concanavalin a Search Results


98
Thermo Fisher lectins
A. Principal component analysis (PCA) of lectin-binding intensities in Cladocopium (orange, N = 18) and Durusdinium (blue, N = 30) symbionts isolated from coral eggs. B. PCA of lectin-binding intensities in Cladocopium and Durusdinium symbionts isolated from parental colonies ( N = 15 and N = 18, respectively). C. PCA of lectin-binding intensities in Cladocopium symbionts isolated from coral eggs (circles) and parental colonies (triangles) pairs ( N = 15). D. PCA of lectin-binding intensities in Durusdinium symbionts isolated from coral eggs and parental colony pairs ( N = 18). In A-D, vectors represent the contribution of individual <t>lectins</t> to the ordination. Ellipses represent the 95% confidence intervals around group centroids. Group separations were statistically significant (PERMANOVA P = 0.001). Asterisks denote adjusted P values (* P < 0.05, ** P < 0.01, *** P < 0.001). E. Partial least squares discriminant analysis (PLS-DA) of each lectin-binding intensity profile for symbionts in eggs and parents. <t>Lectins:</t> <t>ConA</t> (concanavalin A, specific for D-mannose and D-glucose), LTL ( Lotus tetragonolobus lectin, specific for L-fucose), PNA ( Arachis hypogaea lectin, specific for D-galactose), WGA (wheat germ agglutinin, specific for N-acetylglucosamine and N-acetylneuraminic acid), PHA-L (phytohemagglutinin-L from Phaseolus vulgaris , specific for N-acetylglucosamine β(1-2) mannopyranosyl) and GS-IB4 (isolectin from Griffonia simplicifolia , specific for N-acetyl-D-galactosamine and a-D-galactosyl residues).
Lectins, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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95
EpiCypher beads
A. Principal component analysis (PCA) of lectin-binding intensities in Cladocopium (orange, N = 18) and Durusdinium (blue, N = 30) symbionts isolated from coral eggs. B. PCA of lectin-binding intensities in Cladocopium and Durusdinium symbionts isolated from parental colonies ( N = 15 and N = 18, respectively). C. PCA of lectin-binding intensities in Cladocopium symbionts isolated from coral eggs (circles) and parental colonies (triangles) pairs ( N = 15). D. PCA of lectin-binding intensities in Durusdinium symbionts isolated from coral eggs and parental colony pairs ( N = 18). In A-D, vectors represent the contribution of individual <t>lectins</t> to the ordination. Ellipses represent the 95% confidence intervals around group centroids. Group separations were statistically significant (PERMANOVA P = 0.001). Asterisks denote adjusted P values (* P < 0.05, ** P < 0.01, *** P < 0.001). E. Partial least squares discriminant analysis (PLS-DA) of each lectin-binding intensity profile for symbionts in eggs and parents. <t>Lectins:</t> <t>ConA</t> (concanavalin A, specific for D-mannose and D-glucose), LTL ( Lotus tetragonolobus lectin, specific for L-fucose), PNA ( Arachis hypogaea lectin, specific for D-galactose), WGA (wheat germ agglutinin, specific for N-acetylglucosamine and N-acetylneuraminic acid), PHA-L (phytohemagglutinin-L from Phaseolus vulgaris , specific for N-acetylglucosamine β(1-2) mannopyranosyl) and GS-IB4 (isolectin from Griffonia simplicifolia , specific for N-acetyl-D-galactosamine and a-D-galactosyl residues).
Beads, supplied by EpiCypher, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Cell Signaling Technology Inc concanavalin a cona beads
A. Principal component analysis (PCA) of lectin-binding intensities in Cladocopium (orange, N = 18) and Durusdinium (blue, N = 30) symbionts isolated from coral eggs. B. PCA of lectin-binding intensities in Cladocopium and Durusdinium symbionts isolated from parental colonies ( N = 15 and N = 18, respectively). C. PCA of lectin-binding intensities in Cladocopium symbionts isolated from coral eggs (circles) and parental colonies (triangles) pairs ( N = 15). D. PCA of lectin-binding intensities in Durusdinium symbionts isolated from coral eggs and parental colony pairs ( N = 18). In A-D, vectors represent the contribution of individual <t>lectins</t> to the ordination. Ellipses represent the 95% confidence intervals around group centroids. Group separations were statistically significant (PERMANOVA P = 0.001). Asterisks denote adjusted P values (* P < 0.05, ** P < 0.01, *** P < 0.001). E. Partial least squares discriminant analysis (PLS-DA) of each lectin-binding intensity profile for symbionts in eggs and parents. <t>Lectins:</t> <t>ConA</t> (concanavalin A, specific for D-mannose and D-glucose), LTL ( Lotus tetragonolobus lectin, specific for L-fucose), PNA ( Arachis hypogaea lectin, specific for D-galactose), WGA (wheat germ agglutinin, specific for N-acetylglucosamine and N-acetylneuraminic acid), PHA-L (phytohemagglutinin-L from Phaseolus vulgaris , specific for N-acetylglucosamine β(1-2) mannopyranosyl) and GS-IB4 (isolectin from Griffonia simplicifolia , specific for N-acetyl-D-galactosamine and a-D-galactosyl residues).
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93
Santa Cruz Biotechnology concanavalin a cona
Purified CD4 + T cells were added to 24-well plates and incubated in RPMI alone or in RPMI containing G-CSF or G-CSF plus <t>ConA</t> for 24 h. (A) The expression of G-CSFR on CD4 + T cells, evaluated by CD114 staining. (B) The percentage of G-CSFR is summarized in the graph (n=5 per group). After incubation 24h, G-CSF stimulated or left un-stimulated CD4 + T cells were transferred to 96-well plates coated with ICAM-1 and anti-CD3. (C) Cell morphology was examined by fluorescence microscopy at 60 minutes. Arrows indicate polarized T cells with a clear uropod. (D) Cells prepared as in C were quantified. (E) Unbound cells were washed off, and the adherent cells were quantified using a CCK-8 assay kit. The data are represented as the mean ± SD (n=15 per group). * P < 0.05; *** P < 0.001.
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94
Vazyme Biotech Co cona beads
