Evidence map›Paper›PMID 22164243›Full record

ArticlePloS one2011

Identification of lactoferricin B intracellular targets using an Escherichia coli proteome chip.

Yu-Hsuan Tu, Yu-Hsuan Ho, Ying-Chih Chuang, Po-Chung Chen, Chien-Sheng Chen

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
0.9field-weighted citation impact, top 29% 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

22 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Testing Antimicrobial Properties of Human Lactoferrin-Derived Fragments.International journal of molecular sciences · 2023
    Article
  3. Article
  4. Review
  5. Article
  6. Fungicidal Activity of Recombinant Javanicin againstMolecules (Basel, Switzerland) · 2021
    Article
  7. Article
  8. Systematic Identification of Protein Targets of Sub5 UsingInternational journal of molecular sciences · 2021
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Intracellular Targeting Mechanisms by Antimicrobial Peptides.Antimicrobial agents and chemotherapy · 2017
    Review
  15. Article
  16. Article
  17. The Anticancer Peptide TAT-RasGAPFrontiers in microbiology · 2017
    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

5 authors at 2 institutions in 1 country.

Yu-Hsuan TuGraduate Institute of Systems Biology and Bioinformatics, National Central University, Jhongli City, Taiwan.
Yu-Hsuan Ho
Ying-Chih Chuang
Po-Chung Chen
Chien-Sheng Chen
National Central University · TWNational Taiwan Ocean University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactoferricin B (LfcinB) is a well-known antimicrobial peptide. Several studies have indicated that it can inhibit bacteria by affecting intracellular activities, but the intracellular targets of this antimicrobial peptide have not been identified. Therefore, we used E. coli proteome chips to identify the intracellular target proteins of LfcinB in a high-throughput manner. We probed LfcinB with E. coli proteome chips and further conducted normalization and Gene Ontology (GO) analyses. The results of the GO analyses showed that the identified proteins were associated with metabolic processes. Moreover, we validated the interactions between LfcinB and chip assay-identified proteins with fluorescence polarization (FP) assays. Sixteen proteins were identified, and an E. coli interaction database (EcID) analysis revealed that the majority of the proteins that interact with these 16 proteins affected the tricarboxylic acid (TCA) cycle. Knockout assays were conducted to further validate the FP assay results. These results showed that phosphoenolpyruvate carboxylase was a target of LfcinB, indicating that one of its mechanisms of action may be associated with pyruvate metabolism. Thus, we used pyruvate assays to conduct an in vivo validation of the relationship between LfcinB and pyruvate level in E. coli. These results showed that E. coli exposed to LfcinB had abnormal pyruvate amounts, indicating that LfcinB caused an accumulation of pyruvate. In conclusion, this study successfully revealed the intracellular targets of LfcinB using an E. coli proteome chip approach.

Indexed as

Anti-Infective AgentsAntimicrobial Cationic PeptidesBiotinBiotinylationCitric Acid CycleComputational BiologyEscherichia coliEscherichia coli ProteinsLactoferrinMicrobial Sensitivity TestsMicroscopy, FluorescenceModels, BiologicalPeptidesProtein Array AnalysisProteomeProteomicsAnti-Infective AgentsAntimicrobial Cationic PeptidesBiotinEscherichia coli Proteinslactoferricin BLactoferrinPeptidesProteomePyruvic Acid

Identifiers

PMID22164243
PMCPMC3229523
OpenAlexW1992198169

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.