Maltose utilization in Enterococcus faecalis

Breton, Yoann Le; Pichereau, Vianney; Sauvageot, Nicolas; Auffray, Yanick; Rincé, Alain

doi:10.1111/j.1365-2672.2004.02468.x

Cited by 35 publications

(49 citation statements)

References 37 publications

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“…Based on the KEGG website, each of these PTS systems appears to be sugar specific, with EF408 to -412 specific for mannitol, EF0955 to -0958 for maltose, and EF3210 to -3213 for mannose. Interestingly, the ef0954 to -0958 locus has been described in two different papers: (i) as bopABCD (ef0957 to -0954) (20) and (ii) as malT (ef0958) and malPBMR (ef0957 to -0954) (24). Both malT (ef0958) and malP (ef0957/bopA) appear to be essential for maltose transport and utilization in strain JH2-2 (24) and, using E. faecalis type 9 strain, bopD (ef0954/malR, a LacI family transcriptional regulator), but not bopABC, appears to be important for biofilm formation and for bacteremia in mice (20).…”

Section: Vol 188 2006 Transcriptional Analysis Of Og1rf and A ⌬Fsrbmentioning

confidence: 99%

Comparison of OG1RF and an IsogenicfsrBDeletion Mutant by Transcriptional Analysis: the Fsr System ofEnterococcus faecalisIs More than the Activator of Gelatinase and Serine Protease

Bourgogne¹,

et al. 2006

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The FsrABC system of Enterococcus faecalis controls the expression of gelatinase and a serine protease via a quorum-sensing mechanism, and recent studies suggest that the Fsr system may also regulate other genes important for virulence. To investigate the possibility that Fsr influences the expression of additional genes, we used transcriptional profiling, with microarrays based on the E. faecalis strain V583 sequence, to compare the E. faecalis strain OG1RF with its isogenic mutant, TX5266, an fsrB deletion mutant. We found that the presence of an intact fsrB influences expression of numerous genes throughout the growth phases tested, namely, late log to early stationary phase. In addition, the Fsr regulon is independent of the activity of the proteases, GelE and SprE, whose expression was confirmed to be activated at all three time points tested. While expression of some genes (i.e., ef1097 and ef0750 to -757, encoding hypothetical proteins) was activated in late log phase in OG1RF versus the fsrB deletion mutant, expression of ef1617 to -1634 (eut-pdu orthologues) was highly repressed by the presence of an intact Fsr at entry into stationary phase. This is the first time that Fsr has been characterized as a negative regulator. The newly recognized Fsr-regulated targets include other factors, besides gelatinase, described as important for biofilms (BopD), and genes predicted to encode the surface proteins EF0750 to -0757 and EF1097, along with proteins implicated in several metabolic pathways, indicating that the FsrABC system may be an important regulator in strain OG1RF, with both positive and negative effects.Enterococcus faecalis is adapted to survive, persist, and proliferate in a wide range of environments as different as the gastrointestinal tract, heart valves, water, and soil. To do so, it is likely that E. faecalis has developed various mechanisms of adaptation. Examples include transcriptional regulators, such as hypR (47) or efaR (25); two-component systems (etaRS [46], croRS [9], vanSR [11], and RR1-13 [18]); and cell-cell signaling systems, including pheromone-inducible plasmid transfer (for a review, see reference 7), the Cyl system (8, 16), and the FsrABC system (30,31,34,35).The fsrABC operon, a homologue of agrABCD in Staphylococcus aureus, was originally shown by Qin et al. to activate, at the transcriptional level, the expression of two genes, gelE and sprE, coding for a metalloprotease and a serine protease, in addition to fsrBC (34, 35). Nakayama et al. and Qin et al. subsequently purified and characterized the FsrABC system pheromone as an 11-residue peptide lactone, produced from the C-terminal portion of the fsrB gene product and reaching peak levels at entry into stationary phase (ENT-stat) (30,31,35). Studies have also shown that, in the majority of the strains studied, a gelE ϩ genotype with a GelE Ϫ phenotype is associated with a 23.9-kb deletion, from ef1841 through part of ef1820 (ef1820 is fsrC). This deletion is found in many distinct clinical strains, as well as in isolates fr...

