ArticleProceedings of the National Academy of Sciences of the United States of America2012
The E. coli CsgB nucleator of curli assembles to β-sheet oligomers that alter the CsgA fibrillization mechanism.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
38 citing papers in PubMed, 73 citations in OpenAlex.
- Structural and Functional Characterization of Protein Adhesins and Pili in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Article
- Selective inhibition of the amyloid matrix of Escherichia coli biofilms by a bifunctional microbial metabolite.NPJ biofilms and microbiomes · 2023Article
- Cell surface-localized CsgF condensate is a gatekeeper in bacterial curli subunit secretion.Nature communications · 2023Article
- Protein-Based Biological Materials: Molecular Design and Artificial Production.Chemical reviews · 2023Review
- Survival and Virulence Potential of Drug-ResistantInternational journal of environmental research and public health · 2022Article
- Bacterial biofilm functionalization through Bap amyloid engineering.NPJ biofilms and microbiomes · 2022Article
- Functional amyloids from bacterial biofilms - structural properties and interaction partners.Chemical science · 2022Review
- Gram-negative bacteria and their lipopolysaccharides in Alzheimer's disease: pathologic roles and therapeutic implications.Translational neurodegeneration · 2021Review
- Variability of Amyloid Propensity in Imperfect Repeats of CsgA Protein ofInternational journal of molecular sciences · 2021Article
- Accelerated Amyloid Beta Pathogenesis by Bacterial Amyloid FapC.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2020Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- NMR insights into the pre-amyloid ensemble and secretion targeting of the curli subunit CsgA.Scientific reports · 2020Article
- Bacterial functional amyloids: Order from disorder.Biochimica et biophysica acta. Proteins and proteomics · 2019Review
- Congo Red Fluorescence for RapidApplied and environmental microbiology · 2019Article
- Directing curli polymerization with DNA origami nucleators.Nature communications · 2019Article
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- Article
- Propolis potentiates the effect of cranberry (Vaccinium macrocarpon) against the virulence of uropathogenic Escherichia coli.Scientific reports · 2018Article
- Multitasking of Hsp70 chaperone in the biogenesis of bacterial functional amyloids.Communications biology · 2018Article
- Electrostatic lipid-protein interactions sequester the curli amyloid fold on the lipopolysaccharide membrane surface.The Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Curli are extracellular proteinaceous functional amyloid aggregates produced by Escherichia coli, Salmonella spp., and other enteric bacteria. Curli mediate host cell adhesion and invasion and play a critical role in biofilm formation. Curli filaments consist of CsgA, the major subunit, and CsgB, the minor subunit. In vitro, purified CsgA and CsgB exhibit intrinsically disordered properties, and both are capable of forming amyloid fibers similar in morphology to those formed in vivo. However, in vivo, CsgA alone cannot form curli fibers, and CsgB is required for filament growth. Thus, we studied the aggregation of CsgA and CsgB both alone and together in vitro to investigate the different roles of CsgA and CsgB in curli formation. We found that though CsgA and CsgB individually are able to self-associate to form aggregates/fibrils, they do so using different mechanisms and with different kinetic behavior. CsgB rapidly forms structured oligomers, whereas CsgA aggregation is slower and appears to proceed through large amorphous aggregates before forming filaments. Substoichiometric concentrations of CsgB induce a change in the mechanism of CsgA aggregation from that of forming amorphous aggregates to that of structured intermediates similar to those of CsgB alone. Oligomeric CsgB accelerated the aggregation of CsgA, in contrast to monomeric CsgB, which had no effect. The structured β-strand oligomers formed by CsgB serve as nucleators for CsgA aggregation. These results provide insights into the formation of curli in vivo, especially the nucleator function of CsgB.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.