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Dive into the research topics where Neil P. J. Price is active.

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Featured researches published by Neil P. J. Price.


International Journal of Systematic and Evolutionary Microbiology | 2009

Phylogeny and molecular taxonomy of the Bacillus subtilis species complex and description of Bacillus subtilis subsp. inaquosorum subsp. nov.

Alejandro P. Rooney; Neil P. J. Price; Christopher J. Ehrhardt; James L. Swezey; Jason D. Bannan

The Bacillus subtilis species complex is a tight assemblage of closely related species. For many years, it has been recognized that these species cannot be differentiated on the basis of phenotypic characteristics. Recently, it has been shown that phylogenetic analysis of the 16S rRNA gene also fails to differentiate species within the complex due to the highly conserved nature of the gene, yet DNA-DNA hybridization values fall well below 70 % for the same species comparisons. As a complementary approach, we propose that phylogenetic analysis of multiple protein-coding loci can be used as a means to detect and differentiate novel Bacillus taxa. Indeed, our phylogenetic analyses revealed the existence of a previously unknown group of strains closely related to, but distinct from, Bacillus subtilis subsp. spizizenii. Results of matrix-assisted laser desorption ionization-time of flight mass spectrometry analyses revealed that the group produces a novel surfactin-like lipopeptide with mass m/z 1120.8 that is not produced by the other currently recognized subspecies. In addition, the group displayed differences in the total cellular content of the fatty acids C(16 : 0) and iso-C(17 : 1)omega10c that distinguish it from the closely related B. subtilis subsp. spizizenii. Consequently, the correlation of these novel phenotypic traits with the phylogenetic distinctiveness of this previously unknown subspecies group showed that phylogenetic analysis of multiple protein-coding loci can be used as a means to detect and differentiate novel Bacillus taxa. Therefore, we propose that this new group should be recognized as representing a novel taxon, Bacillus subtilis subsp. inaquosorum subsp. nov., with the type strain NRRL B-23052(T) (=KCTC 13429(T)=BGSC 3A28(T)).


Fems Microbiology Letters | 2010

Production of sophorolipid biosurfactants by multiple species of the Starmerella (Candida) bombicola yeast clade

Cletus P. Kurtzman; Neil P. J. Price; Karen Ray; Tsung-Min Kuo

Sophorolipids are carbohydrate-based, amphiphilic biosurfactants that are of increasing interest for use in environmentally benign cleaning agents. Sophorolipid production was tested for 26 strains representing 19 species of the Starmerella yeast clade, including Starmerella bombicola and Candida apicola, which were previously reported to produce sophorolipids. Five of the 19 species tested showed significant production of sophorolipids: S. bombicola, C. apicola, Candida riodocensis, Candida stellata and a new species, Candida sp. NRRL Y-27208. A high-throughput matrix-assisted laser desorption/ionization-time of flight MS assay was developed that showed S. bombicola and C. apicola to produce a lactone form of sophorolipid, whereas C. riodocensis, C. stellata and Candida sp. NRRL Y-27208 produced predominantly free acid sophorolipids. Phylogenetic analysis of sequences for the D1/D2 domains of the nuclear large subunit rRNA gene placed all sophorolipid-producing species in the S. bombicola subclade of the Starmerella clade.


Fems Microbiology Letters | 2009

Isolation and characterization of rhamnolipid‐producing bacterial strains from a biodiesel facility

Alejandro P. Rooney; Neil P. J. Price; Karen Ray; Tsung-Min Kuo

Novel strains of rhamnolipid-producing bacteria were isolated from soils at a biodiesel facility on the basis of their ability to grow on glycerol as a sole carbon source. Strains were identified as Acinetobacter calcoaceticus, Enterobacter asburiae, Enterobacter hormaechei, Pantoea stewartii, and Pseudomonas aeruginosa. The strains of the former five species were found to produce rhamnolipids in quantities the same as, or similar to, coisolated strains of P. aeruginosa. Measurements of surface tension revealed that that emulsifying properties of these strains were similar to levels displayed by rhamnolipids produced by P. aeruginosa. Results of matrix-assisted laser desorption/ionization time-of-flight MS analyses revealed that the predominant compounds made by all strains were C10-C10 mono- and dirhamnolipids. Notably, E. hormaechei and one strain of A. calcoaceticus produced rhamnolipids in amounts similar to the pseudomonads. As all strains examined were from the same taxonomic class of Proteobacteria, further examination of this group may reveal many additional species not previously known to produce rhamnolipids in addition to novel strains of species currently known to produce rhamnolipids.


