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Bacterial amyloid (Curli) biogenesis
Fibrillar amyloid adhesins are an important and common structural motif in biofilm architecture. Many bacteria that form medically relevant biofilms, such as UPEC, enterohemorrhagic E. coli (EHEC), Salmonella spp., Citrobacter spp., and Mycobacterium tuberculosis produce amyloid fibers which can provide structural, adhesive and protective properties to a biofilm. Curli is one such amyloid fiber, produced by UPEC and Salmonella.
Curli assembly in bacteria occurs via a unique, highly regulated and directed process. The formation of the curli fiber consisting of the CsgA (major component) and CsgB (minor component) is facilitated by the functions of two chaperone-like proteins, CsgF and CsgE, and an outer membrane assembly protein, CsgG.
Our work to determine how curli are assembled will provide insight into potential anti-biofilm strategies that could be used to disrupt biofilm formation by pathogenic bacteria and will make important new discoveries at the interface of multiple disciplines: protein folding, amyloid biology, microbiology, biophysics, structural biology, infection, biofilm formation and antibiotic resistance.
In addition, given the high percentage of human diseases thought to involve amyloid formation this may have more general implications related to neurodegenerative disorders and the transmission of food borne pathogens.
Collaborators: Carl Frieden, Matt Chapman, Fredrik Almqvist, Han Remaut.