Two Closely Related ABC Transporters in
            <i>Streptococcus mutans</i>
            Are Involved in Disaccharide and/or Oligosaccharide Uptake

Webb, Alexander J.; Homer, Karen A.; Hosie, Arthur H.F.

doi:10.1128/jb.01509-07

Cited by 77 publications

(87 citation statements)

References 41 publications

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“…including antibiotic resistance, nutrient acquisition, adhesion, protein secretion, environmental sensing, spore formation, conjugation, and growth under stress conditions (39). As a consequence, many ABC transporters have been shown by signature-tagged mutagenesis (STM) screens to be important for the virulence of a range of bacterial pathogens, including Yersinia spp., Staphylococcus aureus, and Streptococcus pneumoniae (9,15,22,26), and these data have been supported by publications on the functions of individual ABC transporters (6,7,38,45).…”

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confidence: 49%

Screening of Streptococcus pneumoniae ABC Transporter Mutants Demonstrates that LivJHMGF, a Branched-Chain Amino Acid ABC Transporter, Is Necessary for Disease Pathogenesis

et al. 2009

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Bacterial ABC transporters are an important class of transmembrane transporters that have a wide variety of substrates and are important for the virulence of several bacterial pathogens, including Streptococcus pneumoniae. However, many S. pneumoniae ABC transporters have yet to be investigated for their role in virulence. Using insertional duplication mutagenesis mutants, we investigated the effects on virulence and in vitro growth of disruption of 9 S. pneumoniae ABC transporters. Several were partially attenuated in virulence compared to the wild-type parental strain in mouse models of infection. For one ABC transporter, required for full virulence and termed LivJHMGF due to its similarity to branched-chain amino acid (BCAA) transporters, a deletion mutant (⌬livHMGF) was constructed to investigate its phenotype in more detail. When tested by competitive infection, the ⌬livHMGF strain had reduced virulence in models of both pneumonia and septicemia but was fully virulent when tested using noncompetitive experiments. The ⌬livHMGF strain had no detectable growth defect in defined or complete laboratory media. Recombinant LivJ, the substrate binding component of the LivJHMGF, was shown by both radioactive binding experiments and tryptophan fluorescence spectroscopy to specifically bind to leucine, isoleucine, and valine, confirming that the LivJHMGF substrates are BCAAs. These data demonstrate a previously unsuspected role for BCAA transport during infection for S. pneumoniae and provide more evidence that functioning ABC transporters are required for the full virulence of bacterial pathogens.

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confidence: 49%

Screening of Streptococcus pneumoniae ABC Transporter Mutants Demonstrates that LivJHMGF, a Branched-Chain Amino Acid ABC Transporter, Is Necessary for Disease Pathogenesis

et al. 2009

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“…In Streptococcus mutans, the MsmEFGK system transports raffinose, melibiose, and stachyose, and the MalXFGK transporter is specific for maltodextrins (32). The two ATPase domains, MsmK and MalX, were shown to interact with either transporter system to energize uptake (32). In B. subtilis it was previously shown that MsmX energizes MdxEFG, a transporter specific for maltodextrins, as the cognate ABC domain (27).…”

Section: Discussionmentioning

confidence: 99%

“…MsiK energizes the cellobiose, xylobiose, and maltose uptake systems in Streptomyces lividans (9,26), the trehalose uptake system in Streptomyces reticuli (25), and the N,NЈ-diacetylchitobiose uptake in Streptomyces coelicolor (21). In Streptococcus mutans, the MsmEFGK system transports raffinose, melibiose, and stachyose, and the MalXFGK transporter is specific for maltodextrins (32). The two ATPase domains, MsmK and MalX, were shown to interact with either transporter system to energize uptake (32).…”

Section: Discussionmentioning

confidence: 99%

A Multitask ATPase Serving Different ABC-Type Sugar Importers in Bacillus subtilis

Ferreira

Sá‐Nogueira

2010

J Bacteriol

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Bacillus subtilis is able to utilize arabinopolysaccharides derived from plant biomass. Here, by combining genetic and physiological analyses we characterize the AraNPQ importer and identify primary and secondary transporters of B. subtilis involved in the uptake of arabinosaccharides. We show that the ABC-type importer AraNPQ is involved in the uptake of ␣-1,5-arabinooligosaccharides, at least up to four L-arabinosyl units. Although this system is the key transporter for ␣-1,5-arabinotriose and ␣-1,5-arabinotetraose, the results indicate that ␣-1,5-arabinobiose also is translocated by the secondary transporter AraE. This broad-specificity proton symporter is the major transporter for arabinose and also is accountable for the uptake of xylose and galactose. In addition, MsmX is shown to be the ATPase that energizes the incomplete AraNPQ importer. Furthermore, the results suggest the existence of at least one more unidentified MsmX-dependent ABC importer responsible for the uptake of nonlinear ␣-1,2-and ␣-1,3-arabinooligosaccharides. This study assigns MsmX as a multipurpose B. subtilis ATPase required to energize different saccharide transporters, the arabinooligosaccharide-specific AraNPQ-MsmX system, a putative MsmX-dependent ABC transporter specific for nonlinear arabinooligosaccharides, and the previously characterized maltodextrin-specific MdxEFGMsmX system.

