Nucleation, cross-reactivity and structure of bacterial functional amyloids

Project Details


It is well established that the self-assembly into cross-ß-structured
fibrils is not restricted to off-pathway protein misfolding events seen
in pathological amyloidosis but is also found as the native
conformation of a wide range of pro- and eukaryotic proteins referred
to as functional amyloids (FA). A significant fraction of the FAs
produced by prokaryotes are related to the persistence and virulence
of bacterial biofilms. Despite their importance, little is known
regarding the FA ultrastructure and their mechanism of formation. In
this project we seek to determine the fiber structures and nucleation
mechanisms of 3 selected FAs that contribute to the virulence of
well-known human pathogens. Because there is an increasing
awareness that bacterial FAs can trigger the co-aggregation of
pathologic amyloid proteins and peptides, we will also study the
cross-reactivity between our FA targets and two amyloid model
systems, Aß and α-synuclein. We are confident that this project can
deepen the understanding of how bacteria handle these potentially
cytotoxic proteins, inspire novel antibacterial strategies by targeting
FA virulence factors and expose additional health risk factors
associated with FA triggered amyloidosis of host proteins.
Effective start/end date1/01/2131/12/24

Flemish discipline codes

  • Molecular and cell biology not elsewhere classified
  • Phase transformations
  • Proteins


  • Structural Biology
  • Functional Amyloids
  • Nucleation