Evidence map›Paper›PMID 28983718›Full record

ReviewCurrent genetics2018

Pediocin-like bacteriocins: new perspectives on mechanism of action and immunity.

Natalia S Ríos Colombo, Miriam C Chalón, Silvia A Navarro, Augusto Bellomio

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Current genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
9.6field-weighted citation impact, top 2% 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

43 citing papers in PubMed, 111 citations in OpenAlex.

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  15. Natural Antimicrobials forMicroorganisms · 2023
    Review
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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

4 authors at 1 institution in 1 country.

Natalia S Ríos ColomboInstituto Superior de Investigaciones Biológicas (INSIBIO, CONICET-UNT) and Instituto de Química Biológica "Dr. Bernabé Bloj", Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán, Chacabuco 461, T4000ILI, San Miguel de Tucumán, Argentina.
Miriam C ChalónInstituto Superior de Investigaciones Biológicas (INSIBIO, CONICET-UNT) and Instituto de Química Biológica "Dr. Bernabé Bloj", Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán, Chacabuco 461, T4000ILI, San Miguel de Tucumán, Argentina.
Silvia A NavarroInstituto Superior de Investigaciones Biológicas (INSIBIO, CONICET-UNT) and Instituto de Química Biológica "Dr. Bernabé Bloj", Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán, Chacabuco 461, T4000ILI, San Miguel de Tucumán, Argentina.
Augusto BellomioInstituto Superior de Investigaciones Biológicas (INSIBIO, CONICET-UNT) and Instituto de Química Biológica "Dr. Bernabé Bloj", Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán, Chacabuco 461, T4000ILI, San Miguel de Tucumán, Argentina. augustobellomio@fbqf.unt.edu.ar.ORCID http://orcid.org/0000-0002-7215-862X
National University of Tucumán · AR

Funding

Agencia Nacional de Promoción Científica y Tecnológica (AR) PICT-2012-2998Consejo Nacional de Investigaciones Científicas y Técnicas PIP 06906 COConsejo Nacional de Investigaciones Científicas y Técnicas PIP112-201101-00779Universidad Nacional de Tucumán PIUNT D548/1
6 · The paper itself

Abstract

This review attempts to analyze the mechanism of action and immunity of class IIa bacteriocins. These peptides are promising alternative food preservatives and they have a great potential application in medical sciences. Class IIa bacteriocins act on the cytoplasmic membrane of Gram-positive cells dissipating the transmembrane electrical potential by forming pores. However, their toxicity and immunity mechanism remains elusive. Here we discuss the role of the mannose phosphotransferase system (man-PTS) as the receptor for class IIa bacteriocins and the influence of the membrane composition on the activity of these antimicrobial peptides. A model that is consistent with experimental results obtained by different researchers involves the non-specific binding of the bacteriocin to the negatively charged membrane of target bacteria. This step would facilitate a specific binding to the receptor protein, altering its functionality and forming an independent pore in which the bacteriocin is inserted in the membrane. An immunity protein could specifically recognize and block the pore. Bacteriocins function in bacterial ecosystems and energetic costs associated with their production are also discussed. Theoretical models based on solid experimental evidence are vital to understand bacteriocins mechanism of action and to promote new technological developments.

Indexed as

Anti-Bacterial AgentsBacteriocinsFood PreservationHumansImmunityModels, TheoreticalPediocinsPeptidesAnti-Bacterial AgentsBacteriocinsPediocinsPeptidesBacteriocinImmunity proteinMan-PTSMechanism of actionMembrane

Identifiers

PMID28983718
OpenAlexW2761886164

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.