Expansion of the tuning range of injection-seeded terahertz-wave parametric generator up to 5 THz

In this paper, we report the improvement of the frequency tuning range of an injection-seeded terahertz (THz)-wave parametric generator (is-TPG). A significant previous limitation was the high absorption coefficient in the higher-frequency region of a MgO:LiNbO3 crystal. Here, we inclined the crystal slightly, so that a fraction of the pump beam was internally reflected at the THz-wave exit surface of the crystal. In this configuration, it was easier for a higher-frequency THz wave to reach the crystal surface, because the center core region of the pump beam was closer to the exit surface. As a result, the upper limit of the frequency tuning range increased from 3.0 to 5.0 THz.journal articl

高機能・環境に配慮した繊維材料およびその加工法に関する研究

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Recombinant FCR3-DBL5-6-ε depletes the adhesion blocking activity in goat serum.

<p><b>(A)</b> Goat Immunization with FCR3-DBL5-6-ε induces adhesion blocking antibodies. Goat purified IgG was tested for inhibition of FCR3-binding of PEs to BeWo and ScC2 cells in flow binding assays after the first boost, second boost and four weeks after the second boost. <b>(B)</b> Recombinant FCR3-DBL5-6-ε depletes the adhesion blocking activity. Goat purified IgG obtained four weeks after the second boost (D98) was depleted on immobilized FCR3-DBL5-6-ε. The inhibition of FCR3-PEs adhesion of IgG before antigen depletion, the depleted IgG, and elution of anti DBL5-6-ε were tested in flow binding assays using BeWo and ScC2 cells.</p

Expression and purification of recombinant var2CSA domains.

<p><b>(A)</b> Purification after refolding of FCR3 var2CSA DBL domains expressed in <i>E. coli</i>. Electrophoresis of purified DBL domains under reduced (+DTT) or non-reduced conditions on NuPAGE Novex 4–12% Bis-Tris gels, Coomasie bleu stained. Arrows indicate the expected proteins. <b>(B)</b> FCR3-DBL5-6-ε recombinant domain competes the adhesion of var2CSA expressing FCR3-PEs but fails to inhibit binding of FCR3^CD36 parasites on CD36 receptor. The adhesion of FCR3-PEs was tested in flow binding assays using ScC2 cells. FCR3-DBL5-6-ε recombinant protein inhibited FCR3^CSA parasite binding in a phenotype specific and dose-dependent manner.</p

Recombinant DBL5-ε, DBL6-ε, and DBL5-6-ε domains induce antibodies that block adhesion to BeWo cells in flow binding assays.

<p><b>(A)</b> Schematic representation of the binding inhibition assay mimicking the flow in placental physiological conditions <b>(B)</b> Inhibition of FCR3 PEs adhesion. Purified IgG at 0.5 mg/ml from a group of 5 mice immunized either with Freund or Alum as adjuvants were tested for inhibition of binding of FCR3-PEs to BeWo cells in flow binding assays. The numbers of bound PEs in the presence of IgG from preimmune serum was used as a reference value. The numbers of bound PEs for anti DBL IgG were used to calculate the binding inhibition as a percentage relative to the reference value. <b>(C)</b> and <b>(D)</b> Recombinant domains from heterologous parasites induce transcending adhesion blocking activity. Purified IgG at 0.5 mg/ml from groups of 5 mice immunized with heterologous DBL5-ε and DBL5-6-ε domains were tested for inhibition of binding of FCR3-PEs to BeWo and ScC2 cells in flow binding assays. Amino acid sequence identity percentages between the heterologous DBL domain and the homologous FCR3 DBL are presented.</p

Recognition of antigens expressed on the surface of PEs.

