Different roles of the two high-oxygen-affinity terminal oxidases of Brucella suis: Cytochrome c oxidase, but not ubiquinol oxidase, is required for persistence in mice

Infect Immun. 2007 Jan;75(1):531-5. doi: 10.1128/IAI.01185-06. Epub 2006 Nov 13.

Abstract

The survival of Brucella suis mutant strains in mice demonstrated different roles of the two high-oxygen-affinity terminal oxidases. The cbb3-type cytochrome c oxidase was essential for chronic infection in oxygen-deficient organs. Lack of the cytochrome bd ubiquinol oxidase led to hypervirulence of bacteria, which could rely on nitrite accumulation inhibiting the inducible nitric oxide synthase of the host.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brucella suis / enzymology
  • Brucella suis / pathogenicity*
  • Brucellosis / enzymology*
  • Disease Models, Animal
  • Electron Transport Complex IV / metabolism*
  • Macrophages / microbiology
  • Mice
  • Mice, Inbred BALB C
  • Oxidoreductases / metabolism*

Substances

  • Oxidoreductases
  • ubiquinol oxidase
  • Electron Transport Complex IV