Evidence map›Paper›PMID 26338197›Full record

ArticleMicrobial cell factories2015

The identification of a novel Sulfolobus islandicus CAMP-like peptide points to archaeal microorganisms as cell factories for the production of antimicrobial molecules.

Eugenio Notomista, Annarita Falanga, Salvatore Fusco, Luciano Pirone, Anna Zanfardino, Stefania Galdiero, Mario Varcamonti, Emilia Pedone, Patrizia Contursi

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
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  9. Antifungal peptides from living organisms.Frontiers in microbiology · 2024
    Review
  10. Review
  11. A Comparative Analysis ofInternational journal of molecular sciences · 2022
    Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Biotechnology of extremely thermophilic archaea.FEMS microbiology reviews · 2018
    Review
  19. 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

9 authors at 2 institutions in 1 country.

Eugenio NotomistaDipartimento di Biologia, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, 80126, Naples, Italy. notomist@unina.it.
Annarita FalangaIstituto di Biostrutture Bioimmagini, CNR, 80134, Naples, Italy. annarita.falanga@unina.it.
Salvatore FuscoDipartimento di Biologia, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, 80126, Naples, Italy. salvatore.fusco@unina.it.
Luciano PironeIstituto di Biostrutture Bioimmagini, CNR, 80134, Naples, Italy. luciano.pirone@unina.it.
Anna ZanfardinoDipartimento di Biologia, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, 80126, Naples, Italy. anna.zanfardino@unina.it.
Stefania GaldieroIstituto di Biostrutture Bioimmagini, CNR, 80134, Naples, Italy. stefania.galdiero@unina.it.
Mario VarcamontiDipartimento di Biologia, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, 80126, Naples, Italy. varcamon@unina.it.
Emilia PedoneIstituto di Biostrutture Bioimmagini, CNR, 80134, Naples, Italy. empedone@unina.it.
Patrizia ContursiDipartimento di Biologia, Università degli Studi di Napoli Federico II, Complesso Universitario Monte S. Angelo, Via Cinthia, 80126, Naples, Italy. contursi@unina.it.
University of Naples Federico II · ITInstitute of Biostructure and Bioimaging · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPathogenic bacteria easily develop resistance to c onventional antibiotics so that even relatively new molecules are quickly losing efficacy. This strongly encourages the quest of new antimicrobials especially for the treatment of chronic infections. Cationic antimicrobial peptides (CAMPs) are small positively charged peptides with an amphipathic structure, active against Gram-positive and Gram-negative bacteria, fungi, as well as protozoa.

resultsA novel (CAMP)-like peptide (VLL-28) was identified in the primary structure of a transcription factor, Stf76, encoded by pSSVx, a hybrid plasmid-virus from the archaeon Sulfolobus islandicus. VLL-28 displays chemical, physical and functional properties typical of CAMPs. Indeed, it has a broad-spectrum antibacterial activity and acquires a defined structure in the presence of membrane mimetics. Furthermore, it exhibits selective leakage and fusogenic capability on vesicles with a lipid composition similar to that of bacterial membranes. VLL-28 localizes not only on the cell membrane but also in the cytoplasm of Escherichia coli and retains the ability to bind nucleic acids. These findings suggest that this CAMP-like peptide could exert its antimicrobial activity both on membrane and intra cellular targets.

conclusionsVLL-28 is the first CAMP-like peptide identified in the archaeal kingdom, thus pointing to archaeal microorganisms as cell factories to produce antimicrobial molecules of biotechnological interest. Furthermore, results from this work show that DNA/RNA-binding proteins could be used as sources of CAMPs.

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesArchaeal ProteinsCyclic AMPDrug Resistance, BacterialEscherichia coliMicrobial Sensitivity TestsModels, MolecularNuclear Magnetic Resonance, BiomolecularSulfolobusAnti-Bacterial AgentsAntimicrobial Cationic PeptidesArchaeal ProteinsCyclic AMP

Identifiers

PMID26338197
PMCPMC4559164
OpenAlexW1810204907

What OpenQuestion holds

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LicenceCC BY
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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.