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Interaction of membrane vesicles with the Pseudomonas functional amyloid protein FapC facilitates amyloid formation.

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  • Zahra Najarzadeh, Interdisciplinary Nanoscience Centre (INANO)
  • ,
  • Hossein Mohammad-Beigi, Interdisciplinary Nanoscience Centre (INANO), Department of Biotechnology and Biomedicine, Technical University of Denmark
  • ,
  • Jannik Nedergaard Pedersen, Interdisciplinary Nanoscience Centre (INANO)
  • ,
  • Gunna Christiansen, Research Centre for Prevention and Health, The Capital Region of Denmark, Copenhagen, Denmark Faculty of Medicine, Department of Health Science and Technology, Aalborg University, Aalborg, Denmark., Aalborg University
  • ,
  • Jan Skov Pedersen
  • Janni Nielsen
  • Daniel E Otzen

Functional amyloids (FA) are proteins which are evolutionarily optimized to form highly stable fibrillar structures that strengthen the bacterial biofilm matrix. FA such as CsgA ( E. coli) and FapC ( Pseudomonas) are secreted to the bacterial surface where they integrate into growing fibril structures projecting from the outer membrane. FA are exposed to membrane surfaces in this process, but it remains unclear how membranes can interact with FA and potentially affect the self-assembly. Here we report the effect of different vesicles (DOPG, DMPG, DOPS, DOPC and DMPC) on the kinetics and structural endpoints of FapC fibrillation using various biophysical techniques. Particularly anionic lipids such as DMPG trigger FapC fibrillation, and the protein's second repeat sequence (R2) appears to be important for this interaction. Vesicles formed from phospholipids extracted from three different Pseudomonas strains (Δfap, ΔFapC and pfap) induce FapC fibrillation by accelerating nucleation. The general aggregation inhibitor epigallocatechin gallate (EGCG) inhibits FapC fibrillation by blocking interactions between FapC and vesicles and redirecting FapC monomers to oligomer structures. Our work indicates that biological membranes can contribute significantly to the fibrillation of functional amyloid.

Original languageEnglish
Article number100055
JournalBBA advances
Pages (from-to)100055
Publication statusPublished - 2022

Bibliographical note

© 2022 The Authors.

    Research areas

  • EGCG, FapC protein, ThT kinetics, bacterial amyloid, membrane vesicle

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