Bryan H. Bellaire

The Siderophore 2,3-Dihydroxybenzoic Acid Is Not Required for Virulence of Brucella abortus in BALB/c Mice

Bellaire, Bryan H., Elzer, Philip H., Baldwin, Cynthia L., Roop, R. Martin

2,3-Dihydroxybenzoic acid (DHBA) is the only siderophore described for Brucella, and previous studies suggested that DHBA might contribute to the capacity of these organisms to persist in host...

Genetic Organization and Iron-Responsive Regulation of the Brucella abortus 2,3-Dihydroxybenzoic Acid Biosynthesis Operon, a Cluster of Genes Required for Wild-Type Virulence in Pregnant Cattle

Bellaire, Bryan H., Elzer, Philip H., Hagius, Sue, Walker, Joel, Baldwin, Cynthia L., Roop II, R. Martin

Brucella abortus reportedly produces the monocatechol siderophore 2,3-dihydroxybenzoic acid (2,3-DHBA) in response to iron limitation. Nucleotide sequence analysis of the cloned DHBA biosynthesis...

Production of the Siderophore 2,3-Dihydroxybenzoic Acid Is Required for Wild-Type Growth of Brucella abortus in the Presence of Erythritol under Low-Iron Conditions In Vitro

Bellaire, Bryan H., Elzer, Philip H., Baldwin, Cynthia L., Roop II, R. Martin

Production of the siderophore 2,3-dihyroxybenzoic acid (2,3-DHBA) is required for the wild-type virulence of Brucella abortus in cattle. A possible explanation for this requirement was uncovered when...

Opsonized Virulent Brucella abortus Replicates within Nonacidic, Endoplasmic Reticulum-Negative, LAMP-1-Positive Phagosomes in Human Monocytes

Bellaire, Bryan H, Roop, R. Martin, Cardelli, James A.

Cells in the Brucella spp. are intracellular pathogens that survive and replicate within host monocytes. Brucella maintains persistent infections in animals despite the production of high levels of...

GLUT1CBP(TIP2/GIPC1) Interactions with GLUT1 and Myosin VI: Evidence Supporting an Adapter Function for GLUT1CBPV⃞

Reed, Brent C., Cefalu, Christopher, Bellaire, Bryan H., Cardelli, James A., Louis, Thomas, Salamon, Joanna, ...

We identified a novel interaction between myosin VI and the GLUT1 transporter binding protein GLUT1CBP(GIPC1) and first proposed that as an adapter molecule it might function to couple vesicle-bound...

RecA and RadA Proteins of Brucella abortus Do Not Perform Overlapping Protective DNA Repair Functions following Oxidative Burst

Roux, Christelle M., Booth, Natha J., Bellaire, Bryan H., Gee, Jason M., Roop, R. Martin, Kovach, Michael E., ...

Very little is known about the role of DNA repair networks in Brucella abortus and its role in pathogenesis. We investigated the roles of RecA protein, DNA repair, and SOS regulation in B. abortus....

The Siderophore 2,3-Dihydroxybenzoic Acid Is Not Required for Virulence of Brucella abortus in BALB/c Mice

Bellaire, Bryan H., Elzer, Philip H., Baldwin, Cynthia L., Roop, R. Martin

2,3-Dihydroxybenzoic acid (DHBA) is the only siderophore described for Brucella, and previous studies suggested that DHBA might contribute to the capacity of these organisms to persist in host...

Genetic Organization and Iron-Responsive Regulation of the Brucella abortus 2,3-Dihydroxybenzoic Acid Biosynthesis Operon, a Cluster of Genes Required for Wild-Type Virulence in Pregnant Cattle

Bellaire, Bryan H., Elzer, Philip H., Hagius, Sue, Walker, Joel, Baldwin, Cynthia L., Roop II, R. Martin

Brucella abortus reportedly produces the monocatechol siderophore 2,3-dihydroxybenzoic acid (2,3-DHBA) in response to iron limitation. Nucleotide sequence analysis of the cloned DHBA biosynthesis...

Production of the Siderophore 2,3-Dihydroxybenzoic Acid Is Required for Wild-Type Growth of Brucella abortus in the Presence of Erythritol under Low-Iron Conditions In Vitro

Bellaire, Bryan H., Elzer, Philip H., Baldwin, Cynthia L., Roop II, R. Martin

Production of the siderophore 2,3-dihyroxybenzoic acid (2,3-DHBA) is required for the wild-type virulence of Brucella abortus in cattle. A possible explanation for this requirement was uncovered when...

Opsonized Virulent Brucella abortus Replicates within Nonacidic, Endoplasmic Reticulum-Negative, LAMP-1-Positive Phagosomes in Human Monocytes

Bellaire, Bryan H, Roop, R. Martin, Cardelli, James A.

Cells in the Brucella spp. are intracellular pathogens that survive and replicate within host monocytes. Brucella maintains persistent infections in animals despite the production of high levels of...

GLUT1CBP(TIP2/GIPC1) Interactions with GLUT1 and Myosin VI: Evidence Supporting an Adapter Function for GLUT1CBPV⃞

Reed, Brent C., Cefalu, Christopher, Bellaire, Bryan H., Cardelli, James A., Louis, Thomas, Salamon, Joanna, ...

We identified a novel interaction between myosin VI and the GLUT1 transporter binding protein GLUT1CBP(GIPC1) and first proposed that as an adapter molecule it might function to couple vesicle-bound...

RecA and RadA Proteins of Brucella abortus Do Not Perform Overlapping Protective DNA Repair Functions following Oxidative Burst

Roux, Christelle M., Booth, Natha J., Bellaire, Bryan H., Gee, Jason M., Roop, R. Martin, Kovach, Michael E., ...

Very little is known about the role of DNA repair networks in Brucella abortus and its role in pathogenesis. We investigated the roles of RecA protein, DNA repair, and SOS regulation in B. abortus....

The β1 Integrin Activates JNK Independent of CagA, and JNK Activation Is Required for Helicobacter pylori CagA+-induced Motility of Gastric Cancer Cells*S⃞

Snider, Jared L., Allison, Cody, Bellaire, Bryan H., Ferrero, Richard L., Cardelli, James A.

The Helicobacter pylori CagA protein is translocated into gastric epithelial cells through a type IV secretion system (TFSS), and published studies suggest CagA is critical for H. pylori-associated...