4541.08), by ARC fellowship (Actions
de Recherche Concertée, conventions 04/09-325 and 08/13-015, French-Speaking Community of Belgium) and by the University of Namur (FUNDP). D. Dotreppe and C. Mullier were holding a Ph.D. fellowship from the FRIA (Fonds pour la formation à la Recherche dans l’Industrie et dans l’Agriculture). Electronic supplementary material Additional file 1: Sequence GDC-0994 nmr alignment between E. coli and B. MI-503 supplier abortus AidB. Alignment of E. coli and B. abortus AidB highlighting the conserved parts of these enzymes, and the absence of high similarity in the C-terminal portion of these proteins. (DOC 28 KB) Additional file 2: 3D structure of E. coli AidB and 3D model of B. abortus AidB. The 3D model of B. abortus AidB suggests that while regions involved in tetramer formation VRT752271 mouse are conserved, the C-terminal domain involved in DNA binding is not conserved. (DOC 2 MB) Additional file 3: Infection
of RAW264.7 macrophages with wild-type and aidB mutants strains. c.f.u. countings during macrophages infection show that aidB mutation or overexpression does not dramatically impair intracellular survival and replication of B. abortus. (DOC 363 KB) References 1. Boschiroli ML, Foulongne V, O’Callaghan D: Brucellosis: a worldwide zoonosis. Curr Opin Microbiol 2001, 4:58–64.PubMedCrossRef 2. Gorvel JP, Moreno E: Brucella intracellular life: from invasion to intracellular replication. Vet Microbiol 2002, 90:281–297.PubMedCrossRef 3. Arenas GN, Staskevich AS, Aballay A, Mayorga LS: Intracellular trafficking of Brucella abortus in J774 macrophages. Infect Immun 2000,
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