Differential use of the two high-oxygen-affinity terminal oxidases of Brucella suis for in vitro and intramacrophagic multiplication.
Expression of the high-oxygen-affinity cytochrome cbb3 and cytochrome bd ubiquinol oxidases of Brucella suis was studied in vitro and in the intramacrophagic niche, which was previously proposed to be oxygen limited. The cytochrome cbb3 oxidase was exclusively expressed in vitro, whereas the cytochrome bd oxidase was preferentially used inside macrophages and contributed to intracellular bacterial replication.
Loisel-Meyer
Séverine
S
INSERM U-431, Université Montpellier II, Place E. Bataillon, CC100, 34095 Montpellier Cedex 05, France.
Jiménez de Bagüés
Maria Pilar
MP
Köhler
Stephan
S
Liautard
Jean-Pierre
JP
Jubier-Maurin
Véronique
V
D000332:Aerobiosis; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D041021:Brucella suis / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development*; D002460:Cell Line; D049109:Cell Proliferation; D003576:Electron Transport Complex IV / Q000235:genetics / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D006801:Humans; D008264:Macrophages / Q000378:metabolism / Q000382:microbiology*; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D010100:Oxygen / Q000378:metabolism*; D014158:Transcription, Genetic
D001426:Bacterial Proteins; D010088:Oxidoreductases; C414443:cbb3 oxidase; D003576:Electron Transport Complex IV; D010100:Oxygen