Ontology highlight
ABSTRACT:
SUBMITTER: Evans ML
PROVIDER: S-EPMC4320674 | biostudies-literature | 2015 Feb
REPOSITORIES: biostudies-literature
Evans Margery L ML Chorell Erik E Taylor Jonathan D JD Åden Jörgen J Götheson Anna A Li Fei F Koch Marion M Sefer Lea L Matthews Steve J SJ Wittung-Stafshede Pernilla P Almqvist Fredrik F Chapman Matthew R MR
Molecular cell 20150122 3
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 forma ...[more]