Evidence map›Paper›PMID 39815265›Full record

ReviewMicrobial cell factories2025

Recent advances in recombinant production of soluble proteins in E. coli.

Ario de Marco

Abstract readReview
In one paragraph

Review in Microbial cell factories, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Recombinant Protein Drugs: A 2025 Update.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  5. Article
  6. Article
  7. Article
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  10. Review
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  16. Review
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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

1 author.

Ario de MarcoLab of Environmental and Life Sciences, University of Nova Gorica, Vipavska cesta 13, Nova Gorica, 5000, Slovenia. ario.demarco@ung.si.ORCID http://orcid.org/0000-0001-7729-819X

Funding

HORIZON-MSCA-2023-SE-01-01 GAP-101182851Javne agencije za znanstveno-raziskovalno in inovacijsko dejavnost Republike Slovenije P3-0428, N4-0282, N4-0325 and J4-50144Loulou Foundation CDKL5-24-102-01
6 · The paper itself

Abstract

backgroundE. coli still remains the most commonly used organism to produce recombinant proteins in research labs. This condition is mirrored by the attention that researchers dedicate to understanding the biology behind protein expression, which is then exploited to improve the effectiveness of the technology. This effort is witnessed by an impressive number of publications, and this review aims to organize the most relevant novelties proposed in recent years.

resultsThe examined contributions address several of the known bottlenecks related to recombinant expression in E. coli, such as improved glycosylation pathways, more reliable production of proteins whose folding depends on the formation of disulfide bonds, the possibility of controlling and even benefiting from the formation of aggregates or the need to overcome the dependence of bacteria on antibiotics during bacterial culture. Nevertheless, the majority of the published papers aimed at identifying the conditions for optimal control of the translation process to achieve maximal yields of functional exogenous proteins.

conclusionsDespite community commitment, the critical question of what really is the metabolic burden and how it affects both host metabolism and recombinant protein production remains elusive because some experimental results are contradictory. This contribution aims to offer researchers a tool to orient themselves in this complexity. The new capacities offered by artificial intelligence tools could help clarifying this issue, but the training phase will probably require more systematic experimental approaches to collect sufficiently uniform data.

Indexed as

Escherichia coliRecombinant ProteinsGlycosylationProtein FoldingSolubilityRecombinant ProteinsDisulfide bondsGlycosylationIntrinsically disordered peptidespET plasmidsT7 RNA polymerase

Identifiers

PMID39815265
PMCPMC11736966

What OpenQuestion holds

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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.