Evidence map›Paper›PMID 28925387›Full record

ArticleCell research2017

A vital sugar code for ricin toxicity.

Jasmin Taubenschmid, Johannes Stadlmann, Markus Jost, Tove Irene Klokk, Cory D Rillahan, Andreas Leibbrandt, Karl Mechtler, James C Paulson, Julian Jude, Johannes Zuber and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Knockout of theZoological research · 2025
    Article
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  7. Article
  8. Article
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  12. Article
  13. Article
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  15. Nucleotide Sugar Transporter SLC35 Family Structure and Function.Computational and structural biotechnology journal · 2019
    Review
  16. Article
  17. Review
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

16 authors at 8 institutions in 4 countries.

Jasmin TaubenschmidIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, VBC - Vienna BioCenter Campus, Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
Johannes StadlmannIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, VBC - Vienna BioCenter Campus, Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
Markus JostUniversitätsklinikum Heidelberg, Zentrum für Kinder- und Jugendmedizin, Analysezentrum III, Klinik für Kinderheilkunde I, Im Neuenheimer Feld 669, 69120 Heidelberg, Germany.
Tove Irene KlokkDepartment of Molecular Cell Biology and Centre for Cancer Biomedicine, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Montebello, 0379 Oslo, Norway.
Cory D RillahanDepartments of Cell and Molecular Biology, Chemical Physiology, and Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.
Andreas LeibbrandtIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, VBC - Vienna BioCenter Campus, Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
Karl MechtlerIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, VBC - Vienna BioCenter Campus, Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
James C PaulsonDepartments of Cell and Molecular Biology, Chemical Physiology, and Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA.
Julian JudeInstitute of Molecular Pathology (IMP), Campus-Vienna-Biocenter 1, 1030 Vienna, Austria.
Johannes ZuberInstitute of Molecular Pathology (IMP), Campus-Vienna-Biocenter 1, 1030 Vienna, Austria.
Kirsten SandvigDepartment of Molecular Cell Biology and Centre for Cancer Biomedicine, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Montebello, 0379 Oslo, Norway.
Ulrich EllingIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, VBC - Vienna BioCenter Campus, Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
Thorsten MarquardtUniversitätsklinikum Münster, Klinik für Kinderheilkunde, Albert-Schweitzer-Campus 1, 48149 Münster, Germany.
Christian ThielUniversitätsklinikum Heidelberg, Zentrum für Kinder- und Jugendmedizin, Analysezentrum III, Klinik für Kinderheilkunde I, Im Neuenheimer Feld 669, 69120 Heidelberg, Germany.
Christian KoernerUniversitätsklinikum Heidelberg, Zentrum für Kinder- und Jugendmedizin, Analysezentrum III, Klinik für Kinderheilkunde I, Im Neuenheimer Feld 669, 69120 Heidelberg, Germany.
Josef M PenningerIMBA, Institute of Molecular Biotechnology of the Austrian Academy of Sciences, VBC - Vienna BioCenter Campus, Dr. Bohr-Gasse 3, 1030 Vienna, Austria.
Institute of Molecular Biotechnology · ATAustrian Academy of Sciences · ATNorwegian Cancer Society · NOScripps Research Institute · USUniversity Hospital Heidelberg · DEZentrum für Kinderheilkunde · DEResearch Institute of Molecular Pathology · ATVienna Biocenter · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ricin is one of the most feared bioweapons in the world due to its extreme toxicity and easy access. Since no antidote exists, it is of paramount importance to identify the pathways underlying ricin toxicity. Here, we demonstrate that the Golgi GDP-fucose transporter Slc35c1 and fucosyltransferase Fut9 are key regulators of ricin toxicity. Genetic and pharmacological inhibition of fucosylation renders diverse cell types resistant to ricin via deregulated intracellular trafficking. Importantly, cells from a patient with SLC35C1 deficiency are also resistant to ricin. Mechanistically, we confirm that reduced fucosylation leads to increased sialylation of Lewis X structures and thus masking of ricin-binding sites. Inactivation of the sialyltransferase responsible for modifications of Lewis X (St3Gal4) increases the sensitivity of cells to ricin, whereas its overexpression renders cells more resistant to the toxin. Thus, we have provided unprecedented insights into an evolutionary conserved modular sugar code that can be manipulated to control ricin toxicity.

Indexed as

AnimalsFucosyltransferasesGene DeletionGolgi ApparatusHumansMembrane Transport ProteinsMiceMonosaccharide Transport ProteinsMutationRicinSialyltransferasesfucosyltransferase 9, mouseFucosyltransferaseshaematoside synthetaseMembrane Transport ProteinsMonosaccharide Transport ProteinsRicinSialyltransferasesSLC35C1 protein, humanSlc35c1 protein, mouse

Identifiers

PMID28925387
PMCPMC5674155
OpenAlexW2755198856

What OpenQuestion holds

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LicenceCC BY
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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.