Evidence map›Paper›PMID 30087409›Full record

ArticleScientific reports2018

The potency of the broad spectrum bacteriocin, bactofencin A, against staphylococci is highly dependent on primary structure, N-terminal charge and disulphide formation.

Paula M O' Connor, Eileen F O' Shea, Paul D Cotter, Colin Hill, R Paul Ross

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 37 citations in OpenAlex.

  1. Bacteriocins fromFrontiers in microbiology · 2026
    Review
  2. Lactic Acid Bacteria Bacteriocins: Safe and Effective Antimicrobial Agents.International journal of molecular sciences · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. A novel of new class II bacteriocin fromFrontiers in microbiology · 2022
    Article
  13. Review
  14. Review
  15. Frontiers in microbiology · 2021
    Review
  16. Potential of Cell-Free Supernatant fromPharmaceuticals (Basel, Switzerland) · 2020
    Article
  17. Journal of bacteriology · 2020
    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.

Paula M O' ConnorTeagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland.
Eileen F O' SheaTeagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland.
Paul D CotterTeagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland.ORCID 0000-0002-5465-9068
Colin HillAPC Microbiome Ireland, University College Cork, Cork, Ireland.
R Paul RossAPC Microbiome Ireland, University College Cork, Cork, Ireland. p.ross@ucc.ie.
Teagasc - The Irish Agriculture and Food Development Authority · IEUniversity College Cork · IE

Funding

Department of Agriculture, Food and the Marine 04/R&D/C/232Science Foundation Ireland (SFI) SFI/12/RC/2273
6 · The paper itself

Abstract

Bactofencin A is a novel class IId bacteriocin, produced by the intestinal isolate Lactobacillus salivarius DPC6502, which has potent activity against medically significant pathogens including Staphylococcus aureus. This bacteriocin is unusual in that it has a highly cationic N terminus and a single disulfide bond between Cys7 and Cys22, resulting in a large C terminal loop. In this study, a library of synthetic bactofencin A variants were screened against the mastitis isolate, S. aureus DPC5246, to identify key residues responsible for activity. It was apparent that substituting either cysteine of the disulfide bond with either serine or alanine significantly reduced the activity of the bacteriocin, confirming the importance of the C terminal loop. Substituting N terminal amino acids with alanine had no effect on activity, whereas sequential removal of the N terminal positively charged residues resulted in an increasingly inactive peptide. A complete (synthetic) alanine scanning analysis revealed that the residues between Val9 and Gly17 were most affected by substitution suggesting that this area has a major influence on the potency of the bacteriocin. Substituting residues in the loop region between Cys7 and Cys22 for D-amino acid equivalents had a more detrimental effect on activity than L-alanine substitutions. Specifically Y10A, N11A, P15A and T16A are active at 4, 16, 1 and 16 μM respectively while their D equivalents were inactive at 1000 μM, the highest concentration tested. Ultimately, this study identifies the critical features in the primary structure of the bacteriocin which gives it such potent activity against pathogenic staphylococci.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnti-Bacterial AgentsBacteriocinsCysteineDisulfidesDose-Response Relationship, DrugLigilactobacillus salivariusMicrobial Sensitivity TestsPeptidesStaphylococcus aureusAnti-Bacterial AgentsBacteriocinsCysteineDisulfidesPeptides

Identifiers

PMID30087409
PMCPMC6081437
OpenAlexW2887890204

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.