A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis

Publication: Research - peer-reviewJournal article



  • Sarah L Rouse
    Sarah L RouseImperial College London
  • William J Hawthorne
    William J HawthorneImperial College London
  • Jamie-Lee Berry
    Jamie-Lee BerryImperial College London
  • Dror S Chorev
    Dror S ChorevUniversity of Oxford
  • Sandra A Ionescu
    Sandra A IonescuUniversity of Oxford
  • Sebastian Lambert
    Sebastian LambertDuke-NUS Medical School
  • Fisentzos Stylianou
    Fisentzos StylianouImperial College London
  • Wiebke Ewert
    Wiebke EwertImperial College London
  • Uma Mackie
    Uma MackieImperial College LondonWalthamstow School for Girls
  • R Marc L Morgan
    R Marc L MorganImperial College London
  • Daniel Otzen
  • Florian-Alexander Herbst
    Florian-Alexander HerbstAalborg Universitet
  • Per H Nielsen
    Per H NielsenAalborg Universitet
  • Morten Dueholm
    Morten DueholmAalborg Universitet
  • Hagan Bayley
    Hagan BayleyUniversity of Oxford
  • Carol V Robinson
    Carol V RobinsonUniversity of Oxford
  • Stephen Hare
    Stephen HareImperial College London
  • Stephen Matthews
    Stephen MatthewsImperial College London

Gram-negative bacteria possess specialised biogenesis machineries that facilitate the export of amyloid subunits for construction of a biofilm matrix. The secretion of bacterial functional amyloid requires a bespoke outer-membrane protein channel through which unfolded amyloid substrates are translocated. Here, we combine X-ray crystallography, native mass spectrometry, single-channel electrical recording, molecular simulations and circular dichroism measurements to provide high-resolution structural insight into the functional amyloid transporter from Pseudomonas, FapF. FapF forms a trimer of gated β-barrel channels in which opening is regulated by a helical plug connected to an extended coil-coiled platform spanning the bacterial periplasm. Although FapF represents a unique type of secretion system, it shares mechanistic features with a diverse range of peptide translocation systems. Our findings highlight alternative strategies for handling and export of amyloid protein sequences.Gram-negative bacteria assemble biofilms from amyloid fibres, which translocate across the outer membrane as unfolded amyloid precursors through a secretion system. Here, the authors characterise the structural details of the amyloid transporter FapF in Pseudomonas.

Original languageEnglish
Article number263
JournalNature Communications
Issue number1
StatePublished - 2017


  • Journal Article

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