Bacterial inclusion bodies are industrially exploitable amyloids
de Marco, Ario (University of Nova Gorica. Laboratory for Environmental and Life Sciences (Slovenia))
Ferrer-Miralles, Neus (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Garcia-Fruitos, Elena (Institut de Recerca i Tecnologia Agroalimentàries)
Mitraki, Anna (University of Crete. Department of Materials Science and Technology (Greece))
Peternel, Spela (Lupinica (Slovenia))
Rinas, Ursula (Leibniz University of Hannover. Technical Chemistry and Life Science (Germany))
Trujillo-Roldán, Mauricio A. (Universidad Nacional Autónoma de México. Instituto de Investigaciones Biomédicas)
Valdez-Cruz, Norma A. (Universidad Nacional Autónoma de México. Instituto de Investigaciones Biomédicas)
Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia

Fecha:	2019
Resumen:	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.
Ayudas:	Ministerio de Economía y Competitividad RTA2015-00064-C02-02 Ministerio de Economía y Competitividad RTA2015-00064-C02-01 Instituto de Salud Carlos III PI15-00272 Ministerio de Ciencia e Innovación BIO2016-76063-R Agència de Gestió d'Ajuts Universitaris i de Recerca 2017/SGR-229
Nota:	Altres ajuts: CERCA Programme/Generalitat de Catalunya
Derechos:	Tots els drets reservats.
Lengua:	Anglès
Documento:	Article ; recerca ; Versió acceptada per publicar
Materia:	Recombinant bacteria ; Protein production ; Inclusion bodies ; Functional amyloids ; Biomaterials ; Protein release
Publicado en:	FEMS Microbiology Reviews, Vol. 43, Issue 1 (January 2019) , p. 53-72, ISSN 1574-6976

DOI: 10.1093/femsre/fuy038
PMID: 30357330

Article. Postprint 62 p, 1.5 MB	Graphical abstract. Arxiu tif 226x219, 37.5 KB	Taula 1 2 p, 539.8 KB	Suplement Taula 1 4 p, 720.2 KB	Figura 1. Arxiu pptx 1.6 MB	Figura 2. Arxiu pptx 86.2 KB
Figura 3. Arxiu pptx 9.6 MB

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