than 10 novel fusaricidins were characterized mass spectrometrically.

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Section: Structural Characterization Of Fusaricidins From Lift-maldi-supporting

confidence: 91%

Section: Demonstration Of the Fusaricidin Complex By Maldi-tof-msmentioning

confidence: 75%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Characterization of Novel Fusaricidins Produced by Paenibacillus polymyxa-M1 Using MALDI-TOF Mass Spectrometry

Vater

Niu

Dietel³

et al. 2015

J. Am. Soc. Mass Spectrom.

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Use of PCR-Targeted Mutagenesis To Disrupt Production of Fusaricidin-Type Antifungal Antibiotics in Paenibacillus polymyxa

Beatty

Shah³

et al. 2007

Appl Environ Microbiol

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Paenibacillus polymyxa (formerly Bacillus polymyxa) PKB1 has been identified as a potential agent for biocontrol of blackleg disease of canola, caused by the pathogenic fungus Leptosphaeria maculans. The factors presumed to contribute to disease suppression by strain PKB1 include the production of fusaricidin-type antifungal metabolites that appear around the onset of bacterial sporulation. The fusaricidins are a family of lipopeptide antibiotics consisting of a ␤-hydroxy fatty acid linked to a cyclic hexapeptide. Using a reverse genetic approach based on conserved motifs of nonribosomal peptide synthetases, a DNA fragment that appears to encode the first two modules of the putative fusaricidin synthetase (fusA) was isolated from PKB1. To confirm the involvement of fusA in production of fusaricidins, a modified PCR targeting mutagenesis protocol was developed to create a fusA mutation in PKB1. A DNA fragment internal to fusA was replaced by a gene disruption cassette containing two antibiotic resistance genes for independent selection of apramycin resistance in Escherichia coli and chloramphenicol resistance in P. polymyxa. Inclusion of an oriT site in the disruption cassette allowed efficient transfer of the inactivated fusA allele to P. polymyxa by intergeneric conjugation. Targeted disruption of fusA led to the complete loss of antifungal activity against L. maculans, suggesting that fusA plays an essential role in the nonribosomal synthesis of fusaricidins.Canola is an economically important oilseed crop grown in Canada and throughout the world. Significant losses in canola seed quality and yield occur every year due to phoma stem canker (blackleg) disease, caused by the fungus Leptosphaeria maculans. The methods that have been applied to control the severity and spread of blackleg include implementation of improved cultural practices, use of fungicides, and breeding of blackleg-resistant cultivars (37), but better control methods are still needed. In an effort to develop efficient and environmentally safe biocontrol agents for blackleg disease, a strain of Paenibacillus polymyxa (designated PKB1) highly inhibitory to the growth of L. maculans was isolated from canola stubble (18).A naturally soilborne bacterium, P. polymyxa possesses several properties desirable in a biocontrol agent active against plant-pathogenic fungi, including production of desiccation-and heat-resistant endospores, and intrinsic resistance to several fungicides and herbicides approved for use on canola crops in Canada. Strains of P. polymyxa have also been shown to produce a wide range of peptide antibiotics, which may give them a growth advantage in the competitive soil environment. The peptide metabolites that have been identified in various isolates of P. polymyxa are generally classified into two groups according to their antimicrobial activities. Members of the first group include the polymyxins (17), polypeptins (32), jolipeptin (12, 13), gavaserin, and saltavalin (27) and are typified by antibacterial activity against both gram...

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Comparative and Functional Analyses of Two Sequenced Paenibacillus polymyxa Genomes Provides Insights Into Their Potential Genes Related to Plant Growth-Promoting Features and Biocontrol Mechanisms

Gao

Wang

2020

Front. Genet.

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Many bacteria belonging to Paenibacillus polymyxa are plant growth-promoting rhizobacteria (PGPR) with the potential to promote plant growth and suppress phytopathogens and have been used as biological control agents (BCAs). However, the growth promotion and biocontrol mechanisms of P. polymyxa have not been thoroughly elucidated thus far. In this investigation, the genome sequences of two P. polymyxa strains, ZF129 and ZF197, with broad anti-pathogen activities and potential for growth promotion were comparatively studied. Comparative and functional analyses of the two sequenced P. polymyxa genomes showed that the ZF129 genome consists of one 5,703,931 bp circular chromosome and two 79,020 bp and 37,602 bp plasmids, designated pAP1 and pAP2, respectively. The complete genome sequence of ZF197 consists of one 5,507,169 bp circular chromosome and one 32,065 bp plasmid, designated pAP197. Phylogenetic analysis revealed that ZF129 is highly similar to two P. polymyxa strains, HY96-2 and SQR-21, while ZF197 is highly similar to P. polymyxa strain J. The genes responsible for secondary metabolite synthesis, plant growth-promoting traits, and systemic resistance inducer production were compared between strains ZF129 and ZF197 as well as other P. polymyxa strains. The results indicated that the variation of the corresponding genes or gene clusters between strains ZF129 and ZF197 may lead to different antagonistic activities of their volatiles or cell-free supernatants against Fusarium oxysporum. This work indicates that plant growth promotion by P. polymyxa is largely mediated by phytohormone production, increased nutrient availability and biocontrol mechanisms. This study provides an in-depth understanding of the genome architecture of P. polymyxa, revealing great potential for the application of this bacterium in the fields of agriculture and horticulture as a PGPR.

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ChemInform Abstract: LI‐F Antibiotics, a Family of Antifungal Cyclic Depsipeptides Produced by Bacillus polymyxa L‐1129

Cited by 8 publications

References 1 publication

Characterization of Novel Fusaricidins Produced by Paenibacillus polymyxa-M1 Using MALDI-TOF Mass Spectrometry

Characterization of Novel Fusaricidins Produced by Paenibacillus polymyxa-M1 Using MALDI-TOF Mass Spectrometry

Use of PCR-Targeted Mutagenesis To Disrupt Production of Fusaricidin-Type Antifungal Antibiotics in Paenibacillus polymyxa

Comparative and Functional Analyses of Two Sequenced Paenibacillus polymyxa Genomes Provides Insights Into Their Potential Genes Related to Plant Growth-Promoting Features and Biocontrol Mechanisms

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