Curli are extracellular organelles produced by Escherichia coli
and certain Salmonella
species. These fibers are structurally and biochemically identical to eukaryotic amyloid fibers, which underlie diverse mammalian ailments including Alzheimer's disease (AD), systemic amyloidosis, bovine spongiform encephalopathy (mad cow disease), and Creutzfeldt-Jacob disease, among others.
E. coli bacteria expressing the functional amyloid fiber, curli.
Curli provide a powerful model system for studying the fundamental principles of amyloid formation. Curli assembly requires the csgBA
operons. The polymerization of the major curli subunit protein, CsgA, is dependent on the CsgB nucleator. Transport of CsgA and CsgB to the cell surface is mediated by the assembly factors CsgE, CsgF, and CsgG. The lab is focused on elucidation of the mechanisms and protein interactions that occur to facilitate the secretion and directed polymerization of CsgA into extracellular amyloid, as well as the consequences of curli formation on the host-pathogen interaction.
Listen to Matt Chapman's interview with MicroWorld Radio
on "Bacteria and Alzheimer's Therapies."