Evidence map›Paper›PMID 32510692›Full record

ArticleThe EMBO journal2020

Direct binding of polymeric GBP1 to LPS disrupts bacterial cell envelope functions.

Miriam Kutsch, Linda Sistemich, Cammie F Lesser, Marcia B Goldberg, Christian Herrmann, Jörn Coers

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

103 citing papers in PubMed, 177 citations in OpenAlex.

  1. Review
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  6. An overview of human inflammasomes: Activation and regulation.Journal of immunology (Baltimore, Md. : 1950) · 2026
    Review
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  12. Review
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  14. TheeLife · 2025
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

43 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

6 authors at 3 institutions in 2 countries.

Miriam KutschDepartment of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC, USA.ORCID 0000-0002-9346-2196
Linda SistemichDepartment of Physical Chemistry I, Ruhr-University Bochum, Bochum, Germany.
Cammie F LesserDivision of Infectious Diseases, Center for Bacterial Pathogenesis, Massachusetts General Hospital, Boston, MA, USA.
Marcia B GoldbergDivision of Infectious Diseases, Center for Bacterial Pathogenesis, Massachusetts General Hospital, Boston, MA, USA.
Christian HerrmannDepartment of Physical Chemistry I, Ruhr-University Bochum, Bochum, Germany.
Jörn CoersDepartment of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, NC, USA.ORCID 0000-0001-8707-4608
Duke Medical Center · USHarvard University · USRuhr University Bochum · DE

Funding

Molecular signaling in Shigella disseminationR01AI081724 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI Marcia B Goldberg · 2010 to 2026
$7.1M
Interferon-inducible cell-autonomous immunity to cytosolic bacterial pathogensR01AI139425 · NIAID · DUKE UNIVERSITY · PI Jorn Coers · 2019 to 2026
$3.4M
Human GBPs as regulators of immunity to intracellular bacterial pathogensR56AI139425 · NIAID · DUKE UNIVERSITY · PI COERS, JOERN · 2018 to 2018
$465k
Molecular signaling in Shigella disseminationR56AI081724 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI GOLDBERG, MARCIA B · 2009 to 2009
$189k
Burroughs Wellcome Fund (BWF)Deutsche Forschungsgemeinschaft (DFG) 427472513Deutsche Forschungsgemeinschaft (DFG) HE2679/6-1Harvard Medical SchoolHHS | National Institutes of Health (NIH) AI081724HHS | National Institutes of Health (NIH) AI139425HHS | National Institutes of Health (NIH) AI28360NIAID NIH HHS R01 AI081724NIAID NIH HHS R01 AI139425NIAID NIH HHS R56 AI081724NIAID NIH HHS R56 AI139425
6 · The paper itself

Abstract

In the outer membrane of gram-negative bacteria, O-antigen segments of lipopolysaccharide (LPS) form a chemomechanical barrier, whereas lipid A moieties anchor LPS molecules. Upon infection, human guanylate binding protein-1 (hGBP1) colocalizes with intracellular gram-negative bacterial pathogens, facilitates bacterial killing, promotes activation of the lipid A sensor caspase-4, and blocks actin-driven dissemination of the enteric pathogen Shigella. The underlying molecular mechanism for hGBP1's diverse antimicrobial functions is unknown. Here, we demonstrate that hGBP1 binds directly to LPS and induces "detergent-like" LPS clustering through protein polymerization. Binding of polymerizing hGBP1 to the bacterial surface disrupts the O-antigen barrier, thereby unmasking lipid A, eliciting caspase-4 recruitment, enhancing antibacterial activity of polymyxin B, and blocking the function of the Shigella outer membrane actin motility factor IcsA. These findings characterize hGBP1 as an LPS-binding surfactant that destabilizes the rigidity of the outer membrane to exert pleiotropic effects on the functionality of gram-negative bacterial cell envelopes.

Indexed as

Bacterial ProteinsCell MembraneGTP-Binding ProteinsHumansLipid AO AntigensProtein BindingShigellaBacterial ProteinsGBP1 protein, humanGTP-Binding ProteinsLipid AO Antigensactin-based motilitygram-negativeguanylate binding proteinslipopolysaccharideO-antigen

Identifiers

PMID32510692
PMCPMC7327485
OpenAlexW3033854583

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.