Evidence map›Paper›PMID 30770741›Full record

ArticleBMC biotechnology2019

A new prokaryotic expression vector for the expression of antimicrobial peptide abaecin using SUMO fusion tag.

Da Sol Kim, Seon Woong Kim, Jae Min Song, Soon Young Kim, Kwang-Chul Kwon

Open access · goldAbstract read
In one paragraph

Article in BMC biotechnology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

20 citing papers in PubMed, 68 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Extracellular production of Ulp1Applied microbiology and biotechnology · 2022
    Article
  13. Article
  14. Frontiers in bioengineering and biotechnology · 2022
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. AP-64, Encoded byBiomolecules · 2021
    Article
  20. Article
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 3 institutions in 2 countries.

Da Sol KimDepartment of Biological Sciences, Andong National University, Andong, South Korea.
Seon Woong KimDepartment of Biological Sciences, Andong National University, Andong, South Korea.
Jae Min SongDepartment of Global Medical Science, Health & Wellness College, Sungshin University, Seoul, South Korea.
Soon Young KimDepartment of Biological Sciences, Andong National University, Andong, South Korea. kimsy@anu.ac.kr.
Kwang-Chul KwonMicroSynbiotiX Ltd, 11011 N Torrey Pines Rd Ste. #135, La Jolla, CA, 92037, USA. kwang-chul.kwon@microsynbiotix.com.ORCID 0000-0002-4037-1776
Gyeongguk National University · KROracle (United States) · USSungshin Women's University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundDespite the growing demand for antimicrobial peptides (AMPs) for clinical use as an alternative approach against antibiotic-resistant bacteria, the manufacture of AMPs relies on expensive, small-scale chemical methods. The small ubiquitin-related modifier (SUMO) tag is industrially practical for increasing the yield of recombinant proteins by increasing solubility and preventing degradation in expression systems.

resultsA new vector system, pKSEC1, was designed to produce AMPs, which can work in prokaryotic systems such as Escherichia coli and plant chloroplasts. 6xHis was tagged to SUMO for purification of SUMO-fused AMPs. Abaecin, a 34-aa-long antimicrobial peptide from honeybees, was expressed in a fusion form to 6xHis-SUMO in a new vector system to evaluate the prokaryotic expression platform of the antimicrobial peptides. The fusion sequences were codon-optimized in three different combinations and expressed in E. coli. The combination of the native SUMO sequence with codon-optimized abaecin showed the highest expression level among the three combinations, and most of the expressed fusion proteins were detected in soluble fractions. Cleavage of the SUMO tag by sumoase produced a 29-aa-long abaecin derivative with a C-terminal deletion. However, this abaecin derivative still retained the binding sequence for its target protein, DnaK. Antibacterial activity of the 29-aa long abaecin was tested against Bacillus subtilis alone or in combination with cecropin B. The combined treatment of the abaecin derivative and cecropin B showed bacteriolytic activity 2 to 3 times greater than that of abaecin alone.

conclusionsUsing a SUMO-tag with an appropriate codon-optimization strategy could be an approach for the production of antimicrobial peptides in E.coli without affecting the viability of the host cell.

Indexed as

Gene ExpressionAnti-Infective AgentsAntimicrobial Cationic PeptidesBacillus subtilisCodonEscherichia coliGenetic VectorsInsect ProteinsRecombinant Fusion ProteinsSmall Ubiquitin-Related Modifier Proteinsabaecin protein, Apis melliferaAnti-Infective AgentsAntimicrobial Cationic PeptidesCodonInsect ProteinsRecombinant Fusion ProteinsSmall Ubiquitin-Related Modifier ProteinsAbaecinAntimicrobial peptideCodon optimizationEscherichia coliSmall ubiquitin-related modifier (SUMO)

Identifiers

PMID30770741
PMCPMC6377777
OpenAlexW2912007564

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.