6g8e: Difference between revisions
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CSGA_ECOLI CSGA_ECOLI]] Curlin is the structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin. | [[http://www.uniprot.org/uniprot/CSGA_ECOLI CSGA_ECOLI]] Curlin is the structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli can bind to fibronectin. | ||
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== Publication Abstract from PubMed == | |||
Curli amyloid fibrils secreted by Enterobacteriaceae mediate host cell adhesion and contribute to biofilm formation, thereby promoting bacterial resistance to environmental stressors. Here, we present crystal structures of amyloid-forming segments from the major curli subunit, CsgA, revealing steric zipper fibrils of tightly mated beta-sheets, demonstrating a structural link between curli and human pathological amyloids. D-enantiomeric peptides, originally developed to interfere with Alzheimer's disease-associated amyloid-beta, inhibited CsgA fibrillation and reduced biofilm formation in Salmonella typhimurium. Moreover, as previously shown, CsgA fibrils cross-seeded fibrillation of amyloid-beta, providing support for the proposed structural resemblance and potential for cross-species amyloid interactions. The presented findings provide structural insights into amyloidogenic regions important for curli formation, suggest a novel strategy for disrupting amyloid-structured biofilms, and hypothesize on the formation of self-propagating prion-like species originating from a microbial source that could influence neurodegenerative diseases. | |||
Structural Insights into Curli CsgA Cross-beta Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents.,Perov S, Lidor O, Salinas N, Golan N, Tayeb-Fligelman E, Deshmukh M, Willbold D, Landau M PLoS Pathog. 2019 Aug 30;15(8):e1007978. doi: 10.1371/journal.ppat.1007978., eCollection 2019 Aug. PMID:31469892<ref>PMID:31469892</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
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</StructureSection> | </StructureSection> | ||
