ArticleThe Journal of biological chemistry2022
Galectin-9 recognizes and exhibits antimicrobial activity toward microbes expressing blood group-like antigens.
Article in The Journal of biological chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 30 citations in OpenAlex.
- A Zebrafish Galectin-1 Isoform Is Expressed in Skin and Gills and Binds to Bacteria, Bacterial Adhesin Receptors, and Epidermal Mucus Glycans.International journal of molecular sciences · 2026Article
- Site-specific profiling of structure and function of Igµ B cell receptor glycans.Nature communications · 2026Article
- Expression and Characterization of Blood Group Binding Lectins.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Mouse Model of Hemolytic Disease of the Fetus and Newborn.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Examination of Antigen-Specific B Cell Responses to Red Blood Cell Transfusion.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Determining the Binding Affinity in Monoclonal Antibody-Alloantigen Interactions.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Analysis of Galectin Binding to Blood Group Expressing Bacteria.Methods in molecular biology (Clifton, N.J.) · 2026Article
- The Historiography of Galactose and Its Recognition by Galectins.Advances in experimental medicine and biology · 2026Review
- Use of Microbial Microarrays to Define Antibody Specificity.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Defining the Specificity of Blood-Group-Binding Lectins Through Microarray Analysis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Flow Cytometric Examination of Galectin Binding to Red Blood Cells.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Acute Incompatible Red Blood Cell Transfusion in Mice.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Analysis of Erythrocyte Membrane Alloantigens.Methods in molecular biology (Clifton, N.J.) · 2026Article
- CD45 and Basigin (CD147) Are Functional Ligands for Galectin-8 on Human Leukocytes.Biomolecules · 2025Article
- Galectin-9-An Emerging Glyco-Immune Checkpoint Target for Cancer Therapy.International journal of molecular sciences · 2025Review
- O-antigen polysaccharides inMicrobiology and molecular biology reviews : MMBR · 2025Review
- CD47 regulates antigen modulation and red blood cell clearance following an incompatible transfusion.Frontiers in immunology · 2025Article
- Identification of galectin-9 and its antibacterial function in Yellow River carp (Frontiers in immunology · 2025Article
- The interplay between hormonal vitamin D and lipopolysaccharide signaling on human neutrophil transcriptional responses.Frontiers in immunology · 2025Article
- Harnessing the potential of red blood cells in immunotherapy.Human immunology · 2024Review
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
While adaptive immunity recognizes a nearly infinite range of antigenic determinants, immune tolerance renders adaptive immunity vulnerable to microbes decorated in self-like antigens. Recent studies suggest that sugar-binding proteins galectin-4 and galectin-8 bind microbes expressing blood group antigens. However, the binding profile and potential antimicrobial activity of other galectins, particularly galectin-9 (Gal-9), has remained incompletely defined. Here, we demonstrate that while Gal-9 possesses strong binding preference for ABO(H) blood group antigens, each domain exhibits distinct binding patterns, with the C-terminal domain (Gal-9C) exhibiting higher binding to blood group B than the N-terminal domain (Gal-9N). Despite this binding preference, Gal-9 readily killed blood group B-positive Escherichia coli, whereas Gal-9N displayed higher killing activity against this microbe than Gal-9C. Utilization of microarrays populated with blood group O antigens from a diverse array of microbes revealed that Gal-9 can bind various microbial glycans, whereas Gal-9N and Gal-9C displayed distinct and overlapping binding preferences. Flow cytometric examination of intact microbes corroborated the microbial glycan microarray findings, demonstrating that Gal-9, Gal-9N, and Gal-9C also possess the capacity to recognize distinct strains of Providencia alcalifaciens and Klebsiella pneumoniae that express mammalian blood group-like antigens while failing to bind related strains that do not express mammalian-like glycans. In each case of microbial binding, Gal-9, Gal-9N, and Gal-9C induced microbial death. In contrast, while Gal-9, Gal-9N, and Gal-9C engaged red blood cells, each failed to induce hemolysis. These data suggest that Gal-9 recognition of distinct microbial strains may provide antimicrobial activity against molecular mimicry.
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