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Host and microbial cell-surface glycans and adhesion receptors refers to the complex network of carbohydrate structures and their cognate binding proteins that mediate interactions at the cellular interface. Glycans, which are complex sugar chains attached to proteins and lipids, serve as essential recognition markers on the surfaces of all cells (Varki et al., Essentials of Glycobiology, 2017). Adhesion receptors, including lectins, selectins, and integrins, specifically recognize these glycan patterns to facilitate processes such as leukocyte trafficking, cell signaling, and tissue organization. In infectious diseases, pathogens exploit these host glycans as attachment sites for entry, while host immune cells use pattern recognition receptors to identify microbial-specific glycans (Imberty & Varrot, Curr Opin Struct Biol, 2008). Aberrant glycosylation and adhesion are also hallmarks of cancer metastasis and chronic inflammatory conditions. Consequently, this interface is a major focus for therapeutic development, with drugs like neuraminidase inhibitors and integrin blockers designed to disrupt pathological binding (Schnaar, Glycobiology of the Immune System, 2016).
Inhibition of adhesion, competitive binding to glycans, enzymatic inhibition of glycan cleavage, blockade of receptor-ligand interaction
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