Carbohydrate Research | 2009

MALDI-TOF mass spectrometry of naturally occurring mixtures of monorhamnolipids and dirhamnolipids ☆

Neil P. J. Price; Karen J. Ray; Karl Vermillion; Tsung-Min Kuo

MALDI-TOFMS approaches have been developed for high-throughput screening of naturally occurring mixtures of rhamnolipids from Pseudomonas spp. Monorhamnolipids and dirhamnolipids are readily distinguished by characteristic molecular adduct ions, [M+Na](+) and [M-H+Na(2)](+), with variously acylated rhamnolipids differing by 28 mu. Following proton-deuterium exchange, deuterated [M+Na-4(1)H+4(2)H](+) and [M+Na-6(1)H+6(2)H](+) ions are observed for the monorhamnolipids and dirhamnolipids, respectively, which allows rapid identification of these molecules. The described approach has been validated by compositional analysis using GC/MS, fractionation by RPHPLC, and analysis by 1D and 2D NMR spectroscopy. MALDI-TOFMS analysis allows the rapid screening of variously acylated rhamnolipids, and has potential for selective identification of new surfactants from microbial strains.


Journal of Microbiology | 2011

Cyclic lipopeptide profile of three Bacillus subtilis strains; antagonists of Fusarium head blight

Christopher A. Dunlap; David A. Schisler; Neil P. J. Price; Steven F. Vaughn

The objective of the study was to identify the lipopetides associated with three Bacillus subtilis strains. The strains are antagonists of Gibberella zeae, and have been shown to be effective in reducing Fusarium head blight in wheat. The lipopeptide profile of three B. subtilis strains (AS43.3, AS43.4, and OH131.1) was determined using mass spectroscopy. Strains AS43.3 and AS43.4 produced the anti-fungal lipopeptides from the iturin and fengycin family during the stationary growth phase. All three strains produced the lipopeptide surfactin at different growth times. Strain OH131.1 only produced surfactin under these conditions. The antifungal activity of the culture supernatant and individual lipopeptides was determined by the inhibition of G. zeae. Cell-free supernatant from strains AS43.3 and AS43.4 demonstrated strong antibiosis of G. zeae, while strain OH131.1 had no antibiosis activity. These results suggest a different mechanism of antagonism for strain OH131.1, relative to AS43.3 and AS43.4.


Applied and Environmental Microbiology | 2008

Catabolic Pathway for the Production of Skatole and Indoleacetic Acid by the Acetogen Clostridium drakei, Clostridium scatologenes, and Swine Manure

Terence R. Whitehead; Neil P. J. Price; Harold L. Drake; Michael A. Cotta

ABSTRACT Skatole (3-methylindole) is a malodorous chemical in stored swine manure and is implicated as a component of foul-tasting pork. Definitive evidence for the skatole pathway is lacking. Deuterium-labeled substrates were employed to resolve this pathway in the acetogenic bacterium Clostridium drakei and Clostridium scatologenes and to determine if a similar pathway is used by microorganisms present in stored swine manure. Indoleacetic acid (IAA) was synthesized from tryptophan by both bacteria, and skatole was synthesized from both IAA and tryptophan. Microorganisms in swine manure produced skatole and other oxidation products from tryptophan, but IAA yielded only skatole. A catabolic mechanism for the synthesis of skatole is proposed.


Carbohydrate Research | 2012

Structural characterization of novel sophorolipid biosurfactants from a newly identified species of Candida yeast

Neil P. J. Price; Karen J. Ray; Karl Vermillion; Christopher A. Dunlap; Cletus P. Kurtzman

Sophorolipids are a group of O-acylsophorose-based biosurfactants produced by several yeasts of the Starmerella clade. The known sophorolipids are typically partially acetylated 2-O-β-D-glucopyranosyl-D-glucopyranose (sophorose) O-β-glycosidically linked to 17-L-hydroxy-Δ9-octadecenoic acid, where the acyl carboxyl group often forms a 4″-lactone to the terminal glucosyl residue. In a recent MALDI-TOFMS-based screen for sophorolipid-producing yeasts we identified a new species, Candida sp. NRRL Y-27208, that produces significant amounts of novel sophorolipids. This paper describes the structural characterization of these new compounds, using carbohydrate and lipid analysis, mass spectrometry, and NMR spectroscopy. Unlike those reported previously, the NRRL Y-27208 sophorolipids contain an ω-hydroxy-linked acyl group (typically 18-hydroxy-Δ9-octadecenoate), and occur predominantly in a non-lactone, anionic form. In addition, 17 dimeric and trimeric sophoroses were identified by MALDI-TOFMS from this strain. The surfactant-like properties of these sophorolipids have value as potential replacements for petroleum-based detergents and emulsifiers.


Applied and Environmental Microbiology | 2012

Glucosylation and other biotransformations of T-2 toxin by yeasts of the trichomonascus clade.

