Evidence map›Paper›PMID 23468636›Full record

ArticlePLoS pathogens2013

Structural determinants for activity and specificity of the bacterial toxin LlpA.

Maarten G K Ghequire, Abel Garcia-Pino, Eline K M Lebbe, Stijn Spaepen, Remy Loris, René De Mot

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
5.5field-weighted citation impact, top 5% 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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Antimicrobial Weapons of Pseudomonas aeruginosa.Advances in experimental medicine and biology · 2022
    Article
  4. Article
  5. The B Subunit of PirABPathogens (Basel, Switzerland) · 2020
    Article
  6. Review
  7. Article
  8. Review
  9. Review
  10. Article
  11. Lectin-Like Bacteriocins.Frontiers in microbiology · 2018
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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 2 institutions in 1 country.

Maarten G K GhequireCentre of Microbial and Plant Genetics, University of Leuven, Heverlee-Leuven, Belgium.
Abel Garcia-Pino
Eline K M Lebbe
Stijn Spaepen
Remy Loris
René De Mot
KU Leuven · BEVrije Universiteit Brussel · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lectin-like bacteriotoxic proteins, identified in several plant-associated bacteria, are able to selectively kill closely related species, including several phytopathogens, such as Pseudomonas syringae and Xanthomonas species, but so far their mode of action remains unrevealed. The crystal structure of LlpABW, the prototype lectin-like bacteriocin from Pseudomonas putida, reveals an architecture of two monocot mannose-binding lectin (MMBL) domains and a C-terminal β-hairpin extension. The C-terminal MMBL domain (C-domain) adopts a fold very similar to MMBL domains from plant lectins and contains a binding site for mannose and oligomannosides. Mutational analysis indicates that an intact sugar-binding pocket in this domain is crucial for bactericidal activity. The N-terminal MMBL domain (N-domain) adopts the same fold but is structurally more divergent and lacks a functional mannose-binding site. Differential activity of engineered N/C-domain chimers derived from two LlpA homologues with different killing spectra, disclosed that the N-domain determines target specificity. Apparently this bacteriocin is assembled from two structurally similar domains that evolved separately towards dedicated functions in target recognition and bacteriotoxicity.

Indexed as

Anti-Bacterial AgentsBacterial ToxinsBacteriocinsCircular DichroismCrystallizationDNA, BacterialDNA Mutational AnalysisDNA, RecombinantMicrobial Sensitivity TestsProtein BindingProtein Structure, TertiaryPseudomonas putidaStructure-Activity RelationshipSubstrate SpecificityAnti-Bacterial AgentsBacterial ToxinsBacteriocinsDNA, BacterialDNA, Recombinant

Identifiers

PMID23468636
PMCPMC3585409
OpenAlexW1983206248

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.