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Section: Vol 188 2006 Transcriptional Analysis Of Og1rf and A ⌬Fsrbmentioning

confidence: 99%

Comparison of OG1RF and an IsogenicfsrBDeletion Mutant by Transcriptional Analysis: the Fsr System ofEnterococcus faecalisIs More than the Activator of Gelatinase and Serine Protease

Bourgogne¹,

et al. 2006

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“…lactic acid bacteria such as Streptococcus bovis, Lactococcus lactis, Lactobacillus sanfrancensis and Enterococcus faecalis (Ehrmann & Vogel, 1998; Nilsson & Radström, 2001;Le Breton et al, 2005) or the endosporeforming Bacillus subtilis (Schönert et al, 2006), has been thoroughly investigated, and proceeds by different pathways, which, unlike the pathway present in E. coli ( Fig. 1), generally do not include reactions that form maltodextrins.…”

Section: Introductionmentioning

confidence: 99%

“…faecalis, maltose uptake is accomplished by a phosphotransferase system (PTS); the maltose 6-phosphate thereby formed is cleaved by maltose-6-phosphate phosphorylase to glucose 6-phosphate and b-glucose 1-phosphate (Le Breton et al, 2005). The conversion of b-glucose 1-phosphate to glucose 6-phosphate is catalysed in these lactic acid bacteria by b-phosphoglucomutase (b-Pgm) (Levander et al, 2001;Ehrmann & Vogel, 1998;Le Breton et al, 2005). In B. subtilis, the uptake of maltose and of maltodextrins is accomplished by a maltose-specific PTS and a maltodextrin-specific ATP-binding cassette (ABC) transporter, respectively (Schönert et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

Roles of maltodextrin and glycogen phosphorylases in maltose utilization and glycogen metabolism in Corynebacterium glutamicum

2009

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Corynebacterium glutamicum transiently accumulates large amounts of glycogen, when cultivated on glucose and other sugars as a source of carbon and energy. Apart from the debranching enzyme GlgX, which is required for the formation of maltodextrins from glycogen, a-glucan phosphorylases were assumed to be involved in glycogen degradation, forming a-glucose 1-phosphate from glycogen and from maltodextrins. We show here that C. glutamicum in fact possesses two a-glucan phosphorylases, which act as a glycogen phosphorylase (GlgP) and as a maltodextrin phosphorylase (MalP). By chromosomal inactivation and subsequent analysis of the mutant, cg1479 was identified as the malP gene. The deletion mutant C. glutamicum DmalP completely lacked MalP activity and showed reduced intracellular glycogen degradation, confirming the proposed pathway for glycogen degradation in C. glutamicum via GlgP, GlgX and MalP. Surprisingly, the DmalP mutant showed impaired growth, reduced viability and altered cell morphology on maltose and accumulated much higher concentrations of glycogen and maltodextrins than the wild-type during growth on this substrate, suggesting an additional role of MalP in maltose metabolism of C. glutamicum. Further assessment of enzyme activities revealed the presence of 4-a-glucanotransferase (MalQ), glucokinase (Glk) and a-phosphoglucomutase (a-Pgm), and the absence of maltose hydrolase, maltose phosphorylase and b-Pgm, all three known to be involved in maltose utilization by Gram-positive bacteria. Based on these findings, we conclude that C. glutamicum metabolizes maltose via a pathway involving maltodextrin and glucose formation by MalQ, glucose phosphorylation by Glk and maltodextrin degradation via the reactions of MalP and a-Pgm, a pathway hitherto known to be present in Gram-negative rather than in Gram-positive bacteria. INTRODUCTIONCorynebacterium glutamicum is a Gram-positive soil bacterium employed in the production of various amino acids (Eggeling & Bott, 2005), and serves as a model organism for the mycolic acid-containing suborder Corynebacterianeae, which includes pathogenic species such as Corynebacterium diphtheriae, Mycobacterium tuberculosis and Mycobacterium leprae. The organism grows on a variety of mono-and disaccharides, alcohols and organic acids as single or combined sources of carbon and energy (Liebl, 2005). and transiently forms intracellular glycogen when cultivated on sugar substrates (Tzvetkov et al., 2003;. We recently showed that C. glutamicum forms maltodextrins in the course of glycogen degradation , and thus we speculate that glycogen is degraded in C. glutamicum by a pathway which proceeds similarly or identically to the one present in Escherichia coli. This pathway involves the interplay of six enzymes (Fig. 1). Glycogen phosphorylase (GlgP) cleaves a-1,4-glycosidic bonds at the non-reducing ends of glycogen and forms glucose 1-phosphate and phosphorylase-limited dextrins (pl-dextrins) (Dauvillee et al., 2005;Alonso-Casajus et al., 2006). Cleavage of the a-1,6-glycosidic bon...

