My research focuses on how the bacterial biofilm are recognized by the immune system. We are mainly interested in bacterial amyloids, protein deposits with a fibrillar cross beta-sheet quaternary structure, which exhibit a starch (amylose)-like ability to stain with iodine. In humans, deposition of various amyloid proteins is associated with a number of illnesses, such as Alzheimer’s disease, Parkinson's disease, prion diseases, and type-2 diabetes. Interestingly, many bacteria produce functional amyloid deposits, which are an important component of their extracellular biofilm matrix. Curli amyloid fibrils, produced by enteric bacteria such as Salmonella enterica serotype Typhimurium and E. coli, are the best-characterized bacterial amyloid fibrils to date. Amyloids of both host and bacterial origin share a number of characteristics, including an ability to trigger innate immune responses. Recently, we discovered that responses to host amyloids and curli amyloid fibrils are mediated through Toll-like receptor (TLR) 2. Currently, we are working on the immune recognition of curli fibers in the intestinal tract and at systemic sites.