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Åberg, Veronica
Publikasjoner (1 av 1) Visa alla publikasjoner
Cegelski, L., Pinkner, J. S., Hammer, N. D., Cusumano, C. K., Hung, C. S., Chorell, E., . . . Hultgren, S. J. (2009). Small-molecule inhibitors target Escherichia coli amyloid biogenesis and biofilm formation. Nature Chemical Biology, 5(12), 913-919
Åpne denne publikasjonen i ny fane eller vindu >>Small-molecule inhibitors target Escherichia coli amyloid biogenesis and biofilm formation
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2009 (engelsk)Inngår i: Nature Chemical Biology, ISSN 1552-4450, EISSN 1552-4469, Vol. 5, nr 12, s. 913-919Artikkel i tidsskrift (Fagfellevurdert) Published
Abstract [en]

Curli are functional extracellular amyloid fibers produced by uropathogenic Escherichia coli (UPEC) and other Enterobacteriaceae. Ring-fused 2-pyridones, such as FN075 and BibC6, inhibited curli biogenesis in UPEC and prevented the in vitro polymerization of the major curli subunit protein CsgA. The curlicides FN075 and BibC6 share a common chemical lineage with other ring-fused 2-pyridones termed pilicides. Pilicides inhibit the assembly of type

1pili, which are required for pathogenesis during urinary tract infection. Notably, the curlicides retained pilicide activities and inhibited both curli-dependent and type 1–dependent biofilms. Furthermore, pretreatment of UPEC with FN075 significantly attenuated virulence in a mouse model of urinary tract infection. Curli and type 1pili exhibited exclusive and independent roles in promoting UPEC biofilms, and curli provided a fitness advantage in vivo. Thus, the ability of FN075 to block the biogenesis of both curli and type 1pili endows unique anti-biofilm and anti-virulence activities on these compounds.

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Nature Publishing Group, 2009
urn:nbn:se:umu:diva-26861 (URN)10.1038/nchembio.242 (DOI)
Published online 25 October 2009Tilgjengelig fra: 2009-10-29 Laget: 2009-10-29 Sist oppdatert: 2018-06-08bibliografisk kontrollert