Purified CD4 + T cells were added to 24-well plates and incubated in RPMI alone or in RPMI containing G-CSF or G-CSF plus <t>ConA</t> for 24 h. (A) The expression of G-CSFR on CD4 + T cells, evaluated by CD114 staining. (B) The percentage of G-CSFR is summarized in the graph (n=5 per group). After incubation 24h, G-CSF stimulated or left un-stimulated CD4 + T cells were transferred to 96-well plates coated with ICAM-1 and anti-CD3. (C) Cell morphology was examined by fluorescence microscopy at 60 minutes. Arrows indicate polarized T cells with a clear uropod. (D) Cells prepared as in C were quantified. (E) Unbound cells were washed off, and the adherent cells were quantified using a CCK-8 assay kit. The data are represented as the mean ± SD (n=15 per group). * P < 0.05; *** P < 0.001.
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Valiant Co Ltd concanavalin a
Purified CD4 + T cells were added to 24-well plates and incubated in RPMI alone or in RPMI containing G-CSF or G-CSF plus <t>ConA</t> for 24 h. (A) The expression of G-CSFR on CD4 + T cells, evaluated by CD114 staining. (B) The percentage of G-CSFR is summarized in the graph (n=5 per group). After incubation 24h, G-CSF stimulated or left un-stimulated CD4 + T cells were transferred to 96-well plates coated with ICAM-1 and anti-CD3. (C) Cell morphology was examined by fluorescence microscopy at 60 minutes. Arrows indicate polarized T cells with a clear uropod. (D) Cells prepared as in C were quantified. (E) Unbound cells were washed off, and the adherent cells were quantified using a CCK-8 assay kit. The data are represented as the mean ± SD (n=15 per group). * P < 0.05; *** P < 0.001.
Concanavalin A, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
Vector Laboratories biotinylated cona
Figure 1 Glycan diversity in human upper respiratory tissues. (a) Costaining of tracheal tissue sections with <t>ConA</t> (red)/Jacalin (green) and SNA-I (red)/ Jacalin (green). The localized regions of Jacalin binding correspond to goblet cells expressing O-linked glycans and the regions of conA binding correspond to ciliated cells expressing N-linked glycans (white arrow) on the apical side of the tracheal epithelium. The extensive binding of SNA-I to both goblet cells (costain with Jacalin in yellow) and ciliated cells indicates predominant expression of O-linked and N-linked a2-6 on the apical side. (b) MALDI-MS glycan profile of human bronchial epithelial (HBE) cells using graphical representation (without explicit linkage assignment) of possible sialylated glycan structures that satisfy the mass peaks (within ± 3.5 Daltons). HBEs predominantly express a2-6 (in comparison with a2-3) sialylated glycans (Supplementary Fig. 1). (c) Desialylation using Sialidase A and subsequent 2-AB labeling of the N-linked glycans observed in b to deconvolute the branching pattern from the number of sialic acids. The peaks highlighted in cyan in b and c were further analyzed using TOF-TOF MS. (d) The MS-MS profile of a representative peak at m/z 2148 shows critical fragment ions at m/z 548 and 713 and their corresponding counter ions (shown in red) that support the long oligosaccharide branch (with multiple lactosamine repeats) over multiple short lactosamine branches. MS-MS profile of m/z 2660 also supports a long oligosaccharide branch (data not shown). Glycans are represented using the graphical nomenclature adopted by the Consortium for Functional Glycomics (CFG).
Biotinylated Cona, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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94
Vector Laboratories cona agarose beads
Figure 1 Glycan diversity in human upper respiratory tissues. (a) Costaining of tracheal tissue sections with <t>ConA</t> (red)/Jacalin (green) and SNA-I (red)/ Jacalin (green). The localized regions of Jacalin binding correspond to goblet cells expressing O-linked glycans and the regions of conA binding correspond to ciliated cells expressing N-linked glycans (white arrow) on the apical side of the tracheal epithelium. The extensive binding of SNA-I to both goblet cells (costain with Jacalin in yellow) and ciliated cells indicates predominant expression of O-linked and N-linked a2-6 on the apical side. (b) MALDI-MS glycan profile of human bronchial epithelial (HBE) cells using graphical representation (without explicit linkage assignment) of possible sialylated glycan structures that satisfy the mass peaks (within ± 3.5 Daltons). HBEs predominantly express a2-6 (in comparison with a2-3) sialylated glycans (Supplementary Fig. 1). (c) Desialylation using Sialidase A and subsequent 2-AB labeling of the N-linked glycans observed in b to deconvolute the branching pattern from the number of sialic acids. The peaks highlighted in cyan in b and c were further analyzed using TOF-TOF MS. (d) The MS-MS profile of a representative peak at m/z 2148 shows critical fragment ions at m/z 548 and 713 and their corresponding counter ions (shown in red) that support the long oligosaccharide branch (with multiple lactosamine repeats) over multiple short lactosamine branches. MS-MS profile of m/z 2660 also supports a long oligosaccharide branch (data not shown). Glycans are represented using the graphical nomenclature adopted by the Consortium for Functional Glycomics (CFG).
Cona Agarose Beads, supplied by Vector Laboratories, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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95
Biotium cf 488a concanavalin a cona
Figure 1 Glycan diversity in human upper respiratory tissues. (a) Costaining of tracheal tissue sections with <t>ConA</t> (red)/Jacalin (green) and SNA-I (red)/ Jacalin (green). The localized regions of Jacalin binding correspond to goblet cells expressing O-linked glycans and the regions of conA binding correspond to ciliated cells expressing N-linked glycans (white arrow) on the apical side of the tracheal epithelium. The extensive binding of SNA-I to both goblet cells (costain with Jacalin in yellow) and ciliated cells indicates predominant expression of O-linked and N-linked a2-6 on the apical side. (b) MALDI-MS glycan profile of human bronchial epithelial (HBE) cells using graphical representation (without explicit linkage assignment) of possible sialylated glycan structures that satisfy the mass peaks (within ± 3.5 Daltons). HBEs predominantly express a2-6 (in comparison with a2-3) sialylated glycans (Supplementary Fig. 1). (c) Desialylation using Sialidase A and subsequent 2-AB labeling of the N-linked glycans observed in b to deconvolute the branching pattern from the number of sialic acids. The peaks highlighted in cyan in b and c were further analyzed using TOF-TOF MS. (d) The MS-MS profile of a representative peak at m/z 2148 shows critical fragment ions at m/z 548 and 713 and their corresponding counter ions (shown in red) that support the long oligosaccharide branch (with multiple lactosamine repeats) over multiple short lactosamine branches. MS-MS profile of m/z 2660 also supports a long oligosaccharide branch (data not shown). Glycans are represented using the graphical nomenclature adopted by the Consortium for Functional Glycomics (CFG).
