title: Chaperone-usher pathways: diversity and pilus assembly mechanism.
abstract: Up to eight different types of secretion systems, and several more subtypes, have been described in Gram-negative bacteria. Here, we focus on the diversity and assembly mechanism of one of the best-studied secretion systems, the widespread chaperone-usher pathway known to assemble and secrete adhesive surface structures, called pili or fimbriae, which play essential roles in targeting bacterial pathogens to the host.
authors.affiliation: Institute of Structural and Molecular Biology, University College London, Malet Street, WC1E 7HX London, UK.
authors.forename: Andreas
authors.initials: A
authors.lastname: Busch
authors.forename: Gabriel
authors.initials: G
authors.lastname: Waksman
mesh_terms: D018830:Adhesins, Escherichia coli / Q000737:chemistry; D058947:Bacterial Secretion Systems; D036781:Fimbriae Proteins / Q000737:chemistry; D010861:Fimbriae, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D005816:Genetic Complementation Test; D014644:Genetic Variation; D006090:Gram-Negative Bacteria / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D054884:Host-Pathogen Interactions; D018832:Molecular Chaperones / Q000737:chemistry* / Q000145:classification; D005810:Multigene Family; D046912:Multiprotein Complexes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011971:Receptors, Immunologic / Q000737:chemistry
chemical_list: D018830:Adhesins, Escherichia coli; D058947:Bacterial Secretion Systems; D018832:Molecular Chaperones; D046912:Multiprotein Complexes; D011971:Receptors, Immunologic; C047105:bacterial adhesin receptor; C063629:fimD protein, bacteria; C058769:fimH protein, E coli; D036781:Fimbriae Proteins