Evidence map›Paper›PMID 26191783›Full record

ArticleBiotechnology and bioengineering2016

Enterocin A mutants identified by saturation mutagenesis enhance potency towards vancomycin-resistant Enterococci.

Maria K McClintock, Yiannis N Kaznessis, Benjamin J Hackel

Open access · greenAbstract read
In one paragraph

Article in Biotechnology and bioengineering, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 20% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

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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

3 authors at 1 institution in 1 country.

Maria K McClintockDepartment of Chemical Engineering and Materials Science, University of Minnesota-Twin Cities, Minneapolis, Minnesota, 55455.
Yiannis N KaznessisDepartment of Chemical Engineering and Materials Science, University of Minnesota-Twin Cities, Minneapolis, Minnesota, 55455.
Benjamin J HackelDepartment of Chemical Engineering and Materials Science, University of Minnesota-Twin Cities, Minneapolis, Minnesota, 55455. hackel@umn.edu.
University of Minnesota · US

Funding

TRAINING FOR FUTURE BIOTECHNOLOGY DEVELOPMENTT32GM008347 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI SCHMIDT-DANNERT, CLAUDIA · 1990 to 2021
$11.0M
Lactic Acid Bacteria that Detect & Inhibit Enterococci in the Mammalian GI TractR01GM111358 · NIGMS · UNIVERSITY OF MINNESOTA · PI DUNNY, GARY M, KAZNESSIS, YIANNIS · 2014 to 2017
$1.4M
NIGMS NIH HHS GM008347NIGMS NIH HHS GM111358NIGMS NIH HHS R01 GM111358NIGMS NIH HHS T32 GM008347
6 · The paper itself

Abstract

Vancomycin-resistant Enterococci infections are a significant clinical problem. One proposed solution is to use probiotics, such as lactic acid bacteria, to produce antimicrobial peptides at the site of infection. Enterocin A, a class 2a bacteriocin, exhibits inhibitory activity against E. faecium and E. faecalis, which account for 86% of vancomycin-resistant Enterococci infections. In this study, we aimed to engineer enterocin A mutants with enhanced potency within a lactic acid bacterial production system. Peptide mutants resulting from saturation mutagenesis at sites A24 and T27 were efficiently screened in a 96-well plate assay for inhibition of pathogen growth. Several mutants exhibit increased potency relative to wild-type enterocin A in both liquid- and solid-medium growth assays. In particular, A24P and T27G exhibit enhanced inhibition of multiple strains of E. faecium and E. faecalis, including clinically isolated vancomycin-resistant strains. A24P and T27G enhance killing of E. faecium 8 by 13 ± 3- and 18 ± 4-fold, respectively. The engineered enterocin A/lactic acid bacteria systems offer significant potential to combat antibiotic-resistant infections.

Indexed as

MutagenesisBacteriocinsLactococcus lactisMicrobial Sensitivity TestsMicrobial ViabilityMutant ProteinsVancomycin-Resistant EnterococciBacteriocinsenterocin AMutant Proteinsantimicrobial peptideenterocin Alactic acid bacteriapeptide engineeringsaturation mutagenesis

Identifiers

PMID26191783
PMCPMC4820536
OpenAlexW2126360191

What OpenQuestion holds

Textmetadata
LicenceTDM
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.