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85
LKT Laboratories concanavalin a
Figure 1 Glycan diversity in human upper respiratory tissues. (a) Costaining of tracheal tissue sections with <t>ConA</t> (red)/Jacalin (green) and SNA-I (red)/ Jacalin (green). The localized regions of Jacalin binding correspond to goblet cells expressing O-linked glycans and the regions of conA binding correspond to ciliated cells expressing N-linked glycans (white arrow) on the apical side of the tracheal epithelium. The extensive binding of SNA-I to both goblet cells (costain with Jacalin in yellow) and ciliated cells indicates predominant expression of O-linked and N-linked a2-6 on the apical side. (b) MALDI-MS glycan profile of human bronchial epithelial (HBE) cells using graphical representation (without explicit linkage assignment) of possible sialylated glycan structures that satisfy the mass peaks (within ± 3.5 Daltons). HBEs predominantly express a2-6 (in comparison with a2-3) sialylated glycans (Supplementary Fig. 1). (c) Desialylation using Sialidase A and subsequent 2-AB labeling of the N-linked glycans observed in b to deconvolute the branching pattern from the number of sialic acids. The peaks highlighted in cyan in b and c were further analyzed using TOF-TOF MS. (d) The MS-MS profile of a representative peak at m/z 2148 shows critical fragment ions at m/z 548 and 713 and their corresponding counter ions (shown in red) that support the long oligosaccharide branch (with multiple lactosamine repeats) over multiple short lactosamine branches. MS-MS profile of m/z 2660 also supports a long oligosaccharide branch (data not shown). Glycans are represented using the graphical nomenclature adopted by the Consortium for Functional Glycomics (CFG).
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94
Vector Laboratories concanavalin a cona
Figure 1 Glycan diversity in human upper respiratory tissues. (a) Costaining of tracheal tissue sections with <t>ConA</t> (red)/Jacalin (green) and SNA-I (red)/ Jacalin (green). The localized regions of Jacalin binding correspond to goblet cells expressing O-linked glycans and the regions of conA binding correspond to ciliated cells expressing N-linked glycans (white arrow) on the apical side of the tracheal epithelium. The extensive binding of SNA-I to both goblet cells (costain with Jacalin in yellow) and ciliated cells indicates predominant expression of O-linked and N-linked a2-6 on the apical side. (b) MALDI-MS glycan profile of human bronchial epithelial (HBE) cells using graphical representation (without explicit linkage assignment) of possible sialylated glycan structures that satisfy the mass peaks (within ± 3.5 Daltons). HBEs predominantly express a2-6 (in comparison with a2-3) sialylated glycans (Supplementary Fig. 1). (c) Desialylation using Sialidase A and subsequent 2-AB labeling of the N-linked glycans observed in b to deconvolute the branching pattern from the number of sialic acids. The peaks highlighted in cyan in b and c were further analyzed using TOF-TOF MS. (d) The MS-MS profile of a representative peak at m/z 2148 shows critical fragment ions at m/z 548 and 713 and their corresponding counter ions (shown in red) that support the long oligosaccharide branch (with multiple lactosamine repeats) over multiple short lactosamine branches. MS-MS profile of m/z 2660 also supports a long oligosaccharide branch (data not shown). Glycans are represented using the graphical nomenclature adopted by the Consortium for Functional Glycomics (CFG).
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99
Thermo Fisher concanavalin a
Figure 1 Glycan diversity in human upper respiratory tissues. (a) Costaining of tracheal tissue sections with <t>ConA</t> (red)/Jacalin (green) and SNA-I (red)/ Jacalin (green). The localized regions of Jacalin binding correspond to goblet cells expressing O-linked glycans and the regions of conA binding correspond to ciliated cells expressing N-linked glycans (white arrow) on the apical side of the tracheal epithelium. The extensive binding of SNA-I to both goblet cells (costain with Jacalin in yellow) and ciliated cells indicates predominant expression of O-linked and N-linked a2-6 on the apical side. (b) MALDI-MS glycan profile of human bronchial epithelial (HBE) cells using graphical representation (without explicit linkage assignment) of possible sialylated glycan structures that satisfy the mass peaks (within ± 3.5 Daltons). HBEs predominantly express a2-6 (in comparison with a2-3) sialylated glycans (Supplementary Fig. 1). (c) Desialylation using Sialidase A and subsequent 2-AB labeling of the N-linked glycans observed in b to deconvolute the branching pattern from the number of sialic acids. The peaks highlighted in cyan in b and c were further analyzed using TOF-TOF MS. (d) The MS-MS profile of a representative peak at m/z 2148 shows critical fragment ions at m/z 548 and 713 and their corresponding counter ions (shown in red) that support the long oligosaccharide branch (with multiple lactosamine repeats) over multiple short lactosamine branches. MS-MS profile of m/z 2660 also supports a long oligosaccharide branch (data not shown). Glycans are represented using the graphical nomenclature adopted by the Consortium for Functional Glycomics (CFG).
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Image Search Results


