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Immune cell surface carbohydrates, collectively known as the immune glycome, are complex sugar structures (glycans) attached to proteins and lipids on the exterior of immune cells. These molecules play a fundamental role in the immune system by serving as ligands for various glycan-binding proteins, or lectins, such as Siglecs, selectins, and galectins [1.1.2, 1.4.4]. Through these interactions, surface carbohydrates regulate critical processes including cell adhesion, migration, and the discrimination between self and non-self [1.1.2, 1.2.3]. In many pathological states, particularly cancer, the glycosylation patterns on immune and tumor cells are altered to create glyco-immune checkpoints that suppress immune activation and facilitate disease progression [1.3.2, 1.3.5]. Therapeutic interventions targeting these carbohydrates include enzymatic modifiers like sialidases, which remove inhibitory sialic acids, and glycomimetics or antibodies that block lectin-carbohydrate interactions [1.3.1, 1.4.5]. These approaches are currently being explored to enhance anti-tumor immunity and treat inflammatory conditions like sickle cell disease and acute myeloid leukemia [1.2.4, 1.4.5].
Enzymatic desialylation of cell surface glycans, competitive inhibition of lectin-carbohydrate binding, and blockade of selectin-mediated leukocyte adhesion.
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