title: Diversity, biogenesis and function of microbial amyloids.
abstract: Amyloid is a distinct β-sheet-rich fold that many proteins can acquire. Frequently associated with neurodegenerative diseases in humans, including Alzheimer's, Parkinson's and Huntington's diseases, amyloids are traditionally considered the product of protein misfolding. However, the amyloid fold is now recognized as a ubiquitous part of normal cellular biology. Functional amyloids have been identified in nearly all facets of cellular life, with microbial functional amyloids leading the way. Unlike disease-associated amyloids, functional amyloids are assembled by dedicated, directed pathways and ultimately perform a physiological function that benefits the organism. The evolved amyloid assembly and disassembly pathways of microbes have provided novel insights into how cells have harnessed the amyloid assembly process for productive means. An understanding of functional amyloid biogenesis promises to provide a fresh perspective on the molecular events that underlie disease-associated amyloidogenesis. Here, we review functional microbial amyloids with an emphasis on curli fibers and their role in promoting biofilm formation and other community behaviors.
authors.affiliation: Department of Molecular Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA.
authors.forename: Luz P
authors.initials: LP
authors.lastname: Blanco
authors.forename: Margery L
authors.initials: ML
authors.lastname: Evans
authors.forename: Daniel R
authors.initials: DR
authors.lastname: Smith
authors.forename: Matthew P
authors.initials: MP
authors.lastname: Badtke
authors.forename: Matthew R
authors.initials: MR
authors.lastname: Chapman
mesh_terms: D018829:Adhesins, Bacterial / Q000737:chemistry / Q000378:metabolism*; D000682:Amyloid / Q000737:chemistry / Q000378:metabolism*; D001419:Bacteria / Q000737:chemistry / Q000378:metabolism*; D044822:Biodiversity; D018441:Biofilms / Q000254:growth & development*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary
chemical_list: D018829:Adhesins, Bacterial; D000682:Amyloid; C109182:CsgB protein, E coli; D029968:Escherichia coli Proteins; C489688:csgA protein, E coli