A. Principal component analysis (PCA) of lectin-binding intensities in Cladocopium (orange, N = 18) and Durusdinium (blue, N = 30) symbionts isolated from coral eggs. B. PCA of lectin-binding intensities in Cladocopium and Durusdinium symbionts isolated from parental colonies ( N = 15 and N = 18, respectively). C. PCA of lectin-binding intensities in Cladocopium symbionts isolated from coral eggs (circles) and parental colonies (triangles) pairs ( N = 15). D. PCA of lectin-binding intensities in Durusdinium symbionts isolated from coral eggs and parental colony pairs ( N = 18). In A-D, vectors represent the contribution of individual lectins to the ordination. Ellipses represent the 95% confidence intervals around group centroids. Group separations were statistically significant (PERMANOVA P = 0.001). Asterisks denote adjusted P values (* P < 0.05, ** P < 0.01, *** P < 0.001). E. Partial least squares discriminant analysis (PLS-DA) of each lectin-binding intensity profile for symbionts in eggs and parents. Lectins: ConA (concanavalin A, specific for D-mannose and D-glucose), LTL ( Lotus tetragonolobus lectin, specific for L-fucose), PNA ( Arachis hypogaea lectin, specific for D-galactose), WGA (wheat germ agglutinin, specific for N-acetylglucosamine and N-acetylneuraminic acid), PHA-L (phytohemagglutinin-L from Phaseolus vulgaris , specific for N-acetylglucosamine β(1-2) mannopyranosyl) and GS-IB4 (isolectin from Griffonia simplicifolia , specific for N-acetyl-D-galactosamine and a-D-galactosyl residues).

