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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.

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

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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