Véronique Jubier-Maurin
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Previous Organizations / Institutes
The organizations / institutes from the scholar's other articles in the past ten years
Research Subjects
Research Interests
Véronique Jubier-Maurin has a total of 15 co-authors. Here are the top co-authors by number of shared publications:
Jean-Pierre Liautard
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
3 shared publications- María Pilar Jiménez de Bagüés
Unidad de Tecnología en Producción y Sanidad Animal, Centro de Investigación y Tecnología Agroalimentaria, Instituto Agroalimentario de Aragón, Universidad de Zaragoza, Zaragoza, Spain
3 shared publications Séverine Loisel-Meyer
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
2 shared publications- Stephan Köhler
Institut National de la Santé et de la Recherche Médicale U-431, Université Montpellier II, F-34095 Montpellier, France
2 shared publications Alan S. Cross
Center for Vaccine Development
1 shared publicationEugénIe BassèrEs
Institut National de la Santé et de la Recherche Médicale, U431, Université Montpellier II, Montpellier, F-34095 France
1 shared publication
Latest Publications
- 1 January 2007
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 75 (1) , 531-535
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
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.
- 1 January 2007
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 75 (1) , 531-535
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
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.
- Open Access
- 1 March 2006
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 74 (3) , 1973-1976
Requirement of norD for Brucella suis Virulence in a Murine Model of In Vitro and In Vivo Infection
A mutant of Brucella suis bearing a Tn 5 insertion in norD , the last gene of the operon norEFCBQD , encoding nitric oxide reductase, was unable to survive under anaerobic denitrifying conditions. The norD strain exhibited attenuated multiplication within nitric oxide-producing murine macrophages and rapid elimination in mice, hence demonstrating that norD is essential for Brucella virulence.
- 1 March 2006
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 74 (3) , 1973-1976
Open AccessRequirement of norD for Brucella suis Virulence in a Murine Model of In Vitro and In Vivo Infection
A mutant of Brucella suis bearing a Tn 5 insertion in norD , the last gene of the operon norEFCBQD , encoding nitric oxide reductase, was unable to survive under anaerobic denitrifying conditions. The norD strain exhibited attenuated multiplication within nitric oxide-producing murine macrophages and rapid elimination in mice, hence demonstrating that norD is essential for Brucella virulence.
- Open Access
- 1 November 2005
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 73 (11) , 7495-7501
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.
- 1 November 2005
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 73 (11) , 7495-7501
Open AccessDifferential 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.