Evidence map›Paper›PMID 30343895›Full record

ArticleCell2018

Bifunctional Immunity Proteins Protect Bacteria against FtsZ-Targeting ADP-Ribosylating Toxins.

See-Yeun Ting, Dustin E Bosch, Sarah M Mangiameli, Matthew C Radey, Shuo Huang, Young-Jun Park, Katherine A Kelly, Szymon Krzysztof Filip, Young Ah Goo, Jimmy K Eng and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
13.2field-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

89 citing papers in PubMed, 148 citations in OpenAlex.

  1. An endonuclease V protectsbioRxiv : the preprint server for biology · 2026
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  4. Review
  5. Article
  6. Article
  7. Transition-state analysis of the arginine-specific human ADP-ribosyltransferase 1.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Type VI Secretion Systems inMicroorganisms · 2026
    Article
  9. Review
  10. Article
  11. Article
  12. The SPI-6 T6SS gene cluster fromFrontiers in microbiology · 2026
    Article
  13. Article
  14. The SPI-20 and SPI-21 T6SS gene clusters fromFrontiers in microbiology · 2026
    Article
  15. Review
  16. Megaplasmids associate withbioRxiv : the preprint server for biology · 2025
    Article
  17. A nonenzymatic effector disruptsProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  18. Article
  19. Article
  20. Deciphering theJournal of bacteriology · 2025
    Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 4 institutions in 1 country.

See-Yeun TingDepartment of Microbiology, University of Washington School of Medicine, Seattle, WA 98195, USA.
Dustin E BoschDepartment of Pathology, University of Washington School of Medicine, Seattle, WA 98195, USA.
Sarah M MangiameliDepartment of Physics, University of Washington, Seattle, WA 98195, USA.
Matthew C RadeyDepartment of Microbiology, University of Washington School of Medicine, Seattle, WA 98195, USA.
Shuo HuangDepartment of Microbiology, University of Washington School of Medicine, Seattle, WA 98195, USA.
Young-Jun ParkDepartment of Biochemistry, University of Washington School of Medicine, Seattle, WA 98195, USA.
Katherine A KellyDepartment of Microbiology, University of Washington School of Medicine, Seattle, WA 98195, USA.
Szymon Krzysztof FilipProteomics Center of Excellence, Northwestern University, Chicago, IL 60611, USA.
Young Ah GooProteomics Center of Excellence, Northwestern University, Chicago, IL 60611, USA.
Jimmy K EngProteomics Resource, University of Washington, Seattle, WA 98195, USA.
Marc AllaireMolecular Biophysics and Integrated Bioimaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
David VeeslerDepartment of Biochemistry, University of Washington School of Medicine, Seattle, WA 98195, USA.
Paul A WigginsDepartment of Microbiology, University of Washington School of Medicine, Seattle, WA 98195, USA; Department of Physics, University of Washington, Seattle, WA 98195, USA; Department of Bioengineering, University of Washington, Seattle, WA 98195, USA.
S Brook PetersonDepartment of Microbiology, University of Washington School of Medicine, Seattle, WA 98195, USA.
Joseph D MougousDepartment of Microbiology, University of Washington School of Medicine, Seattle, WA 98195, USA; Department of Biochemistry, University of Washington School of Medicine, Seattle, WA 98195, USA; Howard Hughes Medical Institute, University of Washington, Seattle, WA 98195, USA. Electronic address: mougous@uw.edu.
University of Washington · USNorthwestern University · USHoward Hughes Medical Institute · USLawrence Berkeley National Laboratory · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LEONIDAS C. PLATANIAS · 1993 to 2026
$153.9M
TR&D 7: Cell Specific ProteomicsP41GM108569 · NIGMS · NORTHWESTERN UNIVERSITY · PI KELLEHER, NEIL L · 2015 to 2024
$13.6M
Type VI secretion effectors and interbacterial competition in vivoR01AI080609 · NIAID · YALE UNIVERSITY · PI MOUGOUS, JOSEPH DAVID · 2009 to 2025
$6.7M
Structural Studies of Coronavirus Fusion ProteinsR01GM120553 · NIGMS · UNIVERSITY OF WASHINGTON · PI VEESLER, DAVID · 2016 to 2020
$1.7M
Howard Hughes Medical InstituteNCI NIH HHS P30 CA060553NIAID NIH HHS R01 AI080609NIGMS NIH HHS P41 GM108569NIGMS NIH HHS R01 GM120553
6 · The paper itself

Abstract

ADP-ribosylation of proteins can profoundly impact their function and serves as an effective mechanism by which bacterial toxins impair eukaryotic cell processes. Here, we report the discovery that bacteria also employ ADP-ribosylating toxins against each other during interspecies competition. We demonstrate that one such toxin from Serratia proteamaculans interrupts the division of competing cells by modifying the essential bacterial tubulin-like protein, FtsZ, adjacent to its protomer interface, blocking its capacity to polymerize. The structure of the toxin in complex with its immunity determinant revealed two distinct modes of inhibition: active site occlusion and enzymatic removal of ADP-ribose modifications. We show that each is sufficient to support toxin immunity; however, the latter additionally provides unprecedented broad protection against non-cognate ADP-ribosylating effectors. Our findings reveal how an interbacterial arms race has produced a unique solution for safeguarding the integrity of bacterial cell division machinery against inactivating post-translational modifications.

Indexed as

Adenosine DiphosphateADP Ribose TransferasesADP-RibosylationAmino Acid SequenceBacterial ProteinsBacterial ToxinsCatalytic DomainCytoskeletal ProteinsEscherichia coliHumansMutagenesis, Site-DirectedN-Glycosyl HydrolasesProtein Structure, TertiaryProtein SubunitsSequence AlignmentSerratiaAdenosine DiphosphateADP Ribose TransferasesADP-ribosylarginine hydrolaseBacterial ProteinsBacterial ToxinsCytoskeletal ProteinsFtsZ protein, BacteriaN-Glycosyl HydrolasesProtein SubunitsADP-ribosylationbacterial communitiesEsx secretiontoxintype VI secretion

Identifiers

PMID30343895
PMCPMC6239978
OpenAlexW2896023929

What OpenQuestion holds

Textmetadata
LicenceTDM
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.