Abstract:
: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.
journal_name
Mol Celljournal_title
Molecular cellauthors
Evans ML,Chorell E,Taylor JD,Åden J,Götheson A,Li F,Koch M,Sefer L,Matthews SJ,Wittung-Stafshede P,Almqvist F,Chapman MRdoi
10.1016/j.molcel.2014.12.025subject
Has Abstractpub_date
2015-02-05 00:00:00pages
445-55issue
3eissn
1097-2765issn
1097-4164pii
S1097-2765(14)01003-Xjournal_volume
57pub_type
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