ReviewFrontiers in microbiology2014
Fusion tags for protein solubility, purification and immunogenicity in Escherichia coli: the novel Fh8 system.
Review in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 171 papers, 2 of them syntheses that pooled it.
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Who cites it
171 citing papers in PubMed, 2 syntheses or guidelines pooled it, 443 citations in OpenAlex.
- Revolutionizing orthopedic healthcare: a systematic review unveiling recombinant antimicrobial peptides.Frontiers in microbiology · 2024Pooled it
- Recombinant expression of insoluble enzymes in Escherichia coli: a systematic review of experimental design and its manufacturing implications.Microbial cell factories · 2021Pooled it
- Engineering a heme-dependent tryptophan hydroxylase pathway inSynthetic and systems biotechnology · 2026Article
- A designed fusion tag improves soluble expression of nanobody inMagnetic resonance letters · 2026Article
- High-yield soluble expression and affinity-tag-free purification of growth hormone receptor antagonist B2036 in Escherichia coli.Bioprocess and biosystems engineering · 2026Article
- Efficient in vivo removal of solubility tag to improve the bacterial production of soluble, bioactive human IGF-1.World journal of microbiology & biotechnology · 2026Article
- A Simple Method to Produce Recombinant Mammalian Serum Albumins inInternational journal of molecular sciences · 2026Article
- Structure-guided optimization of SLY1 expression and purification in Escherichia coli.Protein science : a publication of the Protein Society · 2026Article
- Immunogenicity of anVaccines · 2026Article
- Engineering fusion enzymes for enhanced catalysis and stability: strategies and biotechnological applications.Molecular biology reports · 2026Review
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Production of Xylooligosaccharides (XOSs) with Anti-inflammatory and Prebiotic Activities Using Recombinant Endo-1,4-β-xylanases fromJournal of agricultural and food chemistry · 2026Article
- Challenges, optimization, and delivery strategies in the heterologous expression of aldehyde dehydrogenase: therapeutic applications for acetaldehyde detoxification.Biotechnology letters · 2026Review
- SmallTalk: a novel small-sized fusion tag for peptide expression and purification.FEBS open bio · 2026Article
- EstablishingBiodesign research · 2026Article
- Engineered Escherichia coli as a microbial cell factory for intracellular protein delivery: strains, vectors, mechanisms, and therapeutic applications.Microbial cell factories · 2026Review
- A Simplified Strategy for Nanobody Production and Use Based on Functional GST-Nanobody Fusion Proteins.Biomolecules · 2026Article
- Mechanism-guided control of intracellular alkalinization and process pH for production of recombinant human B-type natriuretic peptide under the cSAT scheme in Escherichia coli.Microbial cell factories · 2026Article
- Peptide and Protein Tags for the Half-Life Extension of Therapeutic Agents: A Review Article.The protein journal · 2026Review
- Cosolvent-induced spontaneous refolding of lipase.Applied microbiology and biotechnology · 2026Article
111 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins are now widely produced in diverse microbial cell factories. The Escherichia coli is still the dominant host for recombinant protein production but, as a bacterial cell, it also has its issues: the aggregation of foreign proteins into insoluble inclusion bodies is perhaps the main limiting factor of the E. coli expression system. Conversely, E. coli benefits of cost, ease of use and scale make it essential to design new approaches directed for improved recombinant protein production in this host cell. With the aid of genetic and protein engineering novel tailored-made strategies can be designed to suit user or process requirements. Gene fusion technology has been widely used for the improvement of soluble protein production and/or purification in E. coli, and for increasing peptide's immunogenicity as well. New fusion partners are constantly emerging and complementing the traditional solutions, as for instance, the Fh8 fusion tag that has been recently studied and ranked among the best solubility enhancer partners. In this review, we provide an overview of current strategies to improve recombinant protein production in E. coli, including the key factors for successful protein production, highlighting soluble protein production, and a comprehensive summary of the latest available and traditionally used gene fusion technologies. A special emphasis is given to the recently discovered Fh8 fusion system that can be used for soluble protein production, purification, and immunogenicity in E. coli. The number of existing fusion tags will probably increase in the next few years, and efforts should be taken to better understand how fusion tags act in E. coli. This knowledge will undoubtedly drive the development of new tailored-made tools for protein production in this bacterial system.
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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.