Details
| Original language | English |
|---|---|
| Article number | 76 |
| Journal | Microbial cell factories |
| Volume | 11 |
| Publication status | Published - 11 Jun 2012 |
Abstract
A growing number of insights on the biology of bacterial inclusion bodies (IBs) have revealed intriguing utilities of these protein particles. Since they combine mechanical stability and protein functionality, IBs have been already exploited in biocatalysis and explored for bottom-up topographical modification in tissue engineering. Being fully biocompatible and with tuneable bio-physical properties, IBs are currently emerging as agents for protein delivery into mammalian cells in protein-replacement cell therapies. So far, IBs formed by chaperones (heat shock protein 70, Hsp70), enzymes (catalase and dihydrofolate reductase), grow factors (leukemia inhibitory factor, LIF) and structural proteins (the cytoskeleton keratin 14) have been shown to rescue exposed cells from a spectrum of stresses and restore cell functions in absence of cytotoxicity. The natural penetrability of IBs into mammalian cells (reaching both cytoplasm and nucleus) empowers them as an unexpected platform for the controlled delivery of essentially any therapeutic polypeptide. Production of protein drugs by biopharma has been traditionally challenged by IB formation. However, a time might have arrived in which recombinant bacteria are to be engineered for the controlled packaging of therapeutic proteins as nanoparticulate materials (nanopills), for their extra- or intra-cellular release in medicine and cosmetics.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biotechnology
- Chemical Engineering(all)
- Bioengineering
- Immunology and Microbiology(all)
- Applied Microbiology and Biotechnology
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In: Microbial cell factories, Vol. 11, 76, 11.06.2012.
Research output: Contribution to journal › Comment/debate › Research › peer review
}
TY - JOUR
T1 - Packaging protein drugs as bacterial inclusion bodies for therapeutic applications
AU - Villaverde, Antonio
AU - García-Fruitós, Elena
AU - Rinas, Ursula
AU - Seras-Franzoso, Joaquin
AU - Kosoy, Ana
AU - Corchero, José L.
AU - Vazquez, Esther
N1 - Funding Information: We appreciate the financial support received for the development of therapeutic inclusion bodies and of the Nanopill concept from MICINN (BFU2010-17450), AGAUR (2009SGR-108) and CIBER de Bioingeniería, Biomateriales y Nanomedicina (CIBER-BBN), Spain. A. Villaverde has been granted with an ICREA ACADEMIA award (from ICREA, Catalonia, Spain) and EGF is supported by the Programa Personal de Técnico de Apoyo (Modalidad Infraestructuras científco-tecnológicas, MICINN). JSF is a PIF fellowship holder from UAB, Spain.
PY - 2012/6/11
Y1 - 2012/6/11
N2 - A growing number of insights on the biology of bacterial inclusion bodies (IBs) have revealed intriguing utilities of these protein particles. Since they combine mechanical stability and protein functionality, IBs have been already exploited in biocatalysis and explored for bottom-up topographical modification in tissue engineering. Being fully biocompatible and with tuneable bio-physical properties, IBs are currently emerging as agents for protein delivery into mammalian cells in protein-replacement cell therapies. So far, IBs formed by chaperones (heat shock protein 70, Hsp70), enzymes (catalase and dihydrofolate reductase), grow factors (leukemia inhibitory factor, LIF) and structural proteins (the cytoskeleton keratin 14) have been shown to rescue exposed cells from a spectrum of stresses and restore cell functions in absence of cytotoxicity. The natural penetrability of IBs into mammalian cells (reaching both cytoplasm and nucleus) empowers them as an unexpected platform for the controlled delivery of essentially any therapeutic polypeptide. Production of protein drugs by biopharma has been traditionally challenged by IB formation. However, a time might have arrived in which recombinant bacteria are to be engineered for the controlled packaging of therapeutic proteins as nanoparticulate materials (nanopills), for their extra- or intra-cellular release in medicine and cosmetics.
AB - A growing number of insights on the biology of bacterial inclusion bodies (IBs) have revealed intriguing utilities of these protein particles. Since they combine mechanical stability and protein functionality, IBs have been already exploited in biocatalysis and explored for bottom-up topographical modification in tissue engineering. Being fully biocompatible and with tuneable bio-physical properties, IBs are currently emerging as agents for protein delivery into mammalian cells in protein-replacement cell therapies. So far, IBs formed by chaperones (heat shock protein 70, Hsp70), enzymes (catalase and dihydrofolate reductase), grow factors (leukemia inhibitory factor, LIF) and structural proteins (the cytoskeleton keratin 14) have been shown to rescue exposed cells from a spectrum of stresses and restore cell functions in absence of cytotoxicity. The natural penetrability of IBs into mammalian cells (reaching both cytoplasm and nucleus) empowers them as an unexpected platform for the controlled delivery of essentially any therapeutic polypeptide. Production of protein drugs by biopharma has been traditionally challenged by IB formation. However, a time might have arrived in which recombinant bacteria are to be engineered for the controlled packaging of therapeutic proteins as nanoparticulate materials (nanopills), for their extra- or intra-cellular release in medicine and cosmetics.
UR - http://www.scopus.com/inward/record.url?scp=84861975854&partnerID=8YFLogxK
U2 - 10.1186/1475-2859-11-76
DO - 10.1186/1475-2859-11-76
M3 - Comment/debate
C2 - 22686540
AN - SCOPUS:84861975854
VL - 11
JO - Microbial cell factories
JF - Microbial cell factories
SN - 1475-2859
M1 - 76
ER -