Journal: bioRxiv

Article Title: Selective conservation of symbiont cell-surface glycans across generations in a vertically transmitting coral

doi: 10.64898/2026.04.21.719984

Figure Lengend Snippet: A. Principal component analysis (PCA) of lectin-binding intensities in Cladocopium (orange, N = 18) and Durusdinium (blue, N = 30) symbionts isolated from coral eggs. B. PCA of lectin-binding intensities in Cladocopium and Durusdinium symbionts isolated from parental colonies ( N = 15 and N = 18, respectively). C. PCA of lectin-binding intensities in Cladocopium symbionts isolated from coral eggs (circles) and parental colonies (triangles) pairs ( N = 15). D. PCA of lectin-binding intensities in Durusdinium symbionts isolated from coral eggs and parental colony pairs ( N = 18). In A-D, vectors represent the contribution of individual lectins to the ordination. Ellipses represent the 95% confidence intervals around group centroids. Group separations were statistically significant (PERMANOVA P = 0.001). Asterisks denote adjusted P values (* P < 0.05, ** P < 0.01, *** P < 0.001). E. Partial least squares discriminant analysis (PLS-DA) of each lectin-binding intensity profile for symbionts in eggs and parents. Lectins: ConA (concanavalin A, specific for D-mannose and D-glucose), LTL ( Lotus tetragonolobus lectin, specific for L-fucose), PNA ( Arachis hypogaea lectin, specific for D-galactose), WGA (wheat germ agglutinin, specific for N-acetylglucosamine and N-acetylneuraminic acid), PHA-L (phytohemagglutinin-L from Phaseolus vulgaris , specific for N-acetylglucosamine β(1-2) mannopyranosyl) and GS-IB4 (isolectin from Griffonia simplicifolia , specific for N-acetyl-D-galactosamine and a-D-galactosyl residues).

