Glycans are carbohydrate modifications typically found on proteins or lipids, and can act as ligands for glycan-binding proteins called lectins. Glycans and lectins play crucial roles in the function of cells and organs, and in the immune system of animals and humans. Viral pathogens use glycans and lectins that are encoded by their own or the host genome for their replication and spread. Recent advances in glycobiological research indicate that glycans and lectins mediate key interactions at the virus-host interface, controlling viral spread and/or activation of the immune system. This review reflects on glycan-lectin interactions in the context of viral infection and antiviral immunity. A short introduction illustrates the nature of glycans and lectins, and conveys the basic principles of their interactions. Subsequently, examples are discussed highlighting specific glycan-lectin interactions and how they affect the progress of viral infections, either benefiting the host or the virus. Moreover, glycan and lectin variability and their potential biological consequences are discussed. Finally, the review outlines how recent advances in the glycan-lectin field might be transformed into promising new approaches to antiviral therapy.
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http://dx.doi.org/10.1111/1574-6976.12052 | DOI Listing |
J Vector Borne Dis
January 2025
Department of Zoology, Faculty of Science, University of Jaffna, Jaffna, Sri Lanka.
Background And Objectives: Salivary glands proteins but not glycoconjugates have been previously studied in mosquito vectors of human diseases. Glycoconjugates from salivary gland-derived proteins from human-feeding tick vectors can elicit hypersensitivity reactions which may also occur with mosquito bites. Protein glycoconjugate in salivary glands of the principal arboviral vector Aedes aegypti and the rapidly spreading malaria vector Anopheles stephensi were therefore investigated.
View Article and Find Full Text PDFCells
December 2024
Department of Orthopedics and Trauma Surgery, University Hospital Bonn, 53127 Bonn, Germany.
Inflammation models with the proinflammatory cytokine interleukin-1β (IL-1β) are widely used in the in vitro investigation of new therapeutic approaches for osteoarthritis (OA). The aim of this study was to systematically analyze the influence of IL-1β in a 3D chondral pellet culture model. Bovine articular chondrocytes were cultured to passage 3 and then placed in pellet culture.
View Article and Find Full Text PDFBBA Adv
December 2024
Cellular and Molecular Biotechnology Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8565, Japan.
Chemical-nose/tongue technologies are emerging as promising analytical tools for glycan analysis. After briefly introducing the importance of glycans and their analytical methods, including the lectin microarray (LMA) as one of the gold standards, the fundamental principles underlying chemical noses/tongues are explained and various applications for monosaccharides and glycans are introduced. Then, the similarities and differences of these two approaches are discussed.
View Article and Find Full Text PDFAnal Chim Acta
January 2025
Department of Biomedical Engineering, Korea University, Seoul, 02841, South Korea; Interdisciplinary Program in Precision Public Health, Korea University, Seoul, 02841, South Korea. Electronic address:
Glycosylation, the intricate process of adding carbohydrate motifs to proteins, lipids, and exosomes on the cell surface, is crucial for both physiological and pathological mechanisms. Alterations in glycans significantly affect cancer cell metastasis by mediating cell-cell and cell-matrix interactions. The subtle changes in glycosylation during malignant transformations highlight the importance of analyzing cell and exosome surface glycosylation for prognostic and early treatment strategies in cancer.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
January 2025
Georgia State University, Chemistry, 50 Decatur ST SE, 30303, Atlanta, UNITED STATES OF AMERICA.
Poly-N-acetyllactosamine (poly-LacNAc) is ubiquitously expressed on cell surface glycoconjugates, serving as the backbone of complex glycans and an extended scaffold that presents diverse glycan epitopes. The branching of poly-LacNAc, where internal galactose (Gal) residues have β1-6 linked N-acetylglucosamine (GlcNAc) attached, forms the blood group I-antigen, which is closely associated with various physiological and pathological processes including cancer progression. However, the underlying mechanisms remain unclear as many of the I-antigen sequences are undefined and inaccessible.
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