Hexose phosphate metabolism and exopolysaccharide formation inPseudomonas cepacia

Sage, Andrew; Linker, Alfred; Evans, Leigh R.; Lessie, T G

doi:10.1007/bf02091996

Cited by 62 publications

(60 citation statements)

References 30 publications

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“…Sugar agar contained 20 g of the sugar of interest, 2 g yeast extract, and 15 g bacteriological agar dissolved in 1 l distilled H 2 O (Sage et al, 1990). The sugars used were as follows: D-fructose, D-galactose, D-mannitol, D-glucose, glycerol, lactose, L-rhamnose, Dmannose, maltose, sucrose, myo-inositol, ribitol (adonitol) and Dglucitol (sorbitol).…”

Section: Methodsmentioning

confidence: 99%

“…The ability of these and related compounds to stimulate EPS biosynthesis in Bcc was then investigated (Table 1). Glycerol and mannitol were included as these sugar alcohols have previously been noted to enhance EPS biosynthesis in Pseudomonas aeruginosa (Whitchurch et al, 1996) and the Bcc (Sage et al, 1990;Zlosnik et al, 2008). Glucitol was included because of its close degradative relationship with fructose and mannitol (Allenza et al, 1982).…”

Section: The Onion Factormentioning

confidence: 99%

“…Other studies have shown that mucoid Bcc isolates mostly synthesize one type of EPS, with a highly branched heptasaccharide repeating unit, which was named cepacian (Moreira et al, 2003;Sist et al, 2003). EPS production has been shown to increase when the Bcc are grown in mannitol-rich yeast extract medium (MYEM) (Sage et al, 1990;Zlosnik et al, 2008).…”

Section: Introductionmentioning

confidence: 99%

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Plant host and sugar alcohol induced exopolysaccharide biosynthesis in the Burkholderia cepacia complex

et al. 2008

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The species that presently constitute the Burkholderia cepacia complex (Bcc) have multiple roles; they include soil and water saprophytes, bioremediators, and plant, animal and human pathogens. Since the first description of pathogenicity in the Bcc was based on sour skin rot of onion bulbs, this study returned to this plant host to investigate the onion-associated phenotype of the Bcc. Many Bcc isolates, which were previously considered to be non-mucoid, produced copious amounts of exopolysaccharide (EPS) when onion tissue was provided as the sole nutrient. EPS production was not species-specific, was observed in isolates from both clinical and environmental sources, and did not correlate with the ability to cause maceration of onion tissue. Chemical analysis suggested that the onion components responsible for EPS induction were primarily the carbohydrates sucrose, fructose and fructans. Additional sugars were investigated, and all alcohol sugars tested were able to induce EPS production, in particular mannitol and glucitol. To investigate the molecular basis for EPS biosynthesis, we focused on the highly conserved bce gene cluster thought to be involved in cepacian biosynthesis. We demonstrated induction of the bce gene cluster by mannitol, and found a clear correlation between the inability of representatives of the Burkholderia cenocepacia ET12 lineage to produce EPS and the presence of an 11 bp deletion within the bceB gene, which encodes a glycosyltransferase. Insertional inactivation of bceB in Burkholderia ambifaria AMMD results in loss of EPS production on sugar alcohol media. These novel and surprising insights into EPS biosynthesis highlight the metabolic potential of the Bcc and show that a potential virulence factor may not be detected by routine laboratory culture. Our results also highlight a potential hazard in the use of inhaled mannitol as an osmolyte to improve mucociliary clearance in individuals with cystic fibrosis.

