Category:Team You cannot B. cereus

FIG. 6. AnkA-mCherry localized diffusely throughout the host cytoplasm.

FIG. 3. Multiple C. burnetii Anks are translocated into the host

cytosol in a Dot/Icm-dependent manner (AnkG).

FIG. 3. Multiple C. burnetii Anks are translocated into the host

cytosol in a Dot/Icm-dependent manner (AnkF).

FIG. 3. Multiple C. burnetii Anks are translocated into the host

cytosol in a Dot/Icm-dependent manner (AnkA).

Fig. 1. Virulence of B. melitensis 16M vjbR mutant.

(A) Intracellular replication of B. melitensis 16M NalR (WT), vjbR mutant (DvjbR or vjbR::mTn5) and complemented vjbR mutant (DvjbRc) in HeLa cells or bovine macrophages. Data (B) Intracellular growth phenotypes of WT, mutant vjbR and complemented mutant vjbR in bovine macrophages cells at 48 h p.i. (C) Accelerated clearance of the vjbR mutant from experimentally infected BALB/c mice.

Fig. 2. Cytosolic localization of HA-tagged RicA

Figure 3. TEM-b-lactamase-RicA translocation into RAW264.7 macrophages.

Fig. 4. VirB-independent secretion of 3Flag-RicA by B. abortus.

Figure 1. (B & D) The protein product of Bab1_1492 (SepA) is secreted during the infection of host cells.

Figure 2. Confocal analysis of the secretion of the protein product of Bab1_1492 (SepA) Figure 3. Secretion of SepA is a virB dependent process.

Figure 3. (A-D) BtpB (BAB1_0756) is translocated into host cells during infection.

BtpB (BAB1_0756); Figure 5. Modulation of NF-κB translocation to the nucleus during Brucella infection. BtpB mutant showed an increase translocation of NF-kB into the nucleus compared to those infected with Brucella WT.

Figure 7. Translocation of TEM1::VceA and TEM1::VceC into J774 macrophages. Cytosolic translocation of b-lactamase by wild type (2308) or virB2 mutant strain (ADH3) of B. abortus was assessed by fluorescence microscopy. Cells in which translocation of the fusion protein has occurred appear blue. Shows translocation of effector protein VceC (BR1038) from Brucella suis strain 1330 by VirB-T4SS.

Figure 8. Translocation of TEM1::VceA and TEM1::VceC into J774 macrophages at different time points after infection. Shows translocation of effector protein VceC (BAR1038) from Brucella suis strain 1330 by VirB-T4SS during Brucella abortus infection.

Figure 2C

Figure 1B

Figure 2A

Figure3

Figure 3

Figure 4

Figure 4B,C

Figure 2 Figure 4

Figure 6

Figure 1D

Figure 1E

Figure 1D

Figure 2. C. burnetii secretion substrates target distinct subcellular compartments when ectopically expressed in HeLa cells. Colocalization of Cbu0388 with the host cell nucleus could be demonstrated.

Figure 2B. C. burnetii secretion substrates target distinct subcellular compartments when ectopically expressed in HeLa cells. CbuA0020 colocalizes with the mitochondrial marker CoxIV (arrow indication).

Figure 2B. C. burnetii secretion substrates target distinct subcellular compartments when ectopically expressed in HeLa cells. Cbu1576 colocalization with the endoplasmic reticulum marker calnexin (arrow indication).

Figure 2B. C. burnetii secretion substrates target distinct subcellular compartments when ectopically expressed in HeLa cells. Cbu0372 colocalizes with

the endoplasmic reticulum marker calnexin (arrow indication)

Figure 6 and 7. Shows that VceC produces ER stress.

Figure 4. Localization of HA-VceC (BAB1_1058) fusions in HeLa cells (A to C) and RAW264.7 macrophages (D). Transfected cells grown on coverslips were stained with anti-calreticulin antibody (red) to visualize the ER (A, B, and D)or with phalloidin (red) to visualize the actin cytoskeleton (C). HA-VceC was visualized with anti-HA antibody (green). The images shown are representative of at least three independent experiments.

Figure 7. Translocation of TEM1::VceA and TEM1::VceC into J774 macrophages. Cytosolic translocation of b-lactamase by wild type (2308) or virB2 mutant strain (ADH3) of B. abortus was assessed by fluorescence microscopy. Cells in which translocation of the fusion protein has occurred appear blue. Shows translocation of effector protein VceA (BAB1_1652) by VirB-T4SS.

Figure 8. Translocation of TEM1::VceA and TEM1::VceC into J774 macrophages at different time points after infection. Shows translocation of effector protein VceA (BAB1_1652) by VirB-T4SS during Brucella abortus infection.