<p>Mouse and goat sera raised against DBL domains were assayed for their binding capacity to the surface of erythrocytoes infected with parasites of the FCR3 strain with CSA- and CD36-binding phenotypes. Analysis was performed using flow cytometry. Panels represent number of events (counts) against fluorescence (FITC) for each antiserum (doted line) when compared to the pre-immune serum (full line). FCR3^CSA parasite binding inhibition on BeWo cells are indicated for the respective antisera.</p

CSA is involved in IE interaction with human NK cell line but not in primary NK cell activation.

<p>(A) The human NK cell line NK92 was incubated with whole culture of IE in different conditions. After 1 h at 37°C, a sample of the co-culture was placed between slide and cover and analyzed under a microscope. The NK92 cells directly interacts with IE (FCR3-CSA strain) as rosettes, but not with uninfected erythrocytes (x100 original magnification, left panel). RBC infected with FCR3-CSA or 2A5 were co-cultured with NK92 cells alone or in the presence of soluble CSA (+CSA), or with NK92 cells pre-treated with chondroitinase ABC (+Case ABC). At the end of the co-culture, the percentage of NK cells interacting with at least two IE was determined and expressed as % of cytoadhesion. Each dot represents one independent experiment (right panel). (B) Freshly isolated human PBMC were cultured with uninfected RBC (RBC), RBC infected with FCR3-CSA or RBC infected with the <i>var2csa</i> KO parasite 2A5. After 24 h, NK cell activation was analyzed by flow cytometry by gating on CD3⁻CD56⁺ lymphocytes. The CD69 MFI (mean fluorescence intensity) staining on NK cells (left panel), the percentage of CD25⁺ NK cells (middle panel) and the percentage of IFN-γ⁺ NK cells (right panel) were determined for 7 different healthy donors. Means±SEM are represented. Statistical analyses were performed using the Wilcoxon test.</p

Deficiency in CD36 does not alter NK cell response to IE.

<p>(A) The level of CD36 expression was determined on PBMC collected from a healthy donor (Control donor) or from a patient deficient for CD36. Total PBMC protein extracts were prepared and analyzed by Western Blot (left panel). Total PBMC were stained with CD36 antibody or with an isotype control (filled grey histogram, right panel). Histograms for CD3⁻CD56⁺ NK cells from a CD36 deficient donor (dotted line) and a control donor (bold line) are represented. (B) Control or CD36-deficient PBMC were cultured with uninfected RBC (RBC, black bars), or with RBC infected with the 3D7 <i>Pf</i> strain (3D7, grey bars). After 24 h, NK cell activation was analyzed by flow cytometry by gating on CD3⁻CD56⁺ NK cells. The CD69 MFI staining on NK cells (left panel), the percentage of CD25⁺ NK cells (middle panel) and the percentage of IFN-γ⁺ NK cells (right panel) were determined in three independent experiments. Means ± SEM are represented. Statistical analyses were performed using the Mann Whitney test.</p

Expression of CSA, CD36 and ICAM-1 on human NK cells.

<p>Primary resting human NK cells (CD56⁺CD3⁻) in total PBMC as well as human NK cell lines, NK92 and NKL were analyzed by flow cytometry to determine the surface expression of three host ligands for PfEMP1: CSA (left panels, dark line), CD36 (middle panels, dark line) and ICAM-1 (right panels, dark line). Stainings with isotype control for each antibody are represented by filled grey histograms. Stainings of primary resting human NK cells are representative of at least 3 donors.</p

PfEMP1 deficient parasites are potent activators of NK cells.

<p>Human PBMC were cultured with uninfected RBC (RBC, black bars) or with RBC infected with the “PfEMP1 KO” strain DC-J. After 24 h, NK cell activation was analyzed by flow cytometry by gating on CD3⁻CD56⁺ NK cells. The CD69 MFI staining on NK cells (left panel), the percentage of CD25⁺ NK cells (middle panel) and the percentage of IFN-γ⁺ NK cells (right panel) were determined for 5 different healthy donors. Means±SEM are represented. Statistical analyses were performed using the Wilcoxon test.</p