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00925njm 22002777a 4500 dc de Marco, Ario author Ferrer-Miralles, Neus author Garcia-Fruitós, Elena author Mitraki, Anna author Peternel, Spela author Rinas, Ursula author Trujillo-Roldán, Mauricio A author Valdez-Cruz, Norma A author Vázquez, Esther author Villaverde, Antonio author 2018-10-24 Understanding the structure, functionalities and biology of functional amyloids is an issue of emerging interest. Inclusion bodies, namely protein clusters formed in recombinant bacteria during protein production processes, have emerged as unanticipated, highly tunable models for the scrutiny of the physiology and architecture of functional amyloids. Based on an amyloidal skeleton combined with varying amounts of native or native-like protein forms, bacterial inclusion bodies exhibit an unusual arrangement that confers mechanical stability, biological activity and conditional protein release, being thus exploitable as versatile biomaterials. The applicability of inclusion bodies in biotechnology as enriched sources of protein and reusable catalysts, and in biomedicine as biocompatible topographies, nanopills or mimetics of endocrine secretory granules has been largely validated. Beyond these uses, the dissection of how recombinant bacteria manage the aggregation of functional protein species into structures of highly variable complexity offers insights about unsuspected connections between protein quality (conformational status compatible with functionality) and cell physiology. de Marco, Ario, Neus Ferrer-Miralles, Elena Garcia-Fruitós, Anna Mitraki, Spela Peternel, Ursula Rinas, Mauricio A Trujillo-Roldán, Norma A Valdez-Cruz, Esther Vázquez, and Antonio Villaverde. 2018. "Bacterial Inclusion Bodies Are Industrially Exploitable Amyloids". FEMS Microbiology Reviews 43 (1): 53-72. Oxford University Press (OUP). doi:10.1093/femsre/fuy038. 0168-6445 http://hdl.handle.net/20.500.12327/401 https://doi.org/10.1093/femsre/fuy038 Bacterial inclusion bodies are industrially exploitable amyloids