Evidence map›Paper›PMID 20497336›Full record

ArticleMolecular microbiology2010

The molecular basis of glycogen breakdown and transport in Streptococcus pneumoniae.

D Wade Abbott, Melanie A Higgins, Susanne Hyrnuik, Benjamin Pluvinage, Alicia Lammerts van Bueren, Alisdair B Boraston

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
4.0field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 68 citations in OpenAlex.

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  11. Role ofFrontiers in cellular and infection microbiology · 2023
    Review
  12. Article
  13. Exogenous glycogen utilization effects the transcriptome and pathogenicity ofFrontiers in cellular and infection microbiology · 2022
    Article
  14. Article
  15. Two complementary α-fucosidases fromThe Journal of biological chemistry · 2019
    Article
  16. Biochemistry insights · 2019
    Article
  17. Article
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

D Wade AbbottBiochemistry and Microbiology, University of Victoria, PO Box 3055 STN CSC, Victoria, BC, Canada V8W 3P6.
Melanie A Higgins
Susanne Hyrnuik
Benjamin Pluvinage
Alicia Lammerts van Bueren
Alisdair B Boraston
University of Victoria · CAUniversity of York · GB

Funding

CIHR 86610
6 · The paper itself

Abstract

The genome of Streptococcus pneumoniae strains, as typified by the TIGR4 strain, contain several genes encoding proteins putatively involved in alpha-glucan degradation, modification and synthesis. The extracellular components comprise an ATP binding cassette-transporter with its solute binding protein, MalX, and the hydrolytic enzyme SpuA. We show that of the commonly occurring exogenous alpha-glucans, S. pneumoniae TIGR4 is only able to grow on glycogen in a MalX- and SpuA-dependent manner. SpuA is able to degrade glycogen into a ladder of alpha-1,4-glucooligosaccharides while the high-affinity interaction (K(a) approximately 10(6) M(-1)) of MalX with maltooligosaccharides plays a key role in promoting the selective uptake of the glycogen degradation products that are produced by SpuA. The X-ray crystallographic analyses of apo- and complexed MalX illuminate the protein's specificity for the degradation products of glycogen and its striking ability to recognize the helical structure of the ligand. Overall, the results of this work provide new structural and functional insight into streptococcal alpha-glucan metabolism while supplying biochemical support for the hypothesis that the substrate of the S. pneumoniaealpha-glucan metabolizing machinery is glycogen, which in a human host is abundant in lung epithelial cells, a common target for invasive S. pneumoniae.

Indexed as

Metabolic Networks and PathwaysBacterial ProteinsCrystallography, X-RayGlycogenMembrane Transport ProteinsModels, MolecularMultigene FamilyOligosaccharidesProtein Structure, TertiaryStreptococcus pneumoniaeBacterial ProteinsGlycogenmaltooligosaccharidesMalX protein, Streptococcus pneumoniaeMembrane Transport ProteinsOligosaccharides

Identifiers

PMID20497336
PMCPMC2911477
OpenAlexW1923166214

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.