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    Packaging protein drugs as bacterial inclusion bodies for therapeutic applications

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    Authors
    Villaverde, Antonio
    García-Fruitós, Elena
    Rinas, Ursula
    Seras-Franzoso, Joaquin
    Kosoy, Ana
    Corchero, José L
    Vazquez, Esther
    Issue Date
    2012-06-11
    
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    Abstract
    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.
    Citation
    Microbial Cell Factories. 2012 Jun 11;11(1):76
    URI
    http://dx.doi.org/10.1186/1475-2859-11-76
    http://hdl.handle.net/10033/620757
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    publications of the research group recombinant protein expression (RPEX)

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