Efficient Production of Polymyxin in the Surrogate Host Bacillus subtilis by Introducing a Foreign
            <i>ectB</i>
            Gene and Disrupting the
            <i>abrB</i>
            Gene

Park, Soo Young; Choi, Soo Keun; Kim, Jihoon; Oh, Tae Kwang; Park, Seung-Hwan

doi:10.1128/aem.07912-11

Cited by 37 publications

(33 citation statements)

References 32 publications

(29 reference statements)

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“…This would make sense given that they are both the polymyxins and octapeptins are produced by closely related Bacillus spp . 62, 63 In line with this theory, the aforementioned mode of action studies suggest that octapeptins have retained the polymyxin-like ability to bind to lipid A (a Gram-negative specific outer membrane component), whilst having developed the extra ability to bind to bacterial phospholipids, which endows them with a broader spectrum of activity against Gram-positives and yeast.…”

Section: Biosynthesismentioning

confidence: 88%

“…It is tenable to imagine that in order to achieve killing of polymyxin-resistant Gram-negative and Gram-positive bacteria which were competing for nutrients in its environment, Bacillus circulans has evolved the octapeptin core scaffold through module swapping and deletion events of its nonribosomal biosynthetic machinery. 62, 63 Whereas, the polymyxin producing Bacillus polymyxa may not have encountered Gram-positive competition, and hence did not have a need to diversify the polymyxin core scaffold to increase its antimicrobial spectrum beyond Gram-negatives. This would make sense given that they are both the polymyxins and octapeptins are produced by closely related Bacillus spp .…”

Section: Biosynthesismentioning

confidence: 99%

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Rediscovering the octapeptins

Velkov

Roberts

2017

Nat. Prod. Rep.

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The decline in the discovery and development of novel antibiotics has resulted in the emergence of bacteria that are resistant to almost all available antibiotics. Currently, polymyxin B and E (colistin) are being used as the last-line therapy against life-threatening infections, unfortunately resistance to polymyxins in both the community and hospital setting is becoming more common. Octapeptins are structurally related non-ribosomal lipopeptide antibiotics that do not exhibit cross-resistance with polymyxins and have a broader spectrum of activity that includes Gram-positive bacteria. This makes them a precious and finite resource for the development of new antibiotics against these problematic polymyxin-resistant Gram-negative pathogens, in particular Pseudomonas aeruginosa, Acinetobacter baumannii and Klebsiella pneumoniae. This review surveys the progress in understanding octapeptin chemistry, mechanisms of antibacterial activity and biosynthesis. With the lack of cross-resistance and their broad antibacterial activity, the octapeptins represent ideal candidates for the development of a new generation of polymyxin-like lipopeptide antibiotics targeting polymyxin-resistant ‘superbugs’.

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Section: Biosynthesismentioning

confidence: 88%

Section: Biosynthesismentioning

confidence: 99%

Rediscovering the octapeptins

Velkov

Roberts

2017

Nat. Prod. Rep.

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“…It is necessary to propose nonlinear NRPS biosynthetic models that can further unravel the details of this biosynthetic mechanism. The Gram-positive bacterium B. subtilis serves as a model organism and is intensively used in the heterologous expression of commercial metabolites (30)(31)(32). However, apart from the present study, no nonlinear NRPS assembly line has been observed in this well-characterized species.…”

