Biological role of bacterial inclusion bodies: a model for amyloid aggregation

Authors

  • Elena García-Fruitós,

    1.  Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Spain
    2.  Department of Genetics and Microbiology, Universitat Autònoma de Barcelona, Spain
    3.  CIBER de Bioingeniería, Biomateriales y Nanomedicina (CIBER-BBN), Barcelona, Spain
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    • These authors contributed equally to this work

  • Raimon Sabate,

    1.  Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Spain
    2.  Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain
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    • These authors contributed equally to this work

  • Natalia S. de Groot,

    1.  Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Spain
    2.  Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain
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  • Antonio Villaverde,

    1.  Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Spain
    2.  Department of Genetics and Microbiology, Universitat Autònoma de Barcelona, Spain
    3.  CIBER de Bioingeniería, Biomateriales y Nanomedicina (CIBER-BBN), Barcelona, Spain
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  • Salvador Ventura

    1.  Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Spain
    2.  Department of Biochemistry and Molecular Biology, Universitat Autònoma de Barcelona, Spain
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A. Villaverde, Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
Fax: +34 93 581 2011
Tel: +34 93 581 2148
E-mail: Antoni.Villaverde@uab.cat

S. Ventura, Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain
Fax: +34 93 581 2011
Tel: +34 93 586 8956
E-mail: salvador.ventura@uab.es

Abstract

Inclusion bodies are insoluble protein aggregates usually found in recombinant bacteria when they are forced to produce heterologous protein species. These particles are formed by polypeptides that cross-interact through sterospecific contacts and that are steadily deposited in either the cell’s cytoplasm or the periplasm. An important fraction of eukaryotic proteins form inclusion bodies in bacteria, which has posed major problems in the development of the biotechnology industry. Over the last decade, the fine dissection of the quality control system in bacteria and the recognition of the amyloid-like architecture of inclusion bodies have provided dramatic insights on the dynamic biology of these aggregates. We discuss here the relevant aspects, in the interface between cell physiology and structural biology, which make inclusion bodies unique models for the study of protein aggregation, amyloid formation and prion biology in a physiologically relevant background.

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