Article Snippet: The following lectins, purchased from Thermo Fisher Scientific, were used: ConA (concanavalin A; specific for D-mannose and D-glucose; cat. no. C21401), LTL ( Lotus tetragonolobus lectin; specific for L-fucose; cat. no. L32480), PNA (peanut agglutinin; specific for D-galactose; cat. no. L21409), WGA (wheat germ agglutinin; specific for N-acetylglucosamine and N-acetylneuraminic acid; cat. no. W11261), PHAL (phytohemagglutinin-L from Phaseolus vulgaris ; specific for N-acetylglucosamine β(1–2) mannopyranosyl residues; cat. no. L11270), and GSIB4 (isolectin B4 from Griffonia simplicifolia ; specific for N-acetyl-D-galactosamine and α-D-galactosyl residues; cat. no. I21411).

Techniques: Binding Assay, Isolation

A. Proportional binding profiles (total positive MFI signal) across lectins in Cladocopium ( N = 18) and Durusdinium ( N = 30) isolated from coral eggs. B. Proportional binding profiles across lectins in Cladocopium ( N = 15) and Durusdinium ( N = 18) isolated from parental colonies. In C and D, bar height represents the relative contribution of each lectin to the total binding signal per symbiont genus. C. Proportional binding profiles across lectins per host genotype in Cladocopium ( N = 18) isolated from coral eggs. D. Proportional binding profiles across lectins per host genotype in Durusdinium ( N =30) isolated from coral eggs. In E and F, bar height represents the relative contribution of each lectin to the total binding signal per genotype. Lectins: ConA (concanavalin A, specific for D-mannose and D-glucose), LTL ( Lotus tetragonolobus lectin, specific for L-fucose), PNA ( Arachis hypogaea lectin, specific for D-galactose), WGA (wheat germ agglutinin, specific for N-acetylglucosamine and N-acetylneuraminic acid), PHA-L (phytohemagglutinin-L from Phaseolus vulgaris , specific for N-acetylglucosamine β(1-2) mannopyranosyl) and GS-IB4 (isolectin from Griffonia simplicifolia , specific for N-acetyl-D-galactosamine and a-D-galactosyl residues).

Journal: bioRxiv

Article Title: Selective conservation of symbiont cell-surface glycans across generations in a vertically transmitting coral

doi: 10.64898/2026.04.21.719984

Figure Lengend Snippet: A. Proportional binding profiles (total positive MFI signal) across lectins in Cladocopium ( N = 18) and Durusdinium ( N = 30) isolated from coral eggs. B. Proportional binding profiles across lectins in Cladocopium ( N = 15) and Durusdinium ( N = 18) isolated from parental colonies. In C and D, bar height represents the relative contribution of each lectin to the total binding signal per symbiont genus. C. Proportional binding profiles across lectins per host genotype in Cladocopium ( N = 18) isolated from coral eggs. D. Proportional binding profiles across lectins per host genotype in Durusdinium ( N =30) isolated from coral eggs. In E and F, bar height represents the relative contribution of each lectin to the total binding signal per genotype. Lectins: ConA (concanavalin A, specific for D-mannose and D-glucose), LTL ( Lotus tetragonolobus lectin, specific for L-fucose), PNA ( Arachis hypogaea lectin, specific for D-galactose), WGA (wheat germ agglutinin, specific for N-acetylglucosamine and N-acetylneuraminic acid), PHA-L (phytohemagglutinin-L from Phaseolus vulgaris , specific for N-acetylglucosamine β(1-2) mannopyranosyl) and GS-IB4 (isolectin from Griffonia simplicifolia , specific for N-acetyl-D-galactosamine and a-D-galactosyl residues).

