Evidence map›Paper›PMID 29024643›Full record

ArticleCell host & microbe2017

GBPs Inhibit Motility of Shigella flexneri but Are Targeted for Degradation by the Bacterial Ubiquitin Ligase IpaH9.8.

Michal P Wandel, Claudio Pathe, Emma I Werner, Cara J Ellison, Keith B Boyle, Alexander von der Malsburg, John Rohde, Felix Randow

Open access · hybridAbstract read
In one paragraph

Article in Cell host & microbe, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
13.6field-weighted citation impact, top 1% 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

121 citing papers in PubMed, 192 citations in OpenAlex.

  1. Review
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  11. Proceedings of the National Academy of Sciences of the United States of America · 2026
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  16. TheeLife · 2025
    Article
  17. Article
  18. Review
  19. Review
  20. Article

61 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Michal P WandelMRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Claudio PatheMRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Emma I WernerMRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Cara J EllisonMRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Keith B BoyleMRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Alexander von der MalsburgMRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK.
John RohdeDepartment of Microbiology and Immunology, Dalhousie University Halifax, Halifax, NS B3H 4R2, Canada.
Felix RandowMRC Laboratory of Molecular Biology, Division of Protein and Nucleic Acid Chemistry, Francis Crick Avenue, Cambridge CB2 0QH, UK; University of Cambridge, Department of Medicine, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK. Electronic address: randow@mrc-lmb.cam.ac.uk.
MRC Laboratory of Molecular Biology · GBDalhousie University · CA

Funding

Medical Research Council MC_U105170648MRF_ MRF-104-0004-S-PATHEWellcome Trust
6 · The paper itself

Abstract

Interferon exposure boosts cell-autonomous immunity for more efficient pathogen control. But how interferon-enhanced immunity protects the cytosol against bacteria and how professionally cytosol-dwelling bacteria avoid clearance are insufficiently understood. Here we demonstrate that the interferon-induced GTPase family of guanylate-binding proteins (GBPs) coats Shigella flexneri in a hierarchical manner reliant on GBP1. GBPs inhibit actin-dependent motility and cell-to-cell spread of bacteria but are antagonized by IpaH9.8, a bacterial ubiquitin ligase secreted into the host cytosol. IpaH9.8 ubiquitylates GBP1, GBP2, and GBP4 to cause the proteasome-dependent destruction of existing GBP coats. This ubiquitin coating of Shigella favors the pathogen as it liberates bacteria from GBP encapsulation to resume actin-mediated motility and cell-to-cell spread. We conclude that an important function of GBP recruitment to S. flexneri is to prevent the spread of infection to neighboring cells while IpaH9.8 helps bacterial propagation by counteracting GBP-dependent cell-autonomous immunity.

Indexed as

Antigens, BacterialBacterial ProteinsCytosolGTP-Binding ProteinsHEK293 CellsHeLa CellsHost-Pathogen InteractionsHumansImmunity, CellularImmunity, InnateInterferonsProteolysisShigella flexneriTHP-1 CellsUbiquitin-Protein LigasesAntigens, BacterialBacterial ProteinsGTP-Binding ProteinsInterferonsUbiquitin-Protein Ligasescell-autonomous immunityE3 ubiquitin ligaseeffector proteinsGBPhost-pathogen interactioninnate immunityIpa9.8ubiquitinubiquitin coat

Identifiers

PMID29024643
PMCPMC5644667
OpenAlexW2763785504

What OpenQuestion holds

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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.