Functional amyloids are produced by organisms that span nearly every facet of cellular life. Curli are functional amyloids produced by many Gram-negative bacteria, including E. coli. Curli fibers are associated with biofilm formation, host cell adhesion and invasion, and immune system activation. The major curli subunit protein, CsgA, polymerizes into amyloid after interacting the CsgB nucleator protein. CsgB presents an amyloid-like template to CsgA on the cell surface that initiates fiber formation. We have identified a powerful anti-aggregation/chaperone-like activity in E. coli that is mediated by the CsgC protein. We will combine the biophysical expertise of the Steel laboratory to interrogate the chaperone-CsgA interaction. We already know that this chaperone-substrate interaction is unique, since the chaperone can prevent CsgA aggregation at a 1:40 molar excess of CsgA. This project will help define the mechanism of CsgC's anti-amyloid activity.
Biofilm formation protects Escherichia coli against killing by Caenorhabditis elegans and Myxococcus xanthus
Published in Applied and Environmental Microbiology, 2014