Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation
Year: 2002
Type: article
Abstract: 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.
Source: Science
Institutions: Washington University in St. Louis, Karolinska Institutet
Language: English
Subfield: Microbiology
Field: Immunology and Microbiology
Domain: Life Sciences
Open Access status: green
Awards: PATHOGENIC FIBER FORMATION IN BACTERIA: STRUCTURAL BASIS, CHARACTERIZATION OF BACTERIAL AMYLOID-LIKE CURLI FIBERS, G400062658, G4035468545, G4877598716, G5326197911, CHAPERONE ASSISTED PILI ASSEMBLY IN PATHOGENIC E COLI, Chaperone-Assisted Pili Assembly in Pathogenic E. Coli, Alzheimer's Disease Research Center, Impact of Foreign Bodies on Infection Susceptibility, Disease and Mucosal Remodeling of the Urinary Tract, Pathogenic Fiber Formation in Bacteria: Structural Basis
OpenAlex ID: W2021785060