Evidence map›Paper›PMID 23878199›Full record

ArticleThe Journal of biological chemistry2013

Identification, structure, and function of a novel type VI secretion peptidoglycan glycoside hydrolase effector-immunity pair.

John C Whitney, Seemay Chou, Alistair B Russell, Jacob Biboy, Taylor E Gardiner, Michael A Ferrin, Mitchell Brittnacher, Waldemar Vollmer, Joseph D Mougous

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
8.8field-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

75 citing papers in PubMed, 142 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Type VI Secretion Systems inMicroorganisms · 2026
    Article
  5. Review
  6. Article
  7. Virulence regulation in the fish pathogenFrontiers in cellular and infection microbiology · 2026
    Review
  8. The SPI-20 and SPI-21 T6SS gene clusters fromFrontiers in microbiology · 2026
    Article
  9. The SPI-6 T6SS gene cluster fromFrontiers in microbiology · 2026
    Article
  10. A nonenzymatic effector disruptsProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  11. Deciphering theJournal of bacteriology · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Genomic analysis ofFrontiers in microbiology · 2024
    Article

15 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

9 authors at 2 institutions in 2 countries.

John C WhitneyFrom the Departments of Microbiology and.
Seemay Chou
Alistair B Russell
Jacob Biboy
Taylor E Gardiner
Michael A Ferrin
Mitchell Brittnacher
Waldemar Vollmer
Joseph D Mougous
Newcastle University · GBUniversity of Washington · US

Funding

Type VI secretion effectors and interbacterial competition in vivoR01AI080609 · NIAID · YALE UNIVERSITY · PI MOUGOUS, JOSEPH DAVID · 2009 to 2025
$6.7M
Biotechnology and Biological Sciences Research Council BB/I020012/1Howard Hughes Medical InstituteNIAID NIH HHS AI080609NIAID NIH HHS R01 AI080609
6 · The paper itself

Abstract

Bacteria employ type VI secretion systems (T6SSs) to facilitate interactions with prokaryotic and eukaryotic cells. Despite the widespread identification of T6SSs among Gram-negative bacteria, the number of experimentally validated substrate effector proteins mediating these interactions remains small. Here, employing an informatics approach, we define novel families of T6S peptidoglycan glycoside hydrolase effectors. Consistent with the known intercellular self-intoxication exhibited by the T6S pathway, we observe that each effector gene is located adjacent to a hypothetical open reading frame encoding a putative periplasmically localized immunity determinant. To validate our sequence-based approach, we functionally investigate a representative family member from the soil-dwelling bacterium Pseudomonas protegens. We demonstrate that this protein is secreted in a T6SS-dependent manner and that it confers a fitness advantage in growth competition assays with Pseudomonas putida. In addition, we determined the 1.4 Å x-ray crystal structure of this effector in complex with its cognate immunity protein. The structure reveals the effector shares highest overall structural similarity to a glycoside hydrolase family associated with peptidoglycan N-acetylglucosaminidase activity, suggesting that T6S peptidoglycan glycoside hydrolase effector families may comprise significant enzymatic diversity. Our structural analyses also demonstrate that self-intoxication is prevented by the immunity protein through direct occlusion of the effector active site. This work significantly expands our current understanding of T6S effector diversity.

Indexed as

Bacterial Secretion SystemsCalorimetryCatalytic DomainComputational BiologyCrystallography, X-RayEscherichia coliMicroscopy, Phase-ContrastMuramidaseN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanProtein ConformationProtein FoldingPseudomonasPseudomonas putidaBacterial Secretion SystemsMuramidaseN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanEffector-Immunity PairGlycoside HydrolasesInterbacterial InteractionsMicrobiologyPeptidoglycanProtein CrystallizationProtein SecretionType VI Secretion

Identifiers

PMID23878199
PMCPMC3772208
OpenAlexW2077545286

What OpenQuestion holds

Textmetadata
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.