Evidence map›Paper›PMID 26512888›Full record

ArticleeLife2015

Fucosylation and protein glycosylation create functional receptors for cholera toxin.

Amberlyn M Wands, Akiko Fujita, Janet E McCombs, Jakob Cervin, Benjamin Dedic, Andrea C Rodriguez, Nicole Nischan, Michelle R Bond, Marcel Mettlen, David C Trudgian and 9 more

Open access · goldAbstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.8field-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

64 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
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  9. Review
  10. The diverse landscape of AB5-type toxins.Engineering microbiology · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Review
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4 more citing papers are in PubMed but not listed here.

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

19 authors at 3 institutions in 3 countries.

Amberlyn M WandsDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Akiko FujitaDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Janet E McCombsDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Jakob CervinDepartment of Microbiology and Immunology, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden.ORCID http://orcid.org/0000-0002-3840-1008
Benjamin DedicDepartment of Biochemistry and Cell Biology, Institute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Andrea C RodriguezDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Nicole NischanDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Michelle R BondDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Marcel MettlenDepartment of Microbiology and Immunology, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden.
David C TrudgianDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Andrew LemoffDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Marianne Quiding-JärbrinkDepartment of Microbiology and Immunology, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden.
Bengt GustavssonDepartment of Surgery, University of Gothenburg, Gothenburg, Sweden.
Catharina SteentoftCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.
Henrik ClausenCopenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, Faculty of Health Sciences, University of Copenhagen, Copenhagen, Denmark.
Hamid MirzaeiDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.
Susann TenebergDepartment of Microbiology and Immunology, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden.
Ulf YrlidDepartment of Microbiology and Immunology, Institute of Biomedicine, University of Gothenburg, Gothenburg, Sweden.
Jennifer J KohlerDepartment of Biochemistry, University of Texas Southwestern Medical Center, Dallas, United States.ORCID http://orcid.org/0000-0001-5373-3329
The University of Texas Southwestern Medical Center · USUniversity of Gothenburg · SEUniversity of Copenhagen · DK

Funding

MECHANISMS OF DRUG ACTION AND DISPOSITIONT32GM007062 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MANGELSDORF, DAVID J · 1985 to 2020
$7.4M
The Clathrin Coated Vesicle CycleR01MH061345 · NIMH · UT SOUTHWESTERN MEDICAL CENTER · PI SCHMID, SANDRA L. · 2010 to 2019
$5.0M
Study of sialoside function using photocrosslinking sialic acidR01GM090271 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI KOHLER, JENNIFER J · 2009 to 2021
$4.4M
Discovery of novel cholera toxin receptorsR21AI094427 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI KOHLER, JENNIFER J · 2011 to 2012
$436k
Photocrosslinking characterization of heat-labile toxin glycoreceptorsF32AI100489 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI WANDS, AMBERLYN M · 2013 to 2014
$107k
NIAID NIH HHS F32 AI100489NIAID NIH HHS F32AI100489NIAID NIH HHS R21 AI094427NIAID NIH HHS R21AI094427NIGMS NIH HHS R01 GM090271NIGMS NIH HHS R01GM090271NIGMS NIH HHS T32 GM007062NIGMS NIH HHS T32GM007062NIMH NIH HHS R01 MH061345NIMH NIH HHS R01MH61345
6 · The paper itself

Abstract

Cholera toxin (CT) enters and intoxicates host cells after binding cell surface receptors using its B subunit (CTB). The ganglioside (glycolipid) GM1 is thought to be the sole CT receptor; however, the mechanism by which CTB binding to GM1 mediates internalization of CT remains enigmatic. Here we report that CTB binds cell surface glycoproteins. Relative contributions of gangliosides and glycoproteins to CTB binding depend on cell type, and CTB binds primarily to glycoproteins in colonic epithelial cell lines. Using a metabolically incorporated photocrosslinking sugar, we identified one CTB-binding glycoprotein and demonstrated that the glycan portion of the molecule, not the protein, provides the CTB interaction motif. We further show that fucosylated structures promote CTB entry into a colonic epithelial cell line and subsequent host cell intoxication. CTB-binding fucosylated glycoproteins are present in normal human intestinal epithelia and could play a role in cholera.

Indexed as

Protein Processing, Post-TranslationalCell LineCholera ToxinEpithelial CellsGlycosylationG(M1) GangliosideHumansMembrane ProteinsProtein BindingReceptors, Cell SurfaceCholera ToxinG(M1) GangliosideMembrane ProteinsReceptors, Cell Surfacebiochemistrycholeraendocytosisepithelial cellsglycolipids/gangliosidesglycoproteininfectious diseasemicrobiologynonetoxins

Identifiers

PMID26512888
PMCPMC4686427
OpenAlexW1885689715

What OpenQuestion holds

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Registered trials

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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.