title: Microbial manipulation of the amyloid fold.
abstract: Microbial biofilms are encased in a protein, DNA, and polysaccharide matrix that protects the community, promotes interactions with the environment, and helps cells adhere together. The protein component of these matrices is often a remarkably stable, β-sheet-rich polymer called amyloid. Amyloids form ordered, self-templating fibers that are highly aggregative, making them a valuable biofilm component. Some eukaryotic proteins inappropriately adopt the amyloid fold, and these misfolded protein aggregates disrupt normal cellular proteostasis, which can cause significant cytotoxicity. Indeed, until recently amyloids were considered solely the result of protein misfolding. However, research over the past decade has revealed how various organisms have capitalized on the amyloid fold by developing sophisticated biogenesis pathways that coordinate gene expression, protein folding, and secretion so that amyloid-related toxicities are minimized. How microbes manipulate amyloids, by augmenting their advantageous properties and by reducing their undesirable properties, will be the subject of this review.
authors.affiliation: Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI 48109-0620, USA. whdepas@umich.edu
authors.forename: William H
authors.initials: WH
authors.lastname: DePas
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Chapman
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism*; D018407:Bacterial Physiological Phenomena; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D018441:Biofilms / Q000254:growth & development*; D008958:Models, Molecular; D017510:Protein Folding; D055503:Protein Multimerization
chemical_list: D000682:Amyloid; D001426:Bacterial Proteins