Evidence map›Paper›PMID 38870903›Full record

ArticleCell host & microbe2024

Bacterial esterases reverse lipopolysaccharide ubiquitylation to block host immunity.

Magdalena Szczesna, Yizhou Huang, Rachel E Lacoursiere, Francesca Bonini, Vito Pol, Fulya Koc, Beatrice Ward, Paul P Geurink, Jonathan N Pruneda, Teresa L M Thurston

Abstract read
In one paragraph

Article in Cell host & microbe, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
–field-weighted citation impact
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

27 citing papers in PubMed.

  1. Article
  2. RNF213-dependent lytic destruction ofProceedings of the National Academy of Sciences of the United States of America · 2026
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  3. Article
  4. Review
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  6. Review
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  8. Article
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  11. TheeLife · 2025
    Article
  12. HoweLife · 2025
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  13. Article
  14. Article
  15. ThebioRxiv : the preprint server for biology · 2025
    Article
  16. mBio · 2025
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  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Magdalena SzczesnaDepartment of Infectious Disease, Centre for Bacterial Resistance Biology, Imperial College London, London SW7 2AZ, UK.
Yizhou HuangDepartment of Infectious Disease, Centre for Bacterial Resistance Biology, Imperial College London, London SW7 2AZ, UK.
Rachel E LacoursiereDepartment of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR 97239, USA.
Francesca BoniniDepartment of Infectious Disease, Centre for Bacterial Resistance Biology, Imperial College London, London SW7 2AZ, UK.
Vito PolDepartment of Cell and Chemical Biology, Leiden University Medical Centre, Leiden, the Netherlands.
Fulya KocDepartment of Infectious Disease, Centre for Bacterial Resistance Biology, Imperial College London, London SW7 2AZ, UK.
Beatrice WardDepartment of Infectious Disease, Centre for Bacterial Resistance Biology, Imperial College London, London SW7 2AZ, UK.
Paul P GeurinkDepartment of Cell and Chemical Biology, Leiden University Medical Centre, Leiden, the Netherlands.
Jonathan N PrunedaDepartment of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR 97239, USA. Electronic address: pruneda@ohsu.edu.
Teresa L M ThurstonDepartment of Infectious Disease, Centre for Bacterial Resistance Biology, Imperial College London, London SW7 2AZ, UK. Electronic address: t.thurston@imperial.ac.uk.

Funding

Exploiting bacterial effector proteins to study human ubiquitin signalingR35GM142486 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI Jonathan N Pruneda · 2021 to 2026
$2.6M
NIGMS NIH HHS R35 GM142486Wellcome Trust
6 · The paper itself

Abstract

Aspects of how Burkholderia escape the host's intrinsic immune response to replicate in the cell cytosol remain enigmatic. Here, we show that Burkholderia has evolved two mechanisms to block the activity of Ring finger protein 213 (RNF213)-mediated non-canonical ubiquitylation of bacterial lipopolysaccharide (LPS), thereby preventing the initiation of antibacterial autophagy. First, Burkholderia's polysaccharide capsule blocks RNF213 association with bacteria and second, the Burkholderia deubiquitylase (DUB), TssM, directly reverses the activity of RNF213 through a previously unrecognized esterase activity. Structural analysis provides insight into the molecular basis of TssM esterase activity, allowing it to be uncoupled from its isopeptidase function. Furthermore, a putative TssM homolog also displays esterase activity and removes ubiquitin from LPS, establishing this as a virulence mechanism. Of note, we also find that additional immune-evasion mechanisms exist, revealing that overcoming this arm of the host's immune response is critical to the pathogen.

Indexed as

Bacterial ProteinsBurkholderiaLipopolysaccharidesUbiquitinationAutophagyEsterasesHost-Pathogen InteractionsHumansImmune EvasionUbiquitin-Protein LigasesVirulenceBacterial ProteinsEsterasesLipopolysaccharidesUbiquitin-Protein LigasesAutophagybacterial effectorBurkholderiacell-autonomous immunitynon-canonical ubiquitylationRNF213TssMUbiquitin esterase

Identifiers

PMID38870903
PMCPMC11271751

What OpenQuestion holds

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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.