Journal: Frontiers in Immunology

Article Title: Cancer cells and viruses share common glycoepitopes: exciting opportunities toward combined treatments

doi: 10.3389/fimmu.2024.1292588

Figure Lengend Snippet: Human and plant lectins binding to glycoepitopes of viral envelop proteins.

Article Snippet: SARS-CoV-2 , DC-SIGN Banana Lectin MGL Galectin-7 Galectin-3 Galectin-8 Siglec-8 Siglec-10 , Mannose, LeX Mannose GalNAc LacNAc LacNAc 3’SLN 6’Sulfo-SLeX SLN , ( ) ( – ) ( ) ( ) ( ) ( ) ( ) ( ) .

Techniques: Binding Assay, Virus

Journal: Acta Crystallographica. Section F, Structural Biology Communications

Article Title: Conformations of the type-1 lacto- N -biose I unit in protein complex structures

doi: 10.1107/S2053230X18006568

Figure Lengend Snippet: Number of LNB structures in the PDB surveyed by GlycoMapsDB

Article Snippet: The PDB contains LNB or LNT structures bound to human galectins (galectin-1, galectin-3, galectin-4, galectin-7 and galectin-8) as a part of a lacto-series of glycosphingolipids.

Techniques: Bacteria

Journal: Scientific Reports

Article Title: Identification of a new regulation pathway of EGFR and E-cadherin dynamics

doi: 10.1038/s41598-021-02042-3

Figure Lengend Snippet: Galectin-7 interacts with both E-cadherin and EGFR and modulates E-cadherin endocytosis. ( A ) Modulation of E-cadherin internalization by galectin-7 and EGF. Representative images of HaCaT and ShGal7 #2 after E-cadherin antibody uptake for 30 min. Cells were previously treated or not with 100 ng/mL of EGF. Histograms represent corresponding quantifications in percentage reported to HaCaT not treated cells. Scale bars stand for standard deviation. ( B ) In vitro binding assays were performed using recombinant wild-type human galectin-7 (rGal7); CRD mutated human galectin-7 (R74S), Extracellular domain of human E-cadherin fused to a His tag (E-cad-his) and extracellular domain of human EGFR fused to human IgG1 Fc fragment (EGFR-Fc). In each conditions, EGFR-Fc was pulled down using protein G sepharose coated beads. E-cadherin precipitated with EGFR-Fc only in presence of galectin-7 (n = 3). Cropped images are from samples run on the same gels. Full-length blots are displayed in supplementary Fig. B.

Article Snippet: Full-length blots are displayed in supplementary Fig. A.Galectin-7 directly interacts with extracellular domain of E-cadherin independently of glycosylation motifs. ( B ) In vitro binding assays were performed using recombinant wild type human galectin-7 (rGal7); CRD mutated human galectin-7 (R74S) and extracellular domain of human EGFR fused to human IgG1 Fc fragment (EGFR-Fc).

Techniques: Standard Deviation, In Vitro, Binding Assay, Recombinant

Journal: Scientific Reports

Article Title: Identification of a new regulation pathway of EGFR and E-cadherin dynamics

doi: 10.1038/s41598-021-02042-3

Figure Lengend Snippet: Galectin-7 interacts and colocalizes with EGFR. ( A ) Co-immunoprecipitation experiments indicate that galectin-7 is a partner of EGFR and E-cadherin. Images shown are representative of images taken from distinct western blots. Full-length blots are displayed in supplementary Fig. A.Galectin-7 directly interacts with extracellular domain of E-cadherin independently of glycosylation motifs. ( B ) In vitro binding assays were performed using recombinant wild type human galectin-7 (rGal7); CRD mutated human galectin-7 (R74S) and extracellular domain of human EGFR fused to human IgG1 Fc fragment (EGFR-Fc). WT galectin-7 (rGal7) precipitated with EGFR-Fc unlike mutated galectin-7 (R74S) Full-length blots are displayed in supplementary Fig. B. ( C ) Confocal images of Proximity Ligation Assays confirming that galectin-7 is in close proximity with EGFR in cellular context. Galectin-7—S100A11 pairs were used as negative controls. At least 3 independent experiments were conducted.

Article Snippet: Full-length blots are displayed in supplementary Fig. A.Galectin-7 directly interacts with extracellular domain of E-cadherin independently of glycosylation motifs. ( B ) In vitro binding assays were performed using recombinant wild type human galectin-7 (rGal7); CRD mutated human galectin-7 (R74S) and extracellular domain of human EGFR fused to human IgG1 Fc fragment (EGFR-Fc).

Techniques: Immunoprecipitation, Western Blot, Glycoproteomics, In Vitro, Binding Assay, Recombinant, Ligation

Journal: Scientific Reports

Article Title: Identification of a new regulation pathway of EGFR and E-cadherin dynamics

doi: 10.1038/s41598-021-02042-3

Figure Lengend Snippet: Absence of galectin-7 impairs skin differentiation. ( A ) Representative staining of wild type and Gal7−/− mice tail with Hematoxylin/Eosin. A thickening of the epidermis is well observable in Gal7−/− mice. Magnification 40 × . ( B ) Curves are the results of total cell proliferation assays of HaCaT and shGal7 #2 cell lines counted during 11 days to calculate the mean ± standard deviation (SD). Results are mean of three independent experiments performed in duplicate. ( C ) Representative immunostaining of keratin 14 (green) and keratin 10 (red) in WT and Gal7−/− mice mice tail epidermis showing localization of these two proteins. Scale bar = 15 µm. ( D ) Quantifications of the ratio of K14 positive/total cells performed of immunostaining of keratin 14 and keratin 10. Quantification were performed on ImageJ software (Version 2.3.0/1.53f.— http://imagej.net/Contributors ) from different samples from different 2 months old female mice (WT : n = 6 and gal7−/−` : n = 4).

Article Snippet: Full-length blots are displayed in supplementary Fig. A.Galectin-7 directly interacts with extracellular domain of E-cadherin independently of glycosylation motifs. ( B ) In vitro binding assays were performed using recombinant wild type human galectin-7 (rGal7); CRD mutated human galectin-7 (R74S) and extracellular domain of human EGFR fused to human IgG1 Fc fragment (EGFR-Fc).

Techniques: Staining, Standard Deviation, Immunostaining, Software