Journal:

Article Title: Complexes of Poliovirus Serotypes with Their Common Cellular Receptor, CD155

doi: 10.1128/JVI.77.8.4827-4835.2003

Figure Lengend Snippet: (a) Ribbon diagram of CD155 domain D1. Residues in the virus-receptor binding interfaces are shown as colored spheres. Residues identified as being in the interface in all three serotypes are shown in red, residues identified in two serotypes are shown in blue, and residues identified in only one serotype are shown in black. Secondary structure elements are identified by A, B, C, C′, C", D, E, F, and G. Residues are numbered at strategic positions. (b) CD155 residues in the virus-receptor binding interface. Residues are colored as in Fig. ​Fig.1a.1a. The residues that are important for receptor binding, as indicated by mutagenesis studies, are marked by “x” (6, 17) and “+” (9, 30, 34).

Article Snippet: An earlier atomic model of CD155 had been generated based on homology of the three different domains to immunoglobulin-like structures and on adjustment with respect to the then-available ∼22-Å resolution cryoEM density of CD155 complexed with PV1 ( 18 ) (PDB accession no. 1DGI ).

Techniques: Binding Assay, Mutagenesis

Journal:

Article Title: Complexes of Poliovirus Serotypes with Their Common Cellular Receptor, CD155

doi: 10.1128/JVI.77.8.4827-4835.2003

Figure Lengend Snippet: Stereoviews of cryoEM reconstructions of PV1, -2, and -3 complexed with glycosylated and fully deglycosylated CD155. Viral surfaces and CD155 are shown in gray and red, respectively. Resolutions of the different reconstructions are given in Table ​Table1.1. Also shown (bottom left) is an enlarged, surface-shaded representation of the icosahedral asymmetric unit showing the complex of glycosylated CD155 with PV1. At the bottom right is an explanation of the north and south notation used to describe the canyon topology.

Article Snippet: An earlier atomic model of CD155 had been generated based on homology of the three different domains to immunoglobulin-like structures and on adjustment with respect to the then-available ∼22-Å resolution cryoEM density of CD155 complexed with PV1 ( 18 ) (PDB accession no. 1DGI ).

Techniques:

Journal:

Article Title: Complexes of Poliovirus Serotypes with Their Common Cellular Receptor, CD155

doi: 10.1128/JVI.77.8.4827-4835.2003

Figure Lengend Snippet: Positions and significance of the glycosylation sites in difference maps

Article Snippet: An earlier atomic model of CD155 had been generated based on homology of the three different domains to immunoglobulin-like structures and on adjustment with respect to the then-available ∼22-Å resolution cryoEM density of CD155 complexed with PV1 ( 18 ) (PDB accession no. 1DGI ).

Techniques:

Journal:

Article Title: Complexes of Poliovirus Serotypes with Their Common Cellular Receptor, CD155

doi: 10.1128/JVI.77.8.4827-4835.2003

Figure Lengend Snippet: Fitting statistics of CD155 model into EM density

Article Snippet: An earlier atomic model of CD155 had been generated based on homology of the three different domains to immunoglobulin-like structures and on adjustment with respect to the then-available ∼22-Å resolution cryoEM density of CD155 complexed with PV1 ( 18 ) (PDB accession no. 1DGI ).

Techniques:

Journal:

Article Title: Complexes of Poliovirus Serotypes with Their Common Cellular Receptor, CD155

doi: 10.1128/JVI.77.8.4827-4835.2003

Figure Lengend Snippet: Stereoviews of superposition of the carbohydrate site difference densities obtained by subtracting the deglycosylated from the glycosylated CD155 densities. The carbohydrate densities are colored in red, green, and blue for those derived from the PV1, PV2, and PV3 complexes, respectively. The Cα backbone of CD155 is shown in black.

Article Snippet: An earlier atomic model of CD155 had been generated based on homology of the three different domains to immunoglobulin-like structures and on adjustment with respect to the then-available ∼22-Å resolution cryoEM density of CD155 complexed with PV1 ( 18 ) (PDB accession no. 1DGI ).

