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000872752 1001_ $$0P:(DE-HGF)0$$aPerov, Sergei$$b0
000872752 245__ $$aStructural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents
000872752 260__ $$aLawrence, Kan.$$bPLoS$$c2019
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000872752 520__ $$aCurli 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 β-sheets, demonstrating a structural link between curli and human pathological amyloids. D-enantiomeric peptides, originally developed to interfere with Alzheimer's disease-associated amyloid-β, inhibited CsgA fibrillation and reduced biofilm formation in Salmonella typhimurium. Moreover, as previously shown, CsgA fibrils cross-seeded fibrillation of amyloid-β, 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
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000872752 7001_ $$00000-0001-6392-4647$$aLidor, Ofir$$b1
000872752 7001_ $$00000-0002-3511-2243$$aSalinas, Nir$$b2
000872752 7001_ $$00000-0001-5064-0776$$aGolan, Nimrod$$b3
000872752 7001_ $$0P:(DE-HGF)0$$aTayeb- Fligelman, Einav$$b4
000872752 7001_ $$00000-0002-3704-3229$$aDeshmukh, Maya$$b5
000872752 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b6
000872752 7001_ $$00000-0002-1743-3430$$aLandau, Meytal$$b7$$eCorresponding author
000872752 773__ $$0PERI:(DE-600)2205412-1$$a10.1371/journal.ppat.1007978$$gVol. 15, no. 8, p. e1007978 -$$n8$$pe1007978 -$$tPLoS pathogens$$v15$$x1553-7374$$y2019
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