Evidence map›Paper›PMID 15917539›Full record

ArticleAntimicrobial agents and chemotherapy2005

Proline conformation-dependent antimicrobial activity of a proline-rich histone h1 N-terminal Peptide fragment isolated from the skin mucus of Atlantic salmon.

Torben Lüders, Gunn Alice Birkemo, Jon Nissen-Meyer, Øivind Andersen, Ingolf F Nes

Abstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.7field-weighted citation impact, top 19% 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

31 citing papers in PubMed, 99 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Fish Epidermal Mucus as a Source of Diverse Therapeutical Compounds.International journal of peptide research and therapeutics · 2023
    Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Dietary Inclusion of Black Soldier Fly (Frontiers in immunology · 2021
    Article
  14. Article
  15. Article
  16. Investigations of the Copper Peptide Hepcidin-25 by LC-MS/MS and NMR.International journal of molecular sciences · 2018
    Article
  17. Epidermal mucus, a major determinant in fish health: a review.Iranian journal of veterinary research · 2018
    Review
  18. Linker Histone in Diseases.International journal of biological sciences · 2017
    Review
  19. Article
  20. Review
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.

Torben LüdersLaboratory of Microbial Gene Technology, Department of Chemistry, Biotechnology, and Food Science, Norwegian University of Life Sciences, POB 5003, N-1432 As, Norway.
Gunn Alice Birkemo
Jon Nissen-Meyer
Øivind Andersen
Ingolf F Nes
Norwegian University of Life Sciences · NOUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A 30-residue N-terminally acetylated peptide derived from the N-terminal part of histone H1 was identified as the dominant antimicrobial peptide in skin mucus from Atlantic salmon (Salmo salar). The peptide (termed salmon antimicrobial peptide [SAMP H1]) was purified to homogeneity by a combination of reversed-phase and cation-exchange chromatographies. By Edman degradation of the deacetylated peptide and by sequencing of the PCR-amplified DNA that encodes the peptide, the complete amino acid sequence was determined to be AEVAPAPAAAAPAKAPKKKAAAKPKKAGPS. The theoretical molecular weight of N-terminally acetylated SAMP H1 was calculated to be 2,836, which is the same as that determined by matrix-assisted laser desorption ionization mass spectrometry. The peptide was active against both gram-negative and -positive bacteria. The N-terminal acetyl group was not necessary for activity since deacetylation did not reduce the activity. A synthetic peptide whose sequence was identical to that of the isolated fragment was initially inactive but could be activated by binding it to a cation-exchange column. Treatment of the synthetic peptide when it was bound to the exchange column with peptidylproline cis-trans-isomerase increased the amount of active peptide, indicating that isomerization of the proline peptide bond(s) was necessary for activation of the synthetic peptide. Comparison of the active and inactive forms by circular dichroism and chromatographic analyses suggests that the active form, both the natural and the synthetic forms, is more structured, condensed, and rigid than the inactive form, which has a more nonstructured conformation. This work shows for the first time the importance of proline isomers in the activity of an antimicrobial peptide.

Indexed as

Amino Acid SequenceAnimalsAnti-Bacterial AgentsEscherichia coliHistonesMicrobial Sensitivity TestsMolecular Sequence DataMucusPeptide FragmentsPeptidylprolyl IsomeraseProlineProtein ConformationSalmo salarSequence Analysis, DNASkinAnti-Bacterial AgentsHistonesPeptide FragmentsPeptidylprolyl IsomeraseProline

Identifiers

PMID15917539
PMCPMC1140541
OpenAlexW2005757610

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.