Evidence map›Paper›PMID 29528148›Full record

ArticleMolecular microbiology2018

SusE facilitates starch uptake independent of starch binding in B. thetaiotaomicron.

Matthew H Foley, Eric C Martens, Nicole M Koropatkin

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  4. Article
  5. Acarbose Impairs GutbioRxiv : the preprint server for biology · 2024
    Article
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  7. mBio · 2024
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  8. mSphere · 2024
    Article
  9. BoGH13ACellular and molecular life sciences : CMLS · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
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

3 authors at 1 institution in 1 country.

Matthew H FoleyDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Eric C MartensDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Nicole M KoropatkinDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109, USA.ORCID 0000-0002-2459-3336
University of Michigan · US

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
Assembly of a model glycan uptake system from a symbiotic human gut bacteriumR01GM118475 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI KOROPATKIN, NICOLE M · 2016 to 2020
$1.8M
NIGMS NIH HHS R01 GM118475NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

The Bacteroides thetaiotaomicron starch utilization system (Sus) is a model system for nutrient acquisition by gut Bacteroidetes, a dominant phylum of gut bacteria. The Sus includes SusCDEFG, which assemble on the cell surface to capture, degrade and import starch. While SusD is an essential starch-binding protein, the precise role(s) of the partially homologous starch-binding proteins SusE and SusF has remained elusive. We previously reported that a non-binding version of SusD (SusD*) supports growth on starch when other members of the multi-protein complex are present. Here we demonstrate that SusE supports SusD* growth on maltooligosaccharides, and determine the domains of SusE essential for this function. Furthermore, we demonstrate that SusE does not need to bind starch to support growth in the presence of SusD*, suggesting that the assembly of SusCDE is most important for maltooligosaccharide uptake in this context. However, starch binding by proteins SusDEF directs the uptake of maltooligosaccharides of specific lengths, suggesting that these proteins equip the cell to scavenge a range of starch fragments. These data demonstrate that the assembly of core Sus proteins SusCDE is secondary to their glycan binding roles, but glycan binding by Sus proteins may fine tune the selection of glycans from the environment.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsBacteroides thetaiotaomicronBinding SitesCarrier ProteinsCell MembraneGastrointestinal TractHumansOligosaccharidesPolysaccharidesRecombinant ProteinsStarchBacterial Outer Membrane ProteinsBacterial ProteinsCarrier ProteinsmaltooligosaccharidesOligosaccharidesPolysaccharidesRecombinant ProteinsStarch

Identifiers

PMID29528148
PMCPMC5980745
OpenAlexW2790489036

What OpenQuestion holds

Textmetadata
LicenceTDM
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.