title: Fiber assembly by the chaperone-usher pathway.
abstract: Bacterial pathogens utilize the chaperone-usher pathway to assemble extracellular multi-subunit fibers essential for virulence. The periplasmic chaperone facilitates the initial folding of fiber subunits but then traps them in activated folding transition states. Chaperone dissociation releases the folding energy that drives subunit incorporation into the fiber, which grows through a pore formed by the outer-membrane usher.
authors.affiliation: Section of Microbial Pathogenesis, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Ave., New Haven, CT 06536, USA.
authors.forename: Frederic G
authors.initials: FG
authors.lastname: Sauer
authors.forename: Han
authors.initials: H
authors.lastname: Remaut
authors.forename: Scott J
authors.initials: SJ
authors.lastname: Hultgren
authors.forename: Gabriel
authors.initials: G
authors.lastname: Waksman
mesh_terms: D001426:Bacterial Proteins / Q000502:physiology*; D036781:Fimbriae Proteins / Q000378:metabolism* / Q000502:physiology; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D006090:Gram-Negative Bacteria / Q000502:physiology*; D018832:Molecular Chaperones / Q000235:genetics / Q000502:physiology*; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D018832:Molecular Chaperones; D036781:Fimbriae Proteins