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Pàgina inicial > Articles > Articles publicats > Bacterial inclusion bodies are industrially exploitable amyloids |
Data: | 2019 |
Resum: | 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. |
Ajuts: | 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 |
Drets: | Tots els drets reservats. |
Llengua: | Anglès |
Document: | Article ; recerca ; Versió acceptada per publicar |
Matèria: | Recombinant bacteria ; Protein production ; Inclusion bodies ; Functional amyloids ; Biomaterials ; Protein release |
Publicat a: | FEMS Microbiology Reviews, Vol. 43, Issue 1 (January 2019) , p. 53-72, ISSN 1574-6976 |
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 |