Evidence map›Paper›PMID 22155816›Full record

ArticleAntimicrobial agents and chemotherapy2012

Identification, characterization, and recombinant expression of epidermicin NI01, a novel unmodified bacteriocin produced by Staphylococcus epidermidis that displays potent activity against Staphylococci.

Stephanie Sandiford, Mathew Upton

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
7.8field-weighted citation impact, top 3% 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

63 citing papers in PubMed, 129 citations in OpenAlex.

  1. Review
  2. Probing theRSC chemical biology · 2026
    Article
  3. Article
  4. Epidermicin NI01 demonstrates potentJAC-antimicrobial resistance · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Complete genome sequence ofMicrobiology resource announcements · 2025
    Article
  11. Review
  12. Article
  13. Ursoricin, a bacteriocin ofApplied and environmental microbiology · 2024
    Article
  14. Article
  15. Towards sustainable antimicrobial therapies forSustainable microbiology · 2024
    Review
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review

3 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

2 authors at 1 institution in 1 country.

Stephanie SandifordDepartment of Medical Microbiology, School of Medicine, University of Manchester, Oxford Road, Manchester, United Kingdom.
Mathew Upton
University of Manchester · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We describe the discovery, purification, characterization, and expression of an antimicrobial peptide, epidermicin NI01, which is an unmodified bacteriocin produced by Staphylococcus epidermidis strain 224. It is a highly cationic, hydrophobic, plasmid-encoded peptide that exhibits potent antimicrobial activity toward a wide range of pathogenic Gram-positive bacteria including methicillin-resistant Staphylococcus aureus (MRSA), enterococci, and biofilm-forming S. epidermidis strains. Purification of the peptide was achieved using a combination of hydrophobic interaction, cation exchange, and high-performance liquid chromatography (HPLC). Matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis yielded a molecular mass of 6,074 Da, and partial sequence data of the peptide were elucidated using a combination of tandem mass spectrometry (MS/MS) and de novo sequencing. The draft genome sequence of the producing strain was obtained using 454 pyrosequencing technology, thus enabling the identification of the structural gene using the de novo peptide sequence data previously obtained. Epidermicin NI01 contains 51 residues with four tryptophan and nine lysine residues, and the sequence showed approximately 50% identity to peptides lacticin Z, lacticin Q, and aureocin A53, all of which belong to a new family of unmodified type II-like bacteriocins. The peptide is active in the nanomolar range against S. epidermidis, MRSA isolates, and vancomycin-resistant enterococci. Other unique features displayed by epidermicin include a high degree of protease stability and the ability to retain antimicrobial activity over a pH range of 2 to 10, and exposure to the peptide does not result in development of resistance in susceptible isolates. In this study we also show the structural gene alone can be cloned into Escherichia coli strain BL21(DE3), and expression yields active peptide.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacteriocinsChromatography, High Pressure LiquidDrug DiscoveryEnterococcusEscherichia coliHumansMethicillin-Resistant Staphylococcus aureusMolecular Sequence DataMolecular WeightPlasmidsProtein StabilityRecombinant ProteinsSequence Analysis, DNAAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacteriocinsepidermicin NI01, Staphylococcus epidermidisRecombinant Proteins

Identifiers

PMID22155816
PMCPMC3294953
OpenAlexW2135560567

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.