Evidence map›Paper›PMID 28468662›Full record

ArticleMicrobial cell factories2017

Heterologous expression of abaecin peptide from Apis mellifera in Pichia pastoris.

Denis Prudencio Luiz, Juliana Franco Almeida, Luiz Ricardo Goulart, Nilson Nicolau-Junior, Carlos Ueira-Vieira

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
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  5. Review
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  8. Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields.Frontiers in cellular and infection microbiology · 2021
    Review
  9. A eukaryotic expression strategy for producing the novel antimicrobial peptide PRW4.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020
    Article
  10. Article
  11. Article
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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

5 authors at 1 institution in 1 country.

Denis Prudencio LuizGenetics Laboratory, Institute of Genetics and Biochemistry, Federal University of Uberlândia, 1720 Pará, Uberlândia, MG, 38400902, Brazil. prudenis@yahoo.com.br.
Juliana Franco AlmeidaNanobiotechnology Laboratory, Institute of Genetics and Biochemistry, Federal University of Uberlândia, 1720 Pará, Uberlândia, MG, 38400902, Brazil.
Luiz Ricardo GoulartNanobiotechnology Laboratory, Institute of Genetics and Biochemistry, Federal University of Uberlândia, 1720 Pará, Uberlândia, MG, 38400902, Brazil.
Nilson Nicolau-JuniorGenetics Laboratory, Institute of Genetics and Biochemistry, Federal University of Uberlândia, 1720 Pará, Uberlândia, MG, 38400902, Brazil.
Carlos Ueira-VieiraGenetics Laboratory, Institute of Genetics and Biochemistry, Federal University of Uberlândia, 1720 Pará, Uberlândia, MG, 38400902, Brazil.
Universidade Federal de Uberlândia · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAntimicrobial peptides (AMPs) are the first line of host immune defense against pathogens. Among AMPs from the honeybee Apis mellifera, abaecin is a major broad-spectrum antibacterial proline-enriched cationic peptide.

resultsFor heterologous expression of abaecin in Pichia pastoris, we designed an ORF with HisTag, and the codon usage was optimized. The gene was chemically synthetized and cloned in the pUC57 vector. The new ORF was sub-cloned in the pPIC9 expression vector and transformed into P. pastoris. After selection of positive clones, the expression was induced by methanol. The supernatant was analyzed at different times to determine the optimal time for the recombinant peptide expression. As a proof-of-concept, Escherichia coli was co-incubated with the recombinant peptide to verify its antimicrobial potential. DISCUSSION: Briefly, the recombinant Abaecin (rAbaecin) has efficiently decreased E. coli growth (P < 0.05) through an in vitro assay, and may be considered as a novel therapeutic agent that may complement other conventional antibiotic therapies.

Indexed as

Gene ExpressionAnimalsAntimicrobial Cationic PeptidesBeesCloning, MolecularEscherichia coliGenetic EngineeringInsect ProteinsPichiaRecombinant Fusion Proteinsabaecin protein, Apis melliferaAntimicrobial Cationic PeptidesInsect ProteinsRecombinant Fusion ProteinsAbaecinApis melliferaHeterologous expressionPichia pastorisProline-rich antimicrobial peptide

Identifiers

PMID28468662
PMCPMC5414229
OpenAlexW2611801669

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.