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Bacterial Amyloid Secretion: Structural Biology and Biotechnology.

Total Cost €


EC-Contrib. €






 BAS-SBBT project word cloud

Explore the words cloud of the BAS-SBBT project. It provides you a very rough idea of what is the project "BAS-SBBT" about.

amyloidogenic    harness    thought    parkinson    assembly    temporally    questions    reconstitution    pro    outer    surface    subunits    proteins    guidance    transport    insights    soluble    found    fiber    biofilm    misfolding    unravel    vitro    bacteroidetes    diseases    periplasm    secretion    sufficient    mediated    biofilms    interdisciplinary    polypeptides    intermediates    unlike    proteobacteria    functional    selective    structurally    curli    specialised    gained    patterned    critical    bacterial    structure    safe    biosynthesis    biotechnological    fundamental    fibers    disease    functionalized    formed    assemble    deposition    alzheimer    directed    events    carriers    coordinate    molecular    amyloid    constitute    aggregation    protein    machinery    coli    extracellular    matrix    biology    pellicle    cell    pathological    self    framework    minimal    accessory    interventions    transporter    structural    concerning    stage    membrane    mechanistically    nanowires    peptide    trap   

Project "BAS-SBBT" data sheet

The following table provides information about the project.


Organization address
postcode: 9052

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country Belgium [BE]
 Total cost 1˙989˙488 €
 EC max contribution 1˙989˙488 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2014-CoG
 Funding Scheme ERC-COG
 Starting year 2015
 Duration (year-month-day) from 2015-06-01   to  2020-05-31


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    VIB BE (ZWIJNAARDE - GENT) coordinator 1˙989˙488.00


 Project objective

Curli are functional amyloid fibers that constitute the major protein component of the extracellular matrix in pellicle biofilms formed by Bacteroidetes and Proteobacteria. Unlike the protein misfolding and aggregation events seen in pathological amyloid diseases such as Alzheimer’s and Parkinson’s disease, curli are the product of a dedicated protein secretion machinery. Curli formation requires a specialised and mechanistically unique transporter in the bacterial outer membrane, as well as two soluble accessory proteins thought to facilitate the safe guidance of the curli subunits across the periplasm and to coordinate their self-assembly at cell surface.

In this interdisciplinary research program we will study the structural and molecular biology of E. coli curli biosynthesis and address the fundamental questions concerning the molecular processes that allow the spatially and temporally controlled transport and deposition of these pro-amyloidogenic polypeptides. We will structurally unravel the secretion machinery, trap and analyse critical secretion intermediates and through in vitro reconstitution, assemble a minimal, self-sufficient peptide transport and fiber assembly system.

The new insights gained will set the stage for targeted interventions in curli -mediated biofilm formation and this research project will develop a new framework to harness the unique properties found in curli structure and biosynthesis for biotechnological applications as in patterned functionalized nanowires and directed, selective peptide carriers.


year authors and title journal last update
List of publications.
2015 Nani Van Gerven, Roger D. Klein, Scott J. Hultgren, Han Remaut
Bacterial Amyloid Formation: Structural Insights into Curli Biogensis
published pages: 693-706, ISSN: 0966-842X, DOI: 10.1016/j.tim.2015.07.010
Trends in Microbiology 23/11 2019-06-07
2017 Mike Sleutel, Imke Van den Broeck, Nani Van Gerven, Cécile Feuillie, Wim Jonckheere, Claire Valotteau, Yves F Dufrêne, Han Remaut
Nucleation and growth of a bacterial functional amyloid at single-fiber resolution
published pages: 902-908, ISSN: 1552-4450, DOI: 10.1038/nchembio.2413
Nature Chemical Biology 13/8 2019-06-07

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