title: Effective assembly of fimbriae in Escherichia coli depends on the translocation assembly module nanomachine.
abstract: Outer membrane proteins are essential for Gram-negative bacteria to rapidly adapt to changes in their environment. Intricate remodelling of the outer membrane proteome is critical for bacterial pathogens to survive environmental changes, such as entry into host tissues(1-3). Fimbriae (also known as pili) are appendages that extend up to 2 μm beyond the cell surface to function in adhesion for bacterial pathogens, and are critical for virulence. The best-studied examples of fimbriae are the type 1 and P fimbriae of uropathogenic Escherichia coli, the major causative agent of urinary tract infections in humans. Fimbriae share a common mode of biogenesis, orchestrated by a molecular assembly platform called 'the usher' located in the outer membrane. Although the mechanism of pilus biogenesis is well characterized, how the usher itself is assembled at the outer membrane is unclear. Here, we report that a rapid response in usher assembly is crucially dependent on the translocation assembly module. We assayed the assembly reaction for a range of ushers and provide mechanistic insight into the β-barrel assembly pathway that enables the rapid deployment of bacterial fimbriae.
authors: Infection &Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Clayton 3800, Australia.
authors: Christopher
authors: C
authors: Stubenrauch
authors: Infection &Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Clayton 3800, Australia.
authors: Matthew J
authors: MJ
authors: Belousoff
authors: Infection &Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Clayton 3800, Australia.
authors: Iain D
authors: ID
authors: Hay
authors: Infection &Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Clayton 3800, Australia.|Department of Materials Engineering, Monash University, Clayton 3800, Australia.
authors: Hsin-Hui
authors: HH
authors: Shen
authors: Institute of Structural and Molecular Biology (ISMB), University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK.
authors: James
authors: J
authors: Lillington
authors: School of Chemistry, Monash University, Clayton 3800, Australia.
authors: Kellie L
authors: KL
authors: Tuck
authors: School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia 4072, Australia.
authors: Kate M
authors: KM
authors: Peters
authors: School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia 4072, Australia.
authors: Minh-Duy
authors: MD
authors: Phan
authors: School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia 4072, Australia.
authors: Alvin W
authors: AW
authors: Lo
authors: School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia 4072, Australia.
authors: Mark A
authors: 0000-0003-4863-9260
authors: MA
authors: Schembri
authors: Department of Microbiology &Immunology, University of Melbourne, Parkville 3052, Australia.
authors: Richard A
authors: 0000-0003-0614-5641
authors: RA
authors: Strugnell
authors: Institute of Structural and Molecular Biology (ISMB), University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK.
authors: Gabriel
authors: G
authors: Waksman
authors: Infection &Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Clayton 3800, Australia.
authors: Trevor
authors: T
authors: Lithgow
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D036781:Fimbriae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000493:pharmacokinetics*; D010861:Fimbriae, Bacterial / Q000235:genetics / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism*; D014551:Urinary Tract / Q000382:microbiology; D014552:Urinary Tract Infections / Q000382:microbiology
chemical_list: D001425:Bacterial Outer Membrane Proteins; C503914:BamA protein, E coli; C574723:CfaC protein, E coli; D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; C489283:fimD protein, E coli; D036781:Fimbriae Proteins