Techniques: Derivative Assay

Journal:

Article Title: Complexes of Poliovirus Serotypes with Their Common Cellular Receptor, CD155

doi: 10.1128/JVI.77.8.4827-4835.2003

Figure Lengend Snippet: r.m.s. deviation (Å) between C α atoms of the three-domain CD155 model when fitted into the various maps representing PV-CD155 complexes a

Article Snippet: An earlier atomic model of CD155 had been generated based on homology of the three different domains to immunoglobulin-like structures and on adjustment with respect to the then-available ∼22-Å resolution cryoEM density of CD155 complexed with PV1 ( 18 ) (PDB accession no. 1DGI ).

Techniques:

Journal:

Article Title: Complexes of Poliovirus Serotypes with Their Common Cellular Receptor, CD155

doi: 10.1128/JVI.77.8.4827-4835.2003

Figure Lengend Snippet: Footprints of CD155 on the surfaces of PV1 (top), PV2 (middle), and PV3 (bottom). Each figure is viewed in the same direction as those shown in Fig. ​Fig.2,2, which is down an icosahedral twofold axis. The viral residues in the footprints are colored according to their nearest approach to a CD155 atom. The projections of the pocket factor to the CD155 footprints are outlined with a dashed line. The relative position of the CD155 footprint in the viral asymmetric unit is shown at the top of each panel. Shown at the top right is a compass to explain the notation used to describe the parts of the canyon.

Article Snippet: An earlier atomic model of CD155 had been generated based on homology of the three different domains to immunoglobulin-like structures and on adjustment with respect to the then-available ∼22-Å resolution cryoEM density of CD155 complexed with PV1 ( 18 ) (PDB accession no. 1DGI ).

Techniques:

Journal:

Article Title: Complexes of Poliovirus Serotypes with Their Common Cellular Receptor, CD155

doi: 10.1128/JVI.77.8.4827-4835.2003

Figure Lengend Snippet: (a) Stereoviews of the carbohydrate difference density (red) of domain D1 and D2 of the PV1-CD155 complex. The deglycosylated CD155 density and the viral surface are shown in green and blue, respectively. (b) The Cα backbone of CD155 D1 is shown in black. The orientation of the canyon is marked as north, south, and east.

Article Snippet: An earlier atomic model of CD155 had been generated based on homology of the three different domains to immunoglobulin-like structures and on adjustment with respect to the then-available ∼22-Å resolution cryoEM density of CD155 complexed with PV1 ( 18 ) (PDB accession no. 1DGI ).

Techniques:

Journal:

Article Title: Complexes of Poliovirus Serotypes with Their Common Cellular Receptor, CD155

doi: 10.1128/JVI.77.8.4827-4835.2003

Figure Lengend Snippet: Model of receptor-mediated PV uncoating. The south wall of the canyon is probably responsible for forming the initial binding state of the PV-CD155 complex. The interaction between the north wall of the canyon and CD155 immediately above the hydrophobic binding pocket helps the release of the pocket factor, thus destabilizing the virus. Heating increases the structural “breathing” of the virus, thus providing the conformational change required for forming the “activated state” of the PV-CD155 complex.

Article Snippet: An earlier atomic model of CD155 had been generated based on homology of the three different domains to immunoglobulin-like structures and on adjustment with respect to the then-available ∼22-Å resolution cryoEM density of CD155 complexed with PV1 ( 18 ) (PDB accession no. 1DGI ).

Techniques: Binding Assay

Journal: PLoS ONE

Article Title: Receptors for Hyaluronic Acid and Poliovirus: A Combinatorial Role in Glioma Invasion?

doi: 10.1371/journal.pone.0030691

Figure Lengend Snippet: a–c , Co-staining of CD44 (red) and CD155 (green) on SNB-19 and UPAB cells; scale bars: 25 µm ( a ) and 10 µm ( b – c ). TIRF microscopy ( c ) clearly demonstrated the juxtaposition of CD44 and CD155. CD155 is mainly expressed on the processes and invadapodia (arrows). d , Significantly increased expression of CD44 ( top panel ) and CD155 ( bottom panel ) in GBM cells confirmed by flow cytometry, as assessed by the percentage of antigen-expressing cells and increase in fluorescence fold. * indicates statistical significance compared to CC-2565, a normal human astrocyte cell line.

Article Snippet: Blocking antibodies for CD44 (1∶100) and CD155 (1∶100) were obtained from Cambridge Biosciences.

