Evidence map›Paper›PMID 33721189›Full record

ArticleThe protein journal2021

Expression and Purification of a Recombinant Enterotoxin Protein Using Different E. coli Host Strains and Expression Vectors.

Hong Zhao, Yongping Xu, Xiaoyu Li, Gen Li, Haofei Zhao, Lili Wang

Abstract read
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In one paragraph

Article in The protein journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Effective Gene Expression Prediction and Optimization from Protein Sequences.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  3. Production of a new tetravalent vaccine targeting fimbriae and enterotoxin of enterotoxigenicCanadian journal of veterinary research = Revue canadienne de recherche veterinaire · 2024
    Article
  4. Article
  5. Tagging Recombinant Proteins to Enhance Solubility and Aid Purification.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  6. Whole Genome Sequencing and CRISPR/Cas9 Gene Editing of EnterotoxigenicInternational journal of molecular sciences · 2022
    Article
  7. MPEPE, a predictive approach to improve protein expression inComputational and structural biotechnology journal · 2022
    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

6 authors at 1 institution in 1 country.

Hong ZhaoSchool of Bioengineering, Dalian University of Technology, Dalian, 116024, China.
Yongping XuSchool of Bioengineering, Dalian University of Technology, Dalian, 116024, China.
Xiaoyu LiSchool of Bioengineering, Dalian University of Technology, Dalian, 116024, China.
Gen LiSchool of Bioengineering, Dalian University of Technology, Dalian, 116024, China.
Haofei ZhaoSchool of Bioengineering, Dalian University of Technology, Dalian, 116024, China.
Lili WangSchool of Bioengineering, Dalian University of Technology, Dalian, 116024, China. wanglili@dlut.edu.cn.ORCID 0000-0002-6621-404X
Dalian University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Infection by Enterotoxigenic Escherichia coli is a common cause of diarrhea in animals. The development of vaccines against enterotoxins can effectively control the infection. We have previously constructed a recombinant antigen SLS fused by STa, LTB and STb enterotoxin and it showed a high immunogenicity in mice. Herein, we evaluated the expression of SLS in three different E. coli cells with corresponding plasmids. SLS proteins expressed in E. coli BL21 (DE3) and Rosetta-gami B (DE3) were aggregated as inclusion bodies, and the proteins solubility were not obviously promoted in low temperature combined with adjustment of inducer concentration. In contrast, SLS protein with maltose-binding protein (MBP) yielded from TB1 (DE3) cells were partially soluble. After increasing the IPTG concentration in the medium up to 2 mM and incubating at 37 ℃ for 4 h, the soluble protein yield reached the highest level (4.533 mg/0.2 L culture), which was significantly higher than the expression of SLS protein in Rosetta-gami B (DE3) (P < 0.05). Therefore, the TB1-pMAL expression system can be used for mass extraction and purification of SLS antigen prior to measuring its immunogenicity in pregnant mammals.

Indexed as

EnterotoxinsEscherichia coliRecombinant Fusion ProteinsInclusion BodiesMaltose-Binding ProteinsPlasmidsSolubilityEnterotoxinsMaltose-Binding ProteinsRecombinant Fusion ProteinsInclusion bodiesMaltose‐binding protein (MBP)Protein expressionSoluble recombinant protein

Identifiers

PMID33721189
OpenAlexW3136441112

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.