Article Snippet: The following lectins, purchased from Thermo Fisher Scientific, were used: ConA (concanavalin A; specific for D-mannose and D-glucose; cat. no. C21401), LTL ( Lotus tetragonolobus lectin; specific for L-fucose; cat. no. L32480), PNA (peanut agglutinin; specific for D-galactose; cat. no. L21409), WGA (wheat germ agglutinin; specific for N-acetylglucosamine and N-acetylneuraminic acid; cat. no. W11261), PHAL (phytohemagglutinin-L from Phaseolus vulgaris ; specific for N-acetylglucosamine β(1–2) mannopyranosyl residues; cat. no. L11270), and GSIB4 (isolectin B4 from Griffonia simplicifolia ; specific for N-acetyl-D-galactosamine and α-D-galactosyl residues; cat. no. I21411).

Techniques: Binding Assay, Isolation

Purified CD4 + T cells were added to 24-well plates and incubated in RPMI alone or in RPMI containing G-CSF or G-CSF plus ConA for 24 h. (A) The expression of G-CSFR on CD4 + T cells, evaluated by CD114 staining. (B) The percentage of G-CSFR is summarized in the graph (n=5 per group). After incubation 24h, G-CSF stimulated or left un-stimulated CD4 + T cells were transferred to 96-well plates coated with ICAM-1 and anti-CD3. (C) Cell morphology was examined by fluorescence microscopy at 60 minutes. Arrows indicate polarized T cells with a clear uropod. (D) Cells prepared as in C were quantified. (E) Unbound cells were washed off, and the adherent cells were quantified using a CCK-8 assay kit. The data are represented as the mean ± SD (n=15 per group). * P < 0.05; *** P < 0.001.

Journal: Oncotarget

Article Title: G-CSF inhibits LFA-1-mediated CD4 + T cell functions by inhibiting Lck and ZAP-70

doi: 10.18632/oncotarget.18194

Figure Lengend Snippet: Purified CD4 + T cells were added to 24-well plates and incubated in RPMI alone or in RPMI containing G-CSF or G-CSF plus ConA for 24 h. (A) The expression of G-CSFR on CD4 + T cells, evaluated by CD114 staining. (B) The percentage of G-CSFR is summarized in the graph (n=5 per group). After incubation 24h, G-CSF stimulated or left un-stimulated CD4 + T cells were transferred to 96-well plates coated with ICAM-1 and anti-CD3. (C) Cell morphology was examined by fluorescence microscopy at 60 minutes. Arrows indicate polarized T cells with a clear uropod. (D) Cells prepared as in C were quantified. (E) Unbound cells were washed off, and the adherent cells were quantified using a CCK-8 assay kit. The data are represented as the mean ± SD (n=15 per group). * P < 0.05; *** P < 0.001.

Article Snippet: Concanavalin A (ConA) was purchased from Santa Cruz Biotechnology (Santa Cruz, Dallas, TX, USA).

Techniques: Purification, Incubation, Expressing, Staining, Fluorescence, Microscopy, CCK-8 Assay

Purified CD4 + T cells were added to 24-well plates and incubated in RPMI alone or in RPMI containing G-CSF or G-CSF plus ConA for 24 h. After the incubation, the cells were transferred to anti-CD3- and ICAM-1-coated 6-well plates and incubated for 1 h at 37°C. (A and B) Lysates from the three groups of CD4 + T cells were analyzed by western blot to detect the expression of Lck, ZAP-70 and phosphorylated Lck and ZAP-70, which were normalized to actin. (C-F) Densitometry quantification was performed and presented. All data are represented as the mean ± SD (n=4 per group). * P < 0.05; ** P < 0.01; *** P < 0.001.

Journal: Oncotarget

Article Title: G-CSF inhibits LFA-1-mediated CD4 + T cell functions by inhibiting Lck and ZAP-70

doi: 10.18632/oncotarget.18194

Figure Lengend Snippet: Purified CD4 + T cells were added to 24-well plates and incubated in RPMI alone or in RPMI containing G-CSF or G-CSF plus ConA for 24 h. After the incubation, the cells were transferred to anti-CD3- and ICAM-1-coated 6-well plates and incubated for 1 h at 37°C. (A and B) Lysates from the three groups of CD4 + T cells were analyzed by western blot to detect the expression of Lck, ZAP-70 and phosphorylated Lck and ZAP-70, which were normalized to actin. (C-F) Densitometry quantification was performed and presented. All data are represented as the mean ± SD (n=4 per group). * P < 0.05; ** P < 0.01; *** P < 0.001.

