Evidence map›Paper›PMID 26574006›Full record

ArticleAntimicrobial agents and chemotherapy2016

Characterization of the Antimicrobial Peptide Penisin, a Class Ia Novel Lantibiotic from Paenibacillus sp. Strain A3.

Piyush Baindara, Vasvi Chaudhry, Garima Mittal, Luciano M Liao, Carolina O Matos, Neeraj Khatri, Octavio L Franco, Prabhu B Patil, Suresh Korpole

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.4field-weighted citation impact, top 5% 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

61 citing papers in PubMed, 113 citations in OpenAlex.

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1 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Piyush BaindaraCSIR Institute of Microbial Technology, Chandigarh, India.
Vasvi ChaudhryCSIR Institute of Microbial Technology, Chandigarh, India.
Garima MittalCSIR Institute of Microbial Technology, Chandigarh, India.
Luciano M LiaoInstitute of Chemistry, Federal University of Goiás, Goiânia, Brazil.
Carolina O MatosInstitute of Chemistry, Federal University of Goiás, Goiânia, Brazil.
Neeraj KhatriCSIR Institute of Microbial Technology, Chandigarh, India.
Octavio L FrancoCentro de Analises Proteomicas e Bioquimicas, Pós-graduacão em Ciências Genomicas e Biotecnologia, Brasília, Brazil S-Inova, Programa de Pós-Graduacão em Biotecnologia, Universidade Católica Dom Bosco, Campo Grande, Brazil.
Prabhu B PatilCSIR Institute of Microbial Technology, Chandigarh, India.
Suresh KorpoleCSIR Institute of Microbial Technology, Chandigarh, India suresh@imtech.res.in.
Institute of Microbial Technology · INUniversidade Federal de Goiás · BRUniversidade Católica Dom Bosco · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Attempts to isolate novel antimicrobial peptides from microbial sources have been on the rise recently, despite their low efficacy in therapeutic applications. Here, we report identification and characterization of a new efficient antimicrobial peptide from a bacterial strain designated A3 that exhibited highest identity with Paenibacillus ehimensis. Upon purification and subsequent molecular characterization of the antimicrobial peptide, referred to as penisin, we found the peptide to be a bacteriocin-like peptide. Consistent with these results, RAST analysis of the entire genome sequence revealed the presence of a lantibiotic gene cluster containing genes necessary for synthesis and maturation of a lantibiotic. While circular dichroism and one-dimension nuclear magnetic resonance experiments confirmed a random coil structure of the peptide, similar to other known lantibiotics, additional biochemical evidence suggests posttranslational modifications of the core peptide yield six thioether cross-links. The deduced amino acid sequence of the putative biosynthetic gene penA showed approximately 74% similarity with elgicin A and 50% similarity with the lantibiotic paenicidin A. Penisin effectively killed methicillin-resistant Staphylococcus aureus (MRSA) and did not exhibit hemolysis activity. Unlike other lantibiotics, it effectively inhibited the growth of Gram-negative bacteria. Furthermore, 80 mg/kg of body weight of penisin significantly reduced bacterial burden in a mouse thigh infection model and protected BALB/c mice in a bacteremia model entailing infection with Staphylococcus aureus MTCC 96, suggesting that it could be a promising new antimicrobial peptide.

Indexed as

Genome, BacterialProtein Processing, Post-TranslationalAmino Acid SequenceAnimalsAnti-Bacterial AgentsBacteriocinsGene ExpressionMethicillin-Resistant Staphylococcus aureusMiceMice, Inbred BALB CMolecular Sequence DataMultigene FamilyPaenibacillusProtein Structure, SecondarySequence AlignmentSequence Homology, Amino AcidAnti-Bacterial AgentsBacteriocinspaenicidin Apenisin protein, Paenibacillus

Identifiers

PMID26574006
PMCPMC4704198
OpenAlexW2259167470

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Registered trials

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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.