Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma.

Gilson, Éric; Alloing, Geneviève; Schmidt, Thomas; Claverys, Jean‐Pierre; Dudler, Robert; Hofnung, Maurice

doi:10.1002/j.1460-2075.1988.tb03284.x

Cited by 208 publications

(152 citation statements)

References 29 publications

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“…When considering the properties of the primary active uptake system for glutamate in C. glutamicum and its apparent similarity to binding-protein-dependent systems in Gramnegative bacteria, the very interesting findings of Gilson et al [27], which have recently been extended by Alloing et al [28], should be taken into account. These papers present convincing genetic evidence for the existence of a transport system similar to binding-protein-dependent mechanisms also in Gram-positive organisms on the basis of DNA sequence similarities, thereby confirming an hypothesis of Nielsen and Lampen [29] about the occurrence of such transport systems.…”

Section: Discussionmentioning

confidence: 99%

Uptake of glutamate in Corynebacterium glutamicum

Krämer

Lambert

1990

European Journal of Biochemistry

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The inducible glutamate uptake system in Corynebacterium glutamicum (Krämer, R., Lambert, C., Hoischen, C. & Ebbighausen, H., preceding paper in this journal) was characterized with respect to its mechanism and energy coupling. All possible secondary active uptake mechanisms can be excluded. Glutamate transport is not coupled to the translocation of H+, Na+ or K+ ions. Although changes in membrane potential and uptake activity cannot completely be separated, no correlation between these two parameters is observed. The uptake of glutamate resembles a primary active, ATP‐dependent transport mechanism in several respects. (a) The substrate affinity is very high (1.3 μM). (b) Accumulation of glutamate reaches values of greater than 2 · 105, at least as high as those reported for binding‐protein‐dependent systems in Gram‐negative bacteria. (c) The uptake is unidirectional. Even after complete deenergization, the accumulation ratio was not significantly reduced. (d) The rate of glutamate uptake is directly correlated to the cytosolic ATP content and also to the ATP/ADP ratio. This is shown by varying internal ATP by different procedures applying inhibitors (NaCN, dicyclohexyl carbodiimide), uncouplers (carbonyl m‐chlorophenylhydrazone), ionophores (valinomycin), and even by shifting the cells to anaerobiosis. Uptake is not promoted by cytosolic ATP levels below 1.5 mM, the maximum uptake rate is reached at 4–5 mM ATP.

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Section: Discussionmentioning

confidence: 99%

Uptake of glutamate in Corynebacterium glutamicum

Krämer

Lambert

1990

European Journal of Biochemistry

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“…It has turned out that Gram-positive species have the equivalent systems with binding proteins that are anchored to the membrane by a lipid group, which restricts diffusion to two dimensions (in the plane of the membrane) [76,77]. The sugar-binding protein MsmE of S. mutans has been shown to be attached to the membrane by means of an amino-terminal lipo-amino acid anchor ( Figs.…”

Section: Atp-driven Nutrient Uptake and Product/drug Excretionmentioning

confidence: 99%

Energy transduction in lactic acid bacteria

Poolman

1993

FEMS Microbiology Reviews

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In the discovery of some general principles of energy transduction, lactic acid bacteria have played an important role. In this review, the energy transducing processes of lactic acid bacteria are discussed with the emphasis on the major developments of the past 5 years. This work not only includes the biochemistry of the enzymes and the bioenergetics of the processes, but also the genetics of the genes encoding the energy transducing proteins. The progress in the area of carbohydrate transport and metabolism is presented first. Sugar translocation involving ATP-driven transport, ion-linked cotransport, heterologous exchange and group translocation are discussed. The coupling of precursor uptake to product product excretion and the linkage of antiport mechanisms to the deiminase pathways of lactic acid bacteria is dealt with in the second section. The third topic relates to metabolic energy conservation by ehemiosmotic processes. There is increasing evidence that precursor/product exchange in combination with precursor decarboxy[ation allows bacteria to generate additional metabolic energy. In the final section transport ot nutrients and ions as well as mechanisms to excrete undesirable (toxic) compounds from the cells are discussed.

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“…For example, a family of proteins found in many streptococci and staphylococci contains a protein motif, LPXTGE, which is the basis for covalent attachment to the cell wall (Fischetti et al, 1990;Schneewind et al, 1992). Another family of proteins contains an N-terminal LXXC motif, which is a signal sequence cleavage site as well as a covalent attachment site for palmitic acid of the bacterial membrane (Gilson et al, 1988). Pneumococci display an unusual surface constituent, phosphorylcholine, on the cell wall teichoic acid and the membranebound lipoteichoic acid (Mosser and Tomasz, 1970;Holtje and Tomasz, 1975;Tomasz et al, 1975).…”

Section: Introductionmentioning

confidence: 99%

Contribution of novel choline‐binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae

Rosenow

Ryan

Weiser

et al. 1997

Molecular Microbiology

437

465

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SummaryThe surface of Streptococcus pneumoniae is decorated with a family of choline-binding proteins (CBPs) that are non-covalently bound to the phosphorylcholine of the teichoic acid. Two examples (PspA, a protective antigen, and LytA, the major autolysin) have been well characterized. We identified additional CPBs and characterized a new CBP, CbpA, as an adhesin and a determinant of virulence. Using choline immobilized on a solid matrix, a mixture of proteins from a pspA-deficient strain of pneumococcus was eluted in a choline-dependent fashion. Antisera to these proteins passively protected mice challenged in the peritoneum with a lethal dose of pneumococci. The predominant component of this mixture, CbpA, is a 75-kDa surface-exposed protein that reacts with human convalescent antisera. The deduced sequence from the corresponding gene showed a chimeric architecture with a unique N-terminal region and a C-terminal domain consisting of 10 repeated choline-binding domains nearly identical to PspA. A cbpA-deficient mutant showed a >50% reduction in adherence to cytokine-activated human cells and failed to bind to immobilized sialic acid or lacto-N-neotetraose, known pneumococcal ligands on eukaryotic cells. Carriage of this mutant in an animal model of nasopharyngeal colonization was reduced 100-fold. There was no difference between the parent strain and this mutant in an intraperitoneal model of sepsis. These data for CbpA extend the important functions of the CBP family to bacterial adherence and identify a pneumococcal vaccine candidate.

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Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma.

Cited by 208 publications

References 29 publications

Uptake of glutamate in Corynebacterium glutamicum

Uptake of glutamate in Corynebacterium glutamicum

Energy transduction in lactic acid bacteria

Contribution of novel choline‐binding proteins to adherence, colonization and immunogenicity of Streptococcus pneumoniae

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