The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
The curli nucleator protein, CsgB, contains an amyloidogenic domain that directs CsgA polymerization
Open accessAbstract
Curli are functional amyloid fibers assembled by enteric bacteria such as Escherichia coli and Salmonella spp. In E. coli , the polymerization of the major curli fiber subunit protein CsgA into an amyloid fiber depends on the minor curli subunit protein, CsgB. The outer membrane-localized CsgB protein shares ≈30% sequence identity with the amyloid-forming protein CsgA, suggesting that CsgB might also have amyloidogenic properties. Here, we characterized the biochemical properties of CsgB and the molecular basis for CsgB-mediated nucleation of CsgA. Deletion analysis revealed that a CsgB molecule missing 19 amino acids from its C terminus (CsgB trunc ) was not outer membrane-associated, but secreted away from the cell. CsgB trunc was overexpressed and purified from the extracellular milieu of cells as an SDS-soluble, nonaggregated protein. Soluble CsgB trunc assembled into fibers that bound to the amyloid-specific dyes Congo red and thioflavin-T. CsgB trunc fibers were able to seed soluble CsgA polymerization in vitro . CsgB trunc displayed modest nucleator activity in vivo , as demonstrated by its ability to convert extracellular CsgA into an amyloid fiber. Unlike WT CsgB, CsgB trunc was only able to act as a nucleator when cells were genetically manipulated to secrete higher concentrations of CsgA. This work represents a unique demonstration of functional amyloid nucleation and it suggests an elegant model for how E. coli guides efficient amyloid fiber formation on the cell surface.
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
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Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
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Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation
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Self-citationAmyloid pores from pathogenic mutations
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Lucin, K. M., & Wyss-Coray, T. (2009) · Neuron · doi:10.1016/j.neuron.2009.08.039 · Cited by 679
Hobley, L., Harkins, C., MacPhee, C. E., & Stanley-Wall, N. R. (2015) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuv015 · Cited by 581
“Overexpression of CsgG re-sultsinerythromycinsensitivityofthecells,butnotvancomycin sensitivityorgrowthdefectsintheabsenceofantibiotics,revealing that overexpressed CsgG forms discrete pores in the membrane and does not cause a general loss of membrane integrity (Robinson et al. 2006).”
BackgroundThe role of microbial amyloid in neurodegeneration
Friedland, R. P., & Chapman, M. R. (2017) · PLOS Pathogens · doi:10.1371/journal.ppat.1006654 · Cited by 391
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Metadata
- Authors
- Hammer, N. D., Schmidt, J. C., & Chapman, M. R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2007-07-24
- Volume
- 104
- Issue
- 30
- Pages
- 12494-12499
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1969465952
- Cited by
- 282
- References
- 49
- FWCI
- 4.50
- Type
- journal article
- Language
- en
- Open access
- green
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