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Infection and Immunity, January 2007, p. 531-535, Vol. 75, No. 1
0019-9567/07/$08.00+0     doi:10.1128/IAI.01185-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

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{triangledown}

Maria Pilar Jiménez de Bagüés,3 Séverine Loisel-Meyer,1,2,{dagger} Jean-Pierre Liautard,1,2 and Véronique Jubier-Maurin1,2*

Institut National de la Santé et de la Recherche Médicale, U431, Montpellier, F-34095 France,1 Université Montpellier II, Montpellier, F-34095 France,2 Unidad de Sanidad Animal, CITA, Gobierno de Aragon, AP. 727, 50080 Zaragoza, Spain3

Received 28 July 2006/ Returned for modification 22 September 2006/ Accepted 11 October 2006

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.

* Corresponding author. Mailing address: INSERM U-431, Université Montpellier II, Place E. Bataillon, CC100, 34095 Montpellier Cedex 05, France. Phone: (33) 4 67 14 42 38. Fax: (33) 4 67 14 33 38. E-mail: v-maurin{at}univ-montp2.fr.

{triangledown} Published ahead of print on 13 November 2006.

Editor: D. L. Burns

{dagger} Present address: University Health Network, Canadian Blood Services, Toronto, ON M5G 2M1, Canada.

Infection and Immunity, January 2007, p. 531-535, Vol. 75, No. 1
0019-9567/07/$08.00+0     doi:10.1128/IAI.01185-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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