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

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

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