Techniques: Staining, Microscopy, Expressing, Flow Cytometry, Fluorescence

Journal: PLoS ONE

Article Title: Receptors for Hyaluronic Acid and Poliovirus: A Combinatorial Role in Glioma Invasion?

doi: 10.1371/journal.pone.0030691

Figure Lengend Snippet: a , siRNA-KD of CD44 and CD155 was confirmed by Western blotting using both wild type ( wt ) and non-targeting siRNA treated cells as controls. GAPD-siRNA was used as a positive control to validate the knockdown effect. b , Expression of CD44 ( top panels ) and CD155 ( bottom panels ) in non-targeting siRNA treated cells ( control/left panels/L ) and relevant siRNA-KD ( right panels/R ) cells; scale bars: 25 µm. In control cells ( L ), CD44 is uniformly distributed with intense staining at the edges of the cells (arrows) whereas CD155 is well distributed with dense staining zones at the leading edges of the cells (arrows). CD44/CD155 staining was reduced in the siRNA-KD cells with clearly altered morphology ( R ). c , CD44/CD155-KD was confirmed by flow cytometry. Expression levels of CD44 and CD155 were significantly reduced in siRNA-KD SNB-19 cells as indicated by percentage of positive cells and fluorescence fold. * indicates statistical significance compared to non-targeting siRNA treated cells (control).

Article Snippet: Blocking antibodies for CD44 (1∶100) and CD155 (1∶100) were obtained from Cambridge Biosciences.

Techniques: Western Blot, Positive Control, Expressing, Staining, Flow Cytometry, Fluorescence

Journal: PLoS ONE

Article Title: Receptors for Hyaluronic Acid and Poliovirus: A Combinatorial Role in Glioma Invasion?

doi: 10.1371/journal.pone.0030691

Figure Lengend Snippet: Non-targeting siRNA treated SNB-19 cells were used as a control. a , Velocity of cell movement ( right panel ) with cell tracking ( left panel ) analysed over a period of 72 h. The speed by which CD44/CD155-KD cells moved was significantly reduced. b , Total distance moved by cells ( right panel ) with cell tracking ( left panel ) over a period of 72 h. The distance travelled by CD44/CD155-KD cells was markedly decreased. Start position: white arrow; end position: black arrow. * indicates statistical significance compared to control.

Article Snippet: Blocking antibodies for CD44 (1∶100) and CD155 (1∶100) were obtained from Cambridge Biosciences.

Techniques: Cell Tracking Assay

Journal: PLoS ONE

Article Title: Receptors for Hyaluronic Acid and Poliovirus: A Combinatorial Role in Glioma Invasion?

doi: 10.1371/journal.pone.0030691

Figure Lengend Snippet: a , Co-staining of F-actin (green/ left panels/L ) or β 1 -integrin (green/ right panels/R ) with CD44 (red/ top panels ) and CD155 (red/ bottom panels ) on wild type UPAB cells. b , Co-staining of α v β 1 -integrin (green/ L ) or α v β 3 -integrin (green/ R ) with CD44 (red/ top panels ) and CD155 (red/ bottom panels ) on wild type UPMC (CD44 staining) and non-targeting siRNA treated SNB-19 cells (CD155 staining). All images in a and b have scale bars of 25 µm. c , Western blotting showed reduced expression of F-actin and integrins (α v , β1 and β 3 ) in CD44/CD155-KD SNB-19 cells when compared to non-targeting siRNA treated cells (control).

Article Snippet: Blocking antibodies for CD44 (1∶100) and CD155 (1∶100) were obtained from Cambridge Biosciences.

Techniques: Staining, Western Blot, Expressing

Journal: PLoS ONE

Article Title: Receptors for Hyaluronic Acid and Poliovirus: A Combinatorial Role in Glioma Invasion?

doi: 10.1371/journal.pone.0030691

Figure Lengend Snippet: High levels of Cdc42, Rac 1/2/3, RhoA, RhoB and RhoC were detected in non-targeting siRNA treated SNB-19 cells (control) whereas those proteins of interest were downregulated in CD44/CD155-KD cells.

Article Snippet: Blocking antibodies for CD44 (1∶100) and CD155 (1∶100) were obtained from Cambridge Biosciences.

Techniques: