title: Biological role of bacterial inclusion bodies: a model for amyloid aggregation.
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.
authors.affiliation: Institute for Biotechnology and Biomedicine, Universitat Autònoma de Barcelona, Barcelona, Spain.
authors.forename: Elena
authors.initials: E
authors.lastname: García-Fruitós
authors.forename: Raimon
authors.initials: R
authors.lastname: Sabate
authors.forename: Natalia S
authors.initials: NS
authors.lastname: de Groot
authors.forename: Antonio
authors.initials: A
authors.lastname: Villaverde
authors.forename: Salvador
authors.initials: S
authors.lastname: Ventura
mesh_terms: D000682:Amyloid / Q000096:biosynthesis / Q000737:chemistry*; D000818:Animals; D006090:Gram-Negative Bacteria / Q000378:metabolism* / Q000648:ultrastructure; D006094:Gram-Positive Bacteria / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D002479:Inclusion Bodies / Q000502:physiology* / Q000648:ultrastructure; D007218:Industrial Microbiology / Q000379:methods; D008954:Models, Biological; D011328:Prions / Q000096:biosynthesis / Q000737:chemistry; D017510:Protein Folding; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry*; D012995:Solubility
chemical_list: D000682:Amyloid; D011328:Prions; D011994:Recombinant Proteins