ArticleMicrobial cell factories2012
Inclusion bodies as potential vehicles for recombinant protein delivery into epithelial cells.
Article in Microbial cell factories, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 43 citations in OpenAlex.
- Challenges Associated With the Formation of Recombinant Protein Inclusion Bodies inFrontiers in bioengineering and biotechnology · 2021Review
- Production of Active Recombinant Hyaluronidase Inclusion Bodies fromInternational journal of molecular sciences · 2020Article
- Targeting Antitumoral Proteins to Breast Cancer by Local Administration of Functional Inclusion Bodies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Article
- Bacterial mimetics of endocrine secretory granules as immobilized in vivo depots for functional protein drugs.Scientific reports · 2016Article
- Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli.Microbial cell factories · 2014Article
- Dynamic transcriptional response of Escherichia coli to inclusion body formation.Biotechnology and bioengineering · 2014Article
- Inclusion bodies: not that bad….Frontiers in microbiology · 2014Review
- Why and how protein aggregation has to be studied in vivo.Microbial cell factories · 2013Article
- Bacterial inclusion bodies as potential synthetic devices for pathogen recognition and a therapeutic substance release.Microbial cell factories · 2013Article
- Packaging protein drugs as bacterial inclusion bodies for therapeutic applications.Microbial cell factories · 2012Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundWe present the potential of inclusion bodies (IBs) as a protein delivery method for polymeric filamentous proteins. We used as cell factory a strain of E. coli, a conventional host organism, and keratin 14 (K14) as an example of a complex protein. Keratins build the intermediate filament cytoskeleton of all epithelial cells. In order to build filaments, monomeric K14 needs first to dimerize with its binding partner (keratin 5, K5), which is then followed by heterodimer assembly into filaments.
resultsK14 IBs were electroporated into SW13 cells grown in culture together with a "reporter" plasmid containing EYFP labeled keratin 5 (K5) cDNA. As SW13 cells do not normally express keratins, and keratin filaments are built exclusively of keratin heterodimers (i.e. K5/K14), the short filamentous structures we obtained in this study can only be the result of: a) if both IBs and plasmid DNA are transfected simultaneously into the cell(s); b) once inside the cells, K14 protein is being released from IBs; c) released K14 is functional, able to form heterodimers with EYFP-K5.
conclusionsSoluble IBs may be also developed for complex cytoskeletal proteins and used as nanoparticles for their delivery into epithelial cells.
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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.