Susan P. McCormick; Neil P. J. Price; Cletus P. Kurtzman

ABSTRACT Trichothecenes are sesquiterpenoid toxins produced by Fusarium species. Since these mycotoxins are very stable, there is interest in microbial transformations that can remove toxins from contaminated grain or cereal products. Twenty-three yeast species assigned to the Trichomonascus clade (Saccharomycotina, Ascomycota), including four Trichomonascus species and 19 anamorphic species presently classified in Blastobotrys, were tested for their ability to convert the trichothecene T-2 toxin to less-toxic products. These species gave three types of biotransformations: acetylation to 3-acetyl T-2 toxin, glycosylation to T-2 toxin 3-glucoside, and removal of the isovaleryl group to form neosolaniol. Some species gave more than one type of biotransformation. Three Blastobotrys species converted T-2 toxin into T-2 toxin 3-glucoside, a compound that has been identified as a masked mycotoxin in Fusarium-infected grain. This is the first report of a microbial whole-cell method for producing trichothecene glycosides, and the potential large-scale availability of T-2 toxin 3-glucoside will facilitate toxicity testing and development of methods for detection of this compound in agricultural and other products.


Journal of Biological Chemistry | 2011

Identification of a chitinase-modifying protein from Fusarium verticillioides: truncation of a host resistance protein by a fungalysin metalloprotease.

Todd A. Naumann; Donald T. Wicklow; Neil P. J. Price

Background: Fusarium fungi manipulate plant defenses to cause disease. Results: Fusarium fungi secrete fungalysin proteases that truncate maize class IV chitinases. Conclusions: Fusarium fungalysins target nonstructural defense proteins associated with plant disease resistance. Significance: Manipulating the fungalysin-chitinase interaction might improve fungal disease resistance of plants. Chitinase-modifying proteins (cmps) are proteases secreted by fungal pathogens that truncate the plant class IV chitinases ChitA and ChitB during maize ear rot. cmp activity has been characterized for Bipolaris zeicola and Stenocarpella maydis, but the identities of the proteases are not known. Here, we report that cmps are secreted by multiple species from the genus Fusarium, that cmp from Fusarium verticillioides (Fv-cmp) is a fungalysin metalloprotease, and that it cleaves within a sequence that is conserved in class IV chitinases. Protein extracts from Fusarium cultures were found to truncate ChitA and ChitB in vitro. Based on this activity, Fv-cmp was purified from F. verticillioides. N-terminal sequencing of truncated ChitA and MALDI-TOF-MS analysis of reaction products showed that Fv-cmp is an endoprotease that cleaves a peptide bond on the C-terminal side of the lectin domain. The N-terminal sequence of purified Fv-cmp was determined and compared with a set of predicted proteins, resulting in its identification as a zinc metalloprotease of the fungalysin family. Recombinant Fv-cmp also truncated ChitA, confirming its identity, but had reduced activity, suggesting that the recombinant protease did not mature efficiently from its propeptide-containing precursor. This is the first report of a fungalysin that targets a nonstructural host protein and the first to implicate this class of virulence-related proteases in plant disease.


Protein & Cell | 2010

Characterization of the tunicamycin gene cluster unveiling unique steps involved in its biosynthesis

Wenqing Chen; Dongjing Qu; Lipeng Zhai; Meifeng Tao; Yemin Wang; Shuangjun Lin; Neil P. J. Price; Zixin Deng

Tunicamycin, a potent reversible translocase I inhibitor, is produced by several Actinomycetes species. The tunicamycin structure is highly unusual, and contains an 11-carbon dialdose sugar and an α, β-1″,11′-glycosidic linkage. Here we report the identification of a gene cluster essential for tunicamycin biosynthesis by high-throughput heterologous expression (HHE) strategy combined with a bioassay. Introduction of the genes into heterologous non-producing Streptomyces hosts results in production of tunicamycin by these strains, demonstrating the role of the genes for the biosynthesis of tunicamycins. Gene disruption experiments coupled with bioinformatic analysis revealed that the tunicamycin gene cluster is minimally composed of 12 genes (tunA-tunL). Amongst these is a putative radical SAM enzyme (Tun B) with a potentially unique role in biosynthetic carbon-carbon bond formation. Hence, a seven-step novel pathway is proposed for tunicamycin biosynthesis. Moreover, two gene clusters for the potential biosynthesis of tunicamycin-like antibiotics were also identified in Streptomyces clavuligerus ATCC 27064 and Actinosynnema mirums DSM 43827. These data provide clarification of the novel mechanisms for tunicamycin biosynthesis, and for the generation of new-designer tunicamycin analogs with selective/enhanced bioactivity via combinatorial biosynthesis strategies.

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Timothy D. Leathers

United States Department of Agriculture

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Kenneth M. Bischoff

National Center for Agricultural Utilization Research

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Todd A. Naumann

National Center for Agricultural Utilization Research

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Karl E. Vermillion

National Center for Agricultural Utilization Research

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Cletus P. Kurtzman

Agricultural Research Service

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Melinda S. Nunnally

National Center for Agricultural Utilization Research

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Anthony Adeuya

Agricultural Research Service

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Christopher D. Skory

National Center for Agricultural Utilization Research

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