Article Snippet: Concanavalin A (ConA) was purchased from Santa Cruz Biotechnology (Santa Cruz, Dallas, TX, USA).

Techniques: Purification, Incubation, Western Blot, Expressing

Figure 1 Glycan diversity in human upper respiratory tissues. (a) Costaining of tracheal tissue sections with ConA (red)/Jacalin (green) and SNA-I (red)/ Jacalin (green). The localized regions of Jacalin binding correspond to goblet cells expressing O-linked glycans and the regions of conA binding correspond to ciliated cells expressing N-linked glycans (white arrow) on the apical side of the tracheal epithelium. The extensive binding of SNA-I to both goblet cells (costain with Jacalin in yellow) and ciliated cells indicates predominant expression of O-linked and N-linked a2-6 on the apical side. (b) MALDI-MS glycan profile of human bronchial epithelial (HBE) cells using graphical representation (without explicit linkage assignment) of possible sialylated glycan structures that satisfy the mass peaks (within ± 3.5 Daltons). HBEs predominantly express a2-6 (in comparison with a2-3) sialylated glycans (Supplementary Fig. 1). (c) Desialylation using Sialidase A and subsequent 2-AB labeling of the N-linked glycans observed in b to deconvolute the branching pattern from the number of sialic acids. The peaks highlighted in cyan in b and c were further analyzed using TOF-TOF MS. (d) The MS-MS profile of a representative peak at m/z 2148 shows critical fragment ions at m/z 548 and 713 and their corresponding counter ions (shown in red) that support the long oligosaccharide branch (with multiple lactosamine repeats) over multiple short lactosamine branches. MS-MS profile of m/z 2660 also supports a long oligosaccharide branch (data not shown). Glycans are represented using the graphical nomenclature adopted by the Consortium for Functional Glycomics (CFG).

Journal: Nature biotechnology

Article Title: Glycan topology determines human adaptation of avian H5N1 virus hemagglutinin.

doi: 10.1038/nbt1375

Figure Lengend Snippet: Figure 1 Glycan diversity in human upper respiratory tissues. (a) Costaining of tracheal tissue sections with ConA (red)/Jacalin (green) and SNA-I (red)/ Jacalin (green). The localized regions of Jacalin binding correspond to goblet cells expressing O-linked glycans and the regions of conA binding correspond to ciliated cells expressing N-linked glycans (white arrow) on the apical side of the tracheal epithelium. The extensive binding of SNA-I to both goblet cells (costain with Jacalin in yellow) and ciliated cells indicates predominant expression of O-linked and N-linked a2-6 on the apical side. (b) MALDI-MS glycan profile of human bronchial epithelial (HBE) cells using graphical representation (without explicit linkage assignment) of possible sialylated glycan structures that satisfy the mass peaks (within ± 3.5 Daltons). HBEs predominantly express a2-6 (in comparison with a2-3) sialylated glycans (Supplementary Fig. 1). (c) Desialylation using Sialidase A and subsequent 2-AB labeling of the N-linked glycans observed in b to deconvolute the branching pattern from the number of sialic acids. The peaks highlighted in cyan in b and c were further analyzed using TOF-TOF MS. (d) The MS-MS profile of a representative peak at m/z 2148 shows critical fragment ions at m/z 548 and 713 and their corresponding counter ions (shown in red) that support the long oligosaccharide branch (with multiple lactosamine repeats) over multiple short lactosamine branches. MS-MS profile of m/z 2660 also supports a long oligosaccharide branch (data not shown). Glycans are represented using the graphical nomenclature adopted by the Consortium for Functional Glycomics (CFG).

Article Snippet: Sections were then incubated with FITC-labeled Jacalin, biotinylated conA and biotinylated Sambuccus nigra agglutinin (SNA-I) (Vector labs; 10 mg/ml in PBS with 0.05% Tween-20) for 3 h. After washing with TBST (Tris-buffered saline with 0.1% Tween-20), the sections were incubated with Alexa fluor 546 streptavidin (Invitrogen) for 1 h. Slides were washed with TBST and viewed under a confocal microscope (Zeiss LSM510 laser scanning confocal microscopy).

Techniques: Glycoproteomics, Binding Assay, Expressing, Comparison, Labeling, Tandem Mass Spectroscopy, Functional Assay