Cupric yersiniabactin is a virulence-associated superoxide dismutase mimic.
ACS Chem Biol
; 9(2): 551-61, 2014 Feb 21.
Article
en En
| MEDLINE
| ID: mdl-24283977
ABSTRACT
Many Gram-negative bacteria interact with extracellular metal ions by expressing one or more siderophore types. Among these, the virulence-associated siderophore yersiniabactin (Ybt) is an avid copper chelator, forming stable cupric (Cu(II)-Ybt) complexes that are detectable in infected patients. Here we show that Ybt-expressing E. coli are protected from intracellular killing within copper-replete phagocytic cells. This survival advantage is highly dependent upon the phagocyte respiratory burst, during which superoxide is generated by the NADPH oxidase complex. Chemical fractionation links this phenotype to a previously unappreciated superoxide dismutase (SOD)-like activity of Cu(II)-Ybt. Unlike previously described synthetic copper-salicylate (Cu(II)-SA) SOD mimics, the salicylate-based natural product Cu(II)-Ybt retains catalytic activity at physiologically plausible protein concentrations. These results reveal a new virulence-associated adaptation based upon spontaneous assembly of a non-protein catalyst.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Fenoles
/
Tiazoles
/
Sideróforos
/
Cobre
/
Escherichia coli
/
Interacciones Huésped-Patógeno
/
Macrófagos
Tipo de estudio:
Risk_factors_studies
Límite:
Animals
Idioma:
En
Revista:
ACS Chem Biol
Año:
2014
Tipo del documento:
Article
País de afiliación:
Estados Unidos