Evidence map›Paper›PMID 23433070›Full record

ArticleMicrobial biotechnology2013

Saturation mutagenesis of selected residues of the α-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity.

Des Field, Evelyn M Molloy, Catalin Iancu, Lorraine A Draper, Paula M O' Connor, Paul D Cotter, Colin Hill, R Paul Ross

Abstract read
In one paragraph

Article in Microbial biotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

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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

8 authors.

Des FieldDepartment of Microbiology, University College Cork, Cork, Ireland.
Evelyn M Molloy
Catalin Iancu
Lorraine A Draper
Paula M O' Connor
Paul D Cotter
Colin Hill
R Paul Ross

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The lantibiotic lacticin 3147 consists of two ribosomally synthesized and post-translationally modified antimicrobial peptides, Ltnα and Ltnβ, which act synergistically against a wide range of Gram-positive microorganisms. We performed saturation mutagenesis of specific residues of Ltnα to determine their functional importance. The results establish that Ltnα is more tolerant to change than previously suggested by alanine scanning mutagenesis. One substitution, LtnαH23S, was identified which improved the specific activity of lacticin 3147 against one pathogenic strain, Staphylococcus aureus NCDO1499. This represents the first occasion upon which the activity of a two peptide lantibiotic has been enhanced through bioengineering.

Indexed as

Mutagenesis, Site-DirectedAmino Acid SequenceAmino Acid SubstitutionAnti-Infective AgentsBacteriocinsMicrobial Sensitivity TestsMolecular Sequence DataStaphylococcus aureusAnti-Infective AgentsBacteriocinslacticin 481

Identifiers

PMID23433070
PMCPMC3918158

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.