ArticleMicrobial cell factories2015
Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins.
Article in Microbial cell factories, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 131 papers.
What it found
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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.
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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.
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Who cites it
131 citing papers in PubMed, 256 citations in OpenAlex.
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- Expanded iOn switch toolkit enables flexible clonal labeling and dynamic imaging in model and non-model animals.Communications biology · 2026Article
- The landscape of antibody production systems: recombinant expression for research, diagnostics and therapy.Frontiers in bioengineering and biotechnology · 2026Review
- Strategic selection of microbial cell factories for sustainable and application-specific terpenoid production.Frontiers in bioengineering and biotechnology · 2026Review
- Heterologous Caseins: The Role of Phosphorylation in Their Functionality and How to Achieve It.Biomolecules · 2025Review
- Streamlined production of immobilized D-psicose 3-epimerase via secretion in Pichia pastoris: a new paradigm for industrial D-psicose production.Microbial cell factories · 2025Article
- Modular assembly and immunological evaluation of a promising bioconjugate nanovaccine against Klebsiella pneumoniae O2 serotype.NPJ vaccines · 2025Article
- Strategy for the Construction of SARS-CoV-2 S and N Recombinant Proteins and Their Immunogenicity Evaluation.Biotech (Basel (Switzerland)) · 2025Article
- A VLP vaccine platform comprising the core protein of hepatitis B virus with N-terminal antigen capture.International journal of biological macromolecules · 2025Article
- Sensitization Potential of the Major Soybean Allergen Gly m 4 and Its Cross-Reactivity with the Birch Pollen Allergen Bet v 1.International journal of molecular sciences · 2025Article
- Bacterial membrane vesicles restore gut anaerobiosis.NPJ biofilms and microbiomes · 2025Article
- Exogenous bone sialoprotein improves extraction socket healing in Ibsp knockout and wild-type mice.Bone · 2025Article
- Evaluation of the immune effect of foot-and-mouth disease virus-like particles derived fromFrontiers in microbiology · 2025Article
71 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
13 authors at 7 institutions in 3 countries.
Funding
Abstract
backgroundLipopolysaccharide (LPS), also referred to as endotoxin, is the major constituent of the outer leaflet of the outer membrane of virtually all Gram-negative bacteria. The lipid A moiety, which anchors the LPS molecule to the outer membrane, acts as a potent agonist for Toll-like receptor 4/myeloid differentiation factor 2-mediated pro-inflammatory activity in mammals and, thus, represents the endotoxic principle of LPS. Recombinant proteins, commonly manufactured in Escherichia coli, are generally contaminated with endotoxin. Removal of bacterial endotoxin from recombinant therapeutic proteins is a challenging and expensive process that has been necessary to ensure the safety of the final product.
resultsAs an alternative strategy for common endotoxin removal methods, we have developed a series of E. coli strains that are able to grow and express recombinant proteins with the endotoxin precursor lipid IVA as the only LPS-related molecule in their outer membranes. Lipid IVA does not trigger an endotoxic response in humans typical of bacterial LPS chemotypes. Hence the engineered cells themselves, and the purified proteins expressed within these cells display extremely low endotoxin levels.
conclusionsThis paper describes the preparation and characterization of endotoxin-free E. coli strains, and demonstrates the direct production of recombinant proteins with negligible endotoxin contamination.
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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.