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“…2). These results therefore suggest that E. faecalis transports and phosphorylates the smallest maltodextrin mainly via the PTS permease MalT, which has previously been shown to transport and phosphorylate maltose (6,7). Indeed, a mutant deleted for mdxF, which encodes one of the transmembrane components of the ABC transporter, exhibited a growth rate on maltotriose similar to that of the wild-type strain (compare Fig.…”

Section: Resultsmentioning

confidence: 66%

Enterococcus faecalis Uses a Phosphotransferase System Permease and a Host Colonization-Related ABC Transporter for Maltodextrin Uptake

et al. 2017

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Maltodextrin is a mixture of maltooligosaccharides, which are produced by the degradation of starch or glycogen. They are mostly composed of ␣-1,4-and some ␣-1,6-linked glucose residues. Genes presumed to code for the Enterococcus faecalis maltodextrin transporter were induced during enterococcal infection. We therefore carried out a detailed study of maltodextrin transport in this organism. Depending on their length (3 to 7 glucose residues), E. faecalis takes up maltodextrins either via MalT, a maltose-specific permease of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS), or the ATP binding cassette (ABC) transporter MdxEFG-MsmX. Maltotriose, the smallest maltodextrin, is primarily transported by the PTS permease. A malT mutant therefore exhibits significantly reduced growth on maltose and maltotriose. The residual uptake of the trisaccharide is catalyzed by the ABC transporter, because a malT mdxF double mutant no longer grows on maltotriose. The trisaccharide arrives as maltotriose-6Љ-P in the cell. MapP, which dephosphorylates maltose-6=-P, also releases P i from maltotriose-6Љ-P. Maltotetraose and longer maltodextrins are mainly (or exclusively) taken up via the ABC transporter, because inactivation of the membrane protein MdxF prevents growth on maltotetraose and longer maltodextrins up to at least maltoheptaose. E. faecalis also utilizes panose and isopanose, and we show for the first time, to our knowledge, that in contrast to maltotriose, its two isomers are primarily transported via the ABC transporter. We confirm that maltodextrin utilization via MdxEFG-MsmX affects the colonization capacity of E. faecalis, because inactivation of mdxF significantly reduced enterococcal colonization and/or survival in kidneys and liver of mice after intraperitoneal infection. IMPORTANCE Infections by enterococci, which are major health care-associated pathogens, are difficult to treat due to their increasing resistance to clinically relevant antibiotics, and new strategies are urgently needed. A largely unexplored aspect is how these pathogens proliferate and which substrates they use in order to grow inside infected hosts. The use of maltodextrins as a source of carbon and energy was studied in Enterococcus faecalis and linked to its virulence. Our results demonstrate that E. faecalis can efficiently use glycogen degradation products. We show here that depending on the length of the maltodextrins, one of two different

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Maltose utilization in Enterococcus faecalis

Cited by 35 publications

References 37 publications

Comparison of OG1RF and an IsogenicfsrBDeletion Mutant by Transcriptional Analysis: the Fsr System ofEnterococcus faecalisIs More than the Activator of Gelatinase and Serine Protease

Comparison of OG1RF and an IsogenicfsrBDeletion Mutant by Transcriptional Analysis: the Fsr System ofEnterococcus faecalisIs More than the Activator of Gelatinase and Serine Protease

Roles of maltodextrin and glycogen phosphorylases in maltose utilization and glycogen metabolism in Corynebacterium glutamicum

Enterococcus faecalis Uses a Phosphotransferase System Permease and a Host Colonization-Related ABC Transporter for Maltodextrin Uptake

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