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“…However, as the substrates are diverse in the types of monomer, bonding (␣-or ␤-glycosidic bonds), and degree of polymerization (disaccharides, trisaccharides, and probably oligosaccharides from the breakdown of starch and glycogen), the latter scenario is less possible. Indeed, the interactions of ATPase subunits with different membrane permeases to form individual ABC transporters were observed with Gram-positive bacteria (42)(43)(44).…”

Section: Resultsmentioning

confidence: 99%

Mechanistic Study of Utilization of Water-Insoluble Saccharomyces cerevisiae Glucans by Bifidobacterium breve Strain JCM1192

Keung

Sham

et al. 2017

Appl Environ Microbiol

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Bifidobacteria exert beneficial effects on hosts and are extensively used as probiotics. However, due to the genetic inaccessibility of these bacteria, little is known about their mechanisms of carbohydrate utilization and regulation. Bifidobacterium breve strain JCM1192 can grow on water-insoluble yeast (Saccharomyces cerevisiae) cell wall glucans (YCWG), which were recently considered as potential prebiotics. According to the results of 1 H nuclear magnetic resonance (NMR) spectrometry, the YCWG were composed of highly branched (1¡3,1¡6)-␤-glucans and (1¡4,1¡6)-␣-glucans. Although the YCWG were composed of 78.3% ␤-glucans and 21.7% ␣-glucans, only ␣-glucans were consumed by the B. breve strain. The ABC transporter (malEFG1) and pullulanase (aapA) genes were transcriptionally upregulated in the metabolism of insoluble yeast glucans, suggesting their potential involvement in the process. A nonsense mutation identified in the gene encoding an ABC transporter ATP-binding protein (MalK) led to growth failure of an ethyl methanesulfonate-generated mutant with yeast glucans. Coculture of the wild-type strain and the mutant showed that this protein was responsible for the import of yeast glucans or their breakdown products, rather than the export of ␣-glucancatabolizing enzymes. Further characterization of the carbohydrate utilization of the mutant and three of its revertants indicated that this mutation was pleiotropic: the mutant could not grow with maltose, glycogen, dextrin, raffinose, cellobiose, melibiose, or turanose. We propose that insoluble yeast ␣-glucans are hydrolyzed by extracellular pullulanase into maltose and/or maltooligosaccharides, which are then transported into the cell by the ABC transport system composed of MalEFG1 and MalK. The mechanism elucidated here will facilitate the development of B. breve and water-insoluble yeast glucans as novel synbiotics.IMPORTANCE In general, Bifidobacterium strains are genetically intractable. Coupling classic forward genetics with next-generation sequencing, here we identified an ABC transporter ATP-binding protein (MalK) responsible for the import of insoluble yeast glucan breakdown products by B. breve JCM1192. We demonstrated the pleiotropic effects of the ABC transporter ATP-binding protein in maltose/maltooligosaccharide, raffinose, cellobiose, melibiose, and turanose transport. With the addition of transcriptional analysis, we propose that insoluble yeast glucans are broken down by extracellular pullulanase into maltose and/or maltooligosaccharides, which are then transported into the cell by the ABC transport system composed of MalEFG1 and MalK. The mechanism elucidated here will facilitate the development of B. breve and water-insoluble yeast glucans as novel synbiotics.

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Two Closely Related ABC Transporters in Streptococcus mutans Are Involved in Disaccharide and/or Oligosaccharide Uptake

Cited by 77 publications

References 41 publications

Screening of Streptococcus pneumoniae ABC Transporter Mutants Demonstrates that LivJHMGF, a Branched-Chain Amino Acid ABC Transporter, Is Necessary for Disease Pathogenesis

Screening of Streptococcus pneumoniae ABC Transporter Mutants Demonstrates that LivJHMGF, a Branched-Chain Amino Acid ABC Transporter, Is Necessary for Disease Pathogenesis

A Multitask ATPase Serving Different ABC-Type Sugar Importers in Bacillus subtilis

Mechanistic Study of Utilization of Water-Insoluble Saccharomyces cerevisiae Glucans by Bifidobacterium breve Strain JCM1192

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