Amyloids in bacterial inclusion bodies
Sánchez de Groot, Natalia (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Sabaté, Raimon (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Ventura, Salvador (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")

Date:	2009
Abstract:	Protein misfolding and aggregation into amyloid structures are associated with dozens of human diseases. Recent studies have provided compelling evidence for the existence of highly ordered, amyloid-like conformations in the insoluble inclusion bodies produced during heterologous protein expression in bacteria. Thus, amyloid aggregation seems to be an omnipresent process in both eukaryotic and prokaryotic organisms. Amyloid formation inside cell factories raises important safety concerns with regard to the toxicity and infectivity of recombinant proteins. Yet such findings also suggest that prokaryotic cells could be useful systems for studying how and why proteins aggregate in vivo, and they could also provide a biologically relevant background for screening therapeutic approaches to pathologic protein deposition.
Grants:	Ministerio de Educación y Ciencia BIO2007-68046 Agència de Gestió d'Ajuts Universitaris i de Recerca 2005/SGR-00037
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Language:	Anglès
Document:	Article de revisió ; recerca ; Versió sotmesa a revisió
Subject:	SDG 3 - Good Health and Well-being
Published in:	Trends in Biochemical Sciences, Vol. 34, Issue 8 (August 2009) , p. 408-416, ISSN 1362-4326

DOI: 10.1016/j.tibs.2009.03.009

Preprint 27 p, 1.8 MB

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Research literature > UAB research groups literature > Research Centres and Groups (research output) > Health sciences and biosciences > Institut de Biotecnologia i de Biomedicina (IBB)
Articles > Research articles
Articles > Published articles