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Trends Microbiol. 2015 Nov;23(11):693-706. doi: 10.1016/j.tim.2015.07.010. Epub 2015 Oct 1.

Bacterial amyloid formation: structural insights into curli biogensis.

Author information

1
Structural and Molecular Microbiology, Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium.
2
Department of Molecular Microbiology and Microbial Pathogenesis, Washington University in Saint Louis School of Medicine, St Louis, MO 63110-1010, USA.
3
Structural and Molecular Microbiology, Structural Biology Research Center, VIB, Pleinlaan 2, 1050 Brussels, Belgium; Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan 2, 1050 Brussels, Belgium. Electronic address: han.remaut@vib-vub.be.

Abstract

Curli are functional amyloid fibers assembled by many Gram-negative bacteria as part of an extracellular matrix that encapsulates the bacteria within a biofilm. A multicomponent secretion system ensures the safe transport of the aggregation-prone curli subunits across the periplasm and outer membrane, and coordinates subunit self-assembly into surface-attached fibers. To avoid the build-up of potentially toxic intracellular protein aggregates, the timing and location of the interactions of the different curli proteins are of paramount importance. Here we review the structural and molecular biology of curli biogenesis, with a focus on the recent breakthroughs in our understanding of subunit chaperoning and secretion. The mechanistic insight into the curli assembly pathway will provide tools for new biotechnological applications and inform the design of targeted inhibitors of amyloid polymerization and biofilm formation.

KEYWORDS:

amyloid chaperone; biofilm matrix; functional amyloid; peptide diffusion channel; protein secretion

PMID:
26439293
PMCID:
PMC4636965
DOI:
10.1016/j.tim.2015.07.010
[Indexed for MEDLINE]
Free PMC Article

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