Figure 7. Translocation of TEM1::VceA and TEM1::VceC into J774 macrophages. Cytosolic translocation of b-lactamase by wild type (2308) or virB2 mutant strain (ADH3) of B. abortus was assessed by fluorescence microscopy. Cells in which translocation of the fusion protein has occurred appear blue. Shows translocation of effector protein VceC (BAB1_1058) by VirB-T4SS.

Figure 8. Translocation of TEM1::VceA and TEM1::VceC into J774 macrophages at different time points after infection. Shows translocation of effector protein VceC (BAB1_1058) by VirB-T4SS during Brucella abortus infection.

Figure 2. Effector proteins (BPE's) translocation into J774.A1. Shows translocation of BPE123 (BAB2_0123) into host cell.

Figure 3. VirB-dependent translocation of effector proteins (BPE's) into J774.A1 cells. Shows translocation of BPE123 (BAB2_0123) dependent on VirB-T4SS.

Figure 2. Effector proteins (BPE's) translocation into J774.A1. Shows translocation of BPE275 (BAB1_1275) into host cell.

Figure 3. VirB-dependent translocation of effector proteins (BPE's) into J774.A1 cells. Shows translocation of BPE275 (BAB1_1275) dependent on VirB-T4SS.

Figure 2. Effector proteins (BPE's) translocation into J774.A1. Shows translocation of BPE 159 (BAB2_0159) into host cell.

Figure 3. VirB-dependent translocation of effector proteins (BPE's) into J774.A1 cells. Shows translocation of BPE 159 (BAB2_0159) dependent on VirB-T4SS.

Figure 2. Effector proteins (BPE's) translocation into J774.A1. Shows translocation of BPE043 (BAB1_1043) into host cell.

Figure 3. VirB-dependent translocation of effector proteins (BPE's) into J774.A1 cells. Shows translocation of BPE043 (BAB1_1043) dependent on VirB-T4SS.

Figure 2. Effector proteins (BPE's) translocation into J774.A1. Shows translocation of BPE005 (BAB1_2005) into host cell.

Figure 3. VirB-dependent translocation of effector proteins (BPE's) into J774.A1 cells. Shows translocation of BPE005 (BAB1_2005) dependent on VirB-T4SS.

Figure 2. Effector proteins (BPE's) translocation into J774.A1. Shows translocation of BPE865 (BAB1_1865) into host cell.

Figure 3. VirB-dependent translocation of effector proteins (BPE's) into J774.A1 cells. Shows translocation of BPE865 (BAB1_1865) dependent on VirB-T4SS.

Figure 5

Figure 4

Figure 6

Figure 6b&c

Figure 2

cAMP-induced tyrosine phosphorylation of ERK2 in Ax2 cells

Figure 2: Fluorescence traces of refolding of RNase T1 (0.2 μM) at 10 °C starting from equilibrium-denatured protein (trace a) in the absence or presence of 0.5 nM (trace b), 2 nM (trace c), and 5 nM (trace d) FkpA (calculated for the dimer). The intensity at 323 nm was followed. Inset, the refolding curves were evaluated with a double exponential fit; and the rates of the faster refolding phase, divided by the uncatalyzed rate, are plotted against the respective FkpA concentration present during the measurement. arb., arbitrary.

Figure S1. Panel B and C shows that, when ectopically expressed in mammalian cells (HEK 293T), BAB2_0541 expression induces significant ER stress to levels similar or higher than a positive control VceC and upregulation of BiP, but not CHOP.

Figure S1. Panel B and C shows that, when ectopically expressed in mammalian cells (HEK 293T), BAB1_0227 expression induces significant ER stress to levels similar or higher than a positive control VceC and upregulation of BiP, but not CHOP.

Figure S1. Panel B and C shows that, when ectopically expressed in mammalian cells (HEK 293T), BAB1_0847 expression induces significant ER stress to levels similar or higher than a positive control VceC and upregulation of BiP, but not CHOP.

Figure 1. TEM1 b-lactamase protein translocation reporter assay. Shows translocation of effector protein BspF (BAB1_1948)

Figure 2. VirB-dependent translocation of Brucella BsP effectors into J774.A1 cells. Shows effector protein BspF (BAB1_01948) translocated by T4SS.

Figure 4. A subset of Bsp effectors target the host secretory pathway. Shows that effector protein BspF (BAB1_1948) targets secretory pathway by colocalization with calnexin a marker of ER.

Figure 5. Ectopic expression of BspF (BAB1_1948) in HeLa cells interferes with the host secretory pathway.

