Evidence map›Paper›PMID 22396551›Full record

ArticleThe Journal of biological chemistry2012

Macin family of antimicrobial proteins combines antimicrobial and nerve repair activities.

Sascha Jung, Frank D Sönnichsen, Chien-Wen Hung, Andreas Tholey, Céline Boidin-Wichlacz, Wiebke Haeusgen, Christoph Gelhaus, Christine Desel, Rainer Podschun, Vicki Waetzig and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-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

24 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Role of Antimicrobial Peptides in Immunity of Parasitic Leeches.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2023
    Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Worms' Antimicrobial Peptides.Marine drugs · 2019
    Review
  17. Article
  18. Article
  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

13 authors at 4 institutions in 2 countries.

Sascha JungInstitute of Biochemistry, Zoophysiology, Christian Albrechts University of Kiel, Olshausenstrasse 40, 24098 Kiel, Germany.
Frank D Sönnichsen
Chien-Wen Hung
Andreas Tholey
Céline Boidin-Wichlacz
Wiebke Haeusgen
Christoph Gelhaus
Christine Desel
Rainer Podschun
Vicki Waetzig
Aurélie Tasiemski
Matthias Leippe
Joachim Grötzinger
Kiel University · DEUniversité de Lille · FRUniversity of Lübeck · DEUniversity Hospital Schleswig-Holstein · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tertiary structures of theromacin and neuromacin confirmed the macin protein family as a self-contained family of antimicrobial proteins within the superfamily of scorpion toxin-like proteins. The macins, which also comprise hydramacin-1, are antimicrobially active against Gram-positive and Gram-negative bacteria. Despite high sequence identity, the three proteins showed distinct differences with respect to their biological activity. Neuromacin exhibited a significantly stronger capacity to permeabilize the cytoplasmic membrane of Bacillus megaterium than theromacin and hydramacin-1. Accordingly, it is the only macin that displays pore-forming activity and that was potently active against Staphylococcus aureus. Moreover, neuromacin and hydramacin-1 led to an aggregation of bacterial cells that was not observed with theromacin. Analysis of the molecular surface properties of macins allowed confirmation of the barnacle model as the mechanistic model for the aggregation effect. Besides being antimicrobially active, neuromacin and theromacin, in contrast to hydramacin-1, were able to enhance the repair of leech nerves ex vivo. Notably, all three macins enhanced the viability of murine neuroblastoma cells, extending their functional characteristics. As neuromacin appears to be both a functional and structural chimera of hydramacin-1 and theromacin, the putative structural correlate responsible for the nerve repair capacity in leech was located to a cluster of six amino acid residues using the sequence similarity of surface-exposed regions.

Indexed as

Amino Acid SequenceAnimalsAntimicrobial Cationic PeptidesBase SequenceCloning, MolecularDisulfidesHumansLeechesMagnetic Resonance SpectroscopyMolecular Sequence DataNeuronsProtein ConformationProtein Structure, TertiarySaltsScattering, RadiationSequence Homology, Amino AcidAntimicrobial Cationic PeptidesDisulfideshydramacin-1, Hydra magnipapillataSaltstheromacin, leech

Identifiers

PMID22396551
PMCPMC3340141
OpenAlexW2079987814

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.