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Section: Methodsmentioning

confidence: 99%

Section: The Onion Factormentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Plant host and sugar alcohol induced exopolysaccharide biosynthesis in the Burkholderia cepacia complex

et al. 2008

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“…The Entner-Doudoroff (ED) pathway enzymes, 6-phosphogluconate dehydratase and 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase were assayed together as described previously by Wood (1972). Other enzymes were assayed as follows: glucokinase (Sage et al, 1990); gluconate kinase (Ng & Dawes, 1973) ; glucose dehydrogenase (Matsushita & Ameyama, 1982) ; Zwf and phosphoglucoisomerase (Pgi) (Lessie & Neidhardt, 1967) ; glyceraldehyde-3-phosphate dehydrogenase (Oshima e t al., 1982); ICDH (Keys & McAlister-Henn, 1990); phosphoglucomutase (Adhya & Schwartz, 1971) ; 6-phosphogluconate dehydrogenase (Lessie & Vander Wyk, 1972).…”

Section: Media and Growth Of Bacterial Cells For Genetic Workmentioning

confidence: 99%

Glucose metabolism in 'Sphingomonas elodea': pathway engineering via construction of a glucose-6-phosphate dehydrogenase insertion mutant

Vartak

Lin²,

Cleary³

et al. 1995

Microbiology

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“…In this report, we demonstrate that full induction of plcH by choline requires several hours when P. aeruginosa is grown in a medium containing succinate as the carbon source (45); however, if a non-catabolite-repressing substrate for P. aeruginosa, such as lactate, is substituted for succinate, induction occurs within 30 min (39). Also, choline transport and acid phosphatase, an enzyme involved in the conversion of PC to choline, have been reported to be subject to CRC (42).…”

mentioning

confidence: 93%

Osmoprotectant-dependent expression of plcH, encoding the hemolytic phospholipase C, is subject to novel catabolite repression control in Pseudomonas aeruginosa PAO1

Sage

Vasil

1997

J Bacteriol

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Expression of the hemolytic phospholipase C (PlcH) of Pseudomonas aeruginosa is induced under phosphate starvation conditions or in the presence of the osmoprotectants choline and glycine betaine. Because choline and glycine betaine may serve as carbon and energy sources in addition to conferring osmoprotection to P. aeruginosa, it seemed possible that induction of plcH is subject to catabolite repression control (CRC) by tricarboxylic cycle intermediates such as succinate. Total phospholipase (PLC) activity in osmoprotectantinduced cultures of P. aeruginosa PAO1 supplemented with 20 mM succinate was three-to fourfold lower than the levels in cultures supplemented with the non-catabolite-repressive substrate lactate. Analyses of osmoprotectant-dependent plcH expression in a derivative of strain PAO1 containing a plcH::lacZ operon fusion showed that (i) succinate prevented induction of plcH expression by osmoprotectants; and (ii) addition of succinate reduced or shut down further expression of plcH in osmoprotectant-induced bacteria, while cultures supplemented with lactate had little or no change in plcH expression. RNase protection analysis confirmed that repression of plcH occurs at the transcriptional level. However, a P. aeruginosa mutant decoupled in CRC exhibited a phenotype similar to that of the wild-type strain (PAO1) with respect to succinate-dependent repression of plcH expression. Osmoprotectant-induced total PLC activities, levels of expression of plcH measured with the same plcH::lacZ fusion, and levels of plcH transcription in a CRC-deficient strain reflected those seen in strain PAO1. This indicates that CRC of plcH functions by a distinct mechanism which differs from that regulating the glucose or mannitol catabolic pathway. A strain carrying a mutation in vfr, which encodes the Escherichia coli Crp homolog in P. aeruginosa, still exhibited a wild-type phenotype with respect to osmoprotectant-dependent expression and CRC of plcH. These data indicate that there is a novel CRC system that regulates the expression of plcH in P. aeruginosa.

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Hexose phosphate metabolism and exopolysaccharide formation inPseudomonas cepacia

Cited by 62 publications

References 30 publications

Plant host and sugar alcohol induced exopolysaccharide biosynthesis in the Burkholderia cepacia complex

Plant host and sugar alcohol induced exopolysaccharide biosynthesis in the Burkholderia cepacia complex

Glucose metabolism in 'Sphingomonas elodea': pathway engineering via construction of a glucose-6-phosphate dehydrogenase insertion mutant

Osmoprotectant-dependent expression of plcH, encoding the hemolytic phospholipase C, is subject to novel catabolite repression control in Pseudomonas aeruginosa PAO1

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