Role of Escherichia coli curli operons in directing amyloid fiber formation

Matthew R. Chapman, Lloyd S. Robinson, Jerome S. Pinkner, Robyn Roth, John Heuser, Mårten Hammar, Staffan Normark, Scott J. Hultgren

Research output: Contribution to journalArticlepeer-review

908 Scopus citations


Amyloid is associated with debilitating human ailments including Alzheimer's and prion diseases. Biochemical, biophysical, and imaging analyses revealed that fibers produced by Escherichia coli called curli were amyloid. The CsgA curlin subunit, purified in the absence of the CsgB nucleator, adopted a soluble, unstructured form that upon prolonged incubation assembled into fibers that were indistinguishable from curli. In vivo, curli biogenesis was dependent on the nucleation-precipitation machinery requiring the CsgE and CsgF chaperone-like and nucleator proteins, respectively. Unlike eukaryotic amyloid formation, curli biogenesis is a productive pathway requiring a specific assembly machinery.

Original languageEnglish
Pages (from-to)851-855
Number of pages5
Issue number5556
StatePublished - Feb 1 2002


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