Figure 7. Contribution of BspF (BAB1_1948) to inhibition of host cell secretion during infection.

Figure 1. TEM1 b-lactamase protein translocation reporter assay.

Panel A and B shows percentage of shift in fluorescence emission that correlates with protein Brucella putative effector BAB1_1671 being translocated into 774A.1 host cell (murine cell line). Panel C and D shows representative fluorescence micrographs of protein translocation. Also look Figure S1 and S2.

Figure 2. VirB-dependent translocation of Brucella BsP effectors into J774.A1 cells.

Panel A. B. abortus strain 2308 (black bars) or virB9 mutant strain (white bars) expressing the CyaA fusions to the indicated Brucella effector proteins were used to infect J774.A1 cells, and the cAMP level of infected cells was determined.

Figure 1. TEM1 b-lactamase protein translocation reporter assay.

Panel A and B shows percentage of shift in fluorescence emission that correlates with protein Brucella putative effector BAB1_0847 being translocated into J774A.1 host cell (murine cell line). Panel C and D shows representative fluorescence micrographs of protein translocation. Also look Figure S1 and S2.

Figure 2. VirB-dependent translocation of Brucella BsP effectors into J774.A1 cells.

Panel A. B. abortus strain 2308 (black bars) or virB9 mutant strain (white bars) expressing the CyaA fusions to the indicated Brucella effector proteins were used to infect J774.A1 cells, and the cAMP level of infected cells was determined.

Figure 2. VirB-dependent translocation of Brucella BsP effectors into J774.A1 cells. Shows effector protein BspA (BAB1_0678) translocated by T4SS.

Figure 7. Contribution of BspA (BAB1_0678) to inhibition of host cell secretion during infection.

Figure 2. VirB-dependent translocation of Brucella BsP effectors into J774.A1 cells. Shows effector protein BspB (BAB1_0712) translocated by T4SS.

Figure 7. Contribution of BspB (BAB1_0712) to inhibition of host cell secretion during infection.

Figure 4B,C

Figure 2

Figure 3. Confocal micrographs of HeLa cells transfected with Brucella abortus effector protein BspC expressing GFP displayed a golgi apparatus localization.

Figure 4. Shows co-localization of BspC with a protein resident in golgi GM130 that confirmed BspC golgi localization.

Figure 3. Confocal micrographs of HeLa cells transfected with Brucella abortus effector protein BspK expressing hemagglutinin displayed a ER localization.

Figure 4. Shows co-localiztion of BspK with ER-resident chaperone, calnexin that confirmed its ER localization.

Figure 3. Confocal micrographs of HeLa cells transfected with Brucella abortus effector protein BspD expressing GFP displayed a ER localization.

Figure 4. Shows co-localization of BspD with ER-resident chaperon, calnexin confirming its localization.

Figure 3. Confocal micrographs of HeLa cells transfected with Brucella abortus effector protein BspB expressing hemagglutinin displayed a localization in the ER.

Figure 4. Shows co_localization of BspB with ER-resident chaperone protein calnexin confirmed its ER localization.

Figure 3. Confocal micrographs of HeLa cells transfected with Brucella abortus effector protein BspF expressing hemagglutinin displayed a host plasma membrane localization.

Figure 3. Confocal micrographs of HeLa cells transfected with Brucella abortus effector protein BspF expressing hemagglutinin displayed a cytosol localization

Figure 3. Confocal micrographs of HeLa cells transfected with Brucella abortus effector protein BspI expressing hemagglutinin displayed cytosolic localization.

Figure 3. Confocal micrgraphs of HeLa transfected cells with Brucella abortus effector proten BspH expressing hemagglutinin display a cytosolic localization

Figure 3. Confocal micrographs of HeLa cells transfected with Brucella abortus effector protein BspA expressing GFP. BspA localizes in the host ER.

Figure 4. Shows co-localization of BspA with ER resident chaperone protein calnexin.

Figure 3. Confocal micrographs of HeLa cells transfected with Brucella abortus effector protein BspE labeled with HA. BspE was observed forming discrete vesicles in the perinuclear area.

Figure 1B and 1C

Pyruvate kinase activity of TEFpr-PYK1 and CYCpr-PYK1.

TEFpr is a strong promotor, CYCpr is a weak promotor.

Figure 1B and C

Pyruvate kinase activity of TEFpr-PYK2 and CYCpr-PYK2. TEFpr is a strong promotor, CYCpr is a weak promotor.

Figure 5B

Cells with low PYK activity have increased concentrations of PPP intermediates

Figure 5B

Cells with low PYK activity have increased concentrations of PPP intermediates

Figure 4B and 5C