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The Bacterial Curli System Possesses a Potent and Selective Inhibitor of Amyloid Formation
Umeå University, Faculty of Science and Technology, Department of Chemistry.
Umeå University, Faculty of Science and Technology, Department of Chemistry.
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2015 (English)In: Molecular Cell, ISSN 1097-2765, E-ISSN 1097-4164, Vol. 57, no 3, 445-455 p.Article in journal (Refereed) Published
Abstract [en]

Summary Curli are extracellular functional amyloids that are assembled by enteric bacteria during biofilm formation and host colonization. An efficient secretion system and chaperone network ensures that the major curli fiber subunit, CsgA, does not form intracellular amyloid aggregates. We discovered that the periplasmic protein CsgC was a highly effective inhibitor of CsgA amyloid formation. In the absence of CsgC, CsgA formed toxic intracellular aggregates. In vitro, CsgC inhibited CsgA amyloid formation at substoichiometric concentrations and maintained CsgA in a non-β-sheet-rich conformation. Interestingly, CsgC inhibited amyloid assembly of human α-synuclein, but not Aβ42, in vitro. We identified a common D-Q-Φ-X0,1-G-K-N-ζ-E motif in CsgC client proteins that is not found in Aβ42. CsgC is therefore both an efficient and selective amyloid inhibitor. Dedicated functional amyloid inhibitors may be a key feature that distinguishes functional amyloids from disease-associated amyloids.

Place, publisher, year, edition, pages
2015. Vol. 57, no 3, 445-455 p.
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Chemical Sciences
URN: urn:nbn:se:umu:diva-100336DOI: 10.1016/j.molcel.2014.12.025ISI: 000349550700008OAI: diva2:791588
Available from: 2015-03-01 Created: 2015-03-01 Last updated: 2015-03-23Bibliographically approved

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Chorell, ErikÅdén, JörgenGötheson, AnnaWittung-Stafshede, PernillaAlmqvist, FredrikChapman, Matthew R.
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Department of ChemistryUmeå Centre for Microbial Research (UCMR)
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Molecular Cell
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