mentioning

confidence: 65%

Unusual Biosynthesis and Structure of Locillomycins from Bacillus subtilis 916

Luo

Liu

Zhou

et al. 2015

Appl Environ Microbiol

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In the competition for nutrients, members of the Bacillus genus often produce a vast array of biologically active molecules that potentially inhibit the development of competing organisms. The Gram-positive bacterium Bacillus subtilis has an average of 4 to 5% of its genome devoted to antibiotic synthesis and is able to produce more than two dozen antibiotics with an amazing variety of structures (1). Many of these compounds, which have a peptide origin, are synthesized either ribosomally or nonribosomally. Among the nonribosomally generated amphipathic cyclic lipopeptides, surfactins, iturins, and fengycins have well-recognized potential applications in biotechnology and biopharmaceutical products due to their antagonistic activities and surfactant properties (2, 3). Furthermore, the mechanisms behind the observed biocontrol efficacy of different Bacillus strains have also been well described (4-6). Lipopeptides are able to induce systemic resistance in plants and to facilitate the multicellular behaviors of the producing strains, such as swarming motility, biofilm formation, and colony morphology (5-7).Surfactins, iturins, and fengycins are synthesized by nonribosomal peptide synthetases (NRPSs) which exhibit a distinct modular architecture (2, 8-10). A module is typically composed of three core domains, with each domain responsible for a certain biochemical reaction (11). Specifically, the amino acid adenylation domain (A domain) controls the entry of substrates into the peptide structure by recognizing and activating a specific amino acid. The thiolation domain (T domain), also referred to as the peptidyl carrier protein (PCP), contains an invariant serine residue which is essential for the binding of a 4=-phosphopantetheine cofactor. The N-terminal condensation domain (C domain) is required for the coupling of two consecutively bound amino acids (12, 13). These three domains constitute a minimal elongation module, the basic repetitive unit of a multimodular NRPS. Furthermore, modules can be supplemented with domains that catalyze modifications of the activated amino acid, such as N-methylation and epimerization. In some cases, when the first module of an NRPS complex lacks a C domain, the last module contains a termination thioesterase domain (TE domain) to release the end product (14). The order and specificity of the modules within the protein template determine the sequence of the product (for type A, linear NRPSs) (8, 11). Genetic and biochemical analyses have revealed that the modular arrangement of most lipopeptide synthetases is colinear with the amino acid sequences of lipopeptides (1, 2). This assembly line arrangement of the conserved catalytic modules and domains provides the means to construct hybrid NRPSs for use in the synthesis of new lipopeptide compounds (15-18). The prospect of creating numerous bioactive lipopeptides by engineering existing lipopeptide synthetases has stimulated the search for new NRPSs responsible for lipopeptide synthesis (19-24).To date, only two reported kinds of bios...

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“…However, as a metabolite, surfactin synthesis is regulated by several global transcription genes, and these genes also regulate other gene’s expression. For example, AbrB gene encodes a repressor that controls the expression of genes involved in sporulation (Robertson et al, 1989) and the production of antibiotics (Park et al, 2012). Jung et al (2012) reported that surfactin production can be improved by activating two competence-stimulating pheromones, ComX and the competence and sporulation factor, to stimulate the transcription of srfA operon.…”

Section: Discussionmentioning

confidence: 99%

Rhizosphere Inhibition of Cucumber Fusarium Wilt by Different Surfactinexcreting Strains of Bacillus subtilis

Jia

Gao

Huang

et al. 2015

The Plant Pathology Journal

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Bacillus subtilis B006 strain effectively suppresses the cucumber fusarium wilt caused by Fusarium oxysporum f. sp. cucumerinum (Foc). The population dynamics of Foc, strain B006 and its surfactin over-producing mutant B841 and surfactin-deficient mutant B1020, in the rhizosphere were determined under greenhouse conditions to elucidate the importance of the lipopeptides excreted by these strains in suppressing Foc. Results showed that B. subtilis strain B006 effectively suppressed the disease in natural soil by 42.9%, five weeks after transplanting, whereas B841 and B1020 suppressed the disease by only 22.6% and 7.1%, respectively. Quantitative PCR assays showed that effective colonization of strain B006 in the rhizosphere suppressed Foc propagation by more than 10 times both in nursery substrate and in field-infected soil. Reduction of Foc population at the cucumber stems in a range of 0.96 log10 ng/g to 2.39 log10 ng/g was attained at the third and the fifth weeks of B006 treatment in nursery substrate. In field-infected soil, all three treatments with B. subtilis suppressed Foc infection, indicated by the reduction of Foc population at a range of 2.91 log10 ng/g to 3.36 log10 ng/g at the stem base, one week after transplanting. This study reveals that the suppression of fusarium wilt disease is affected by the effective colonization of the surfactin-producing B. subtilis strain in the rhizosphere. These results improved our understanding of the biocontrol mechanism of the B. subtilis strain B006 in the natural soil and facilitate its application as biocontrol agent in the field.

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Efficient Production of Polymyxin in the Surrogate Host Bacillus subtilis by Introducing a Foreign ectB Gene and Disrupting the abrB Gene

Cited by 37 publications

References 32 publications

Rediscovering the octapeptins

Rediscovering the octapeptins

Unusual Biosynthesis and Structure of Locillomycins from Bacillus subtilis 916

Rhizosphere Inhibition of Cucumber Fusarium Wilt by Different Surfactinexcreting Strains of Bacillus subtilis

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