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
| Autor: | Séverine Loisel-Meyer, María Pilar Jiménez de Bagüés, Véronique Jubier-Maurin, Jean-Pierre Liautard |
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| Přispěvatelé: | Institut de Recherche en Infectiologie de Montpellier (IRIM), Université de Montpellier (UM)-Centre National de la Recherche Scientifique (CNRS) |
| Rok vydání: | 2006 |
| Předmět: |
Cytochrome
Brucella suis Immunology Ubiquinol oxidase MESH: Mice Inbred BALB C Microbiology Brucellosis Electron Transport Complex IV 03 medical and health sciences Mice MESH: Electron Transport Complex IV MESH: Brucellosis Cytochrome c oxidase Animals MESH: Animals MESH: Oxidoreductases MESH: Mice MESH: Brucella suis 030304 developmental biology 0303 health sciences Oxidase test Mice Inbred BALB C biology 030306 microbiology Macrophages MESH: Macrophages biology.organism_classification [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Molecular Pathogenesis 3. Good health Nitric oxide synthase Disease Models Animal Infectious Diseases Biochemistry biology.protein Parasitology MESH: Disease Models Animal Oxidoreductases Brucella melitensis |
| Zdroj: | Infection and Immunity Infection and Immunity, American Society for Microbiology, 2007, 75 (1), pp.531-5. ⟨10.1128/IAI.01185-06⟩ |
| ISSN: | 0019-9567 1098-5522 |
| DOI: | 10.1128/IAI.01185-06⟩ |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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