The Formation of Escherichia coli Curli Amyloid Fibrils is Mediated by Prion-like Peptide Repeats

Cherny, Izhack; Rockah, Liat; Levy-Nissenbaum, Orlev; Gophna, Uri; Ron, Eliora Z.; Gazit, Ehud

doi:10.1016/j.jmb.2005.07.028

Cited by 86 publications

(77 citation statements)

References 37 publications

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“…However, until recently there was no evidence that CsgA is secreted from wild-type (Wt) cells in an unpolymerized form. Cherny and colleagues (65) showed that small, rationally designed peptides could abrogate curli formation when added to the media. These peptides are predicted to block reactive surfaces on CsgA that would prevent it from assembling into a fiber.…”

Section: Curli Biogenesismentioning

confidence: 99%

“…Expression of the curli genes in a K-12 E. coli strain that normally does not express curli resulted in the invasion of human cervical epithelial (HeLa) cells (31). Invasion by K-12 isolates expressing curli can be inhibited by peptides that block curli formation (65). E. coli 0157:H7 strains that produce curli attach and invade human laryngeal epithelial (Hep-2) cells (41,82).…”

Section: Role Of Curli In Attachment and Invasion Of Host Cellsmentioning

confidence: 99%

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Curli Biogenesis and Function

Barnhart

Chapman

2006

Annu. Rev. Microbiol.

976

1,028

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Curli are the major proteinaceous component of a complex extra-cellular matrix produced by many Enterobacteriaceae. Curli were first discovered in the late 1980s on Escherichia coli strains that caused bovine mastitis, and have since been implicated in many physiological and pathogenic processes of E. coli and Salmonella spp. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation. Curli also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response. The structure and biogenesis of curli are unique among bacterial fibers that have been described to date. Structurally and biochemically, curli belong to a growing class of fibers known as amyloids. Amyloid fiber formation is responsible for several human diseases including Alzheimer's, Huntington's, and prion diseases, although the process of in vivo amyloid formation is not well understood. Curli provide a unique system to study macromolecular assembly in bacteria and in vivo amyloid fiber formation. Here, we review curli biogenesis, regulation, role in biofilm formation, and role in pathogenesis.

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Section: Curli Biogenesismentioning

confidence: 99%

Section: Role Of Curli In Attachment and Invasion Of Host Cellsmentioning

confidence: 99%

Curli Biogenesis and Function

Barnhart

Chapman

2006

Annu. Rev. Microbiol.

976

1,028

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“…In Escherichia coli, this system is composed of the products of seven curli-specific genes (csg) encoded by two separately transcribed operons, csgBAC and csgDEFG (10). Among the multiple products of the csg gene operons, CsgA forms the major curli subunit and exhibits nucleationdependent oligomerization kinetics in vitro similar to what is observed for pathogenic amyloids from eukaryotic cells (11,12). CsgB, the minor curli subunit, acts as the nucleator for the aggregation of the secreted CsgA curli subunits into curli fibers and is responsible for anchoring the fibers on the producing cell (13).…”

mentioning

confidence: 93%

Structure of the nonameric bacterial amyloid secretion channel

Cao

Zhao

Kou

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

102

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Various strains of bacteria are able to produce a unique class of functional amyloids termed curli, which are critical for biofilm formation, host cell adhesion, and colonization of inert surfaces. Curli are secreted via the type VIII bacterial secretion system, and they share biochemical and structural characteristics with amyloid fibers that have been implicated in deleterious disease in humans. Here, we report the crystal structure of Escherichia coli CsgG, which is an essential lipoprotein component of the type VIII secretion system and which forms a secretion channel in the bacterial outer membrane for transporting curli subunits. CsgG forms a crown-shaped, symmetric nonameric channel that spans the outer membrane via a 36-strand β-barrel, with each subunit contributing four β-strands. This nonameric complex contains a central channel with a pore located at the middle. The eyelet of the pore is ∼12 Å in diameter and is lined with three stacked nine-residue rings consisting of Tyr-66, Asn-70, or Phe-71. Our structure-based functional studies suggest that Tyr-66 and Phe-71 residues function as gatekeepers for the selective secretion of curli subunits. Our study describes in detail, to our knowledge, the first core structure of the type VIII bacterial secretion machinery. Importantly, our structural analysis suggests that the curli subunits are secreted via CsgG across the bacterial outer membrane in an unfolded form.CsgG | curli | amyloids | outer membrane protein | biofilm

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“…The complete absence of aromatic residues in the repeats emphasizes that aromatic residues play no role in these functional amyloids, as seen also for CsgA 66 but in contrast to other modes of stacking β-strands in amyloid 67,68 and prions. 69 Rather the composition is indicative of a very economical use of simple amino acids, which presumably involves minimal metabolic cost. 74 An additional intriguing distinction is the presence of large linkers between FapC's variable repeats.…”

Section: The Role Of the Other Operon Membersmentioning

confidence: 99%

Functional amyloid

Otzen

2010

Prion

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The Formation of Escherichia coli Curli Amyloid Fibrils is Mediated by Prion-like Peptide Repeats

Cited by 86 publications

References 37 publications

Curli Biogenesis and Function

Curli Biogenesis and Function

Structure of the nonameric bacterial amyloid secretion channel

Functional amyloid

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