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Host cell surface glycoproteins are proteins embedded in the plasma membrane of eukaryotic cells, covalently linked to oligosaccharide chains that extend into the extracellular space, forming part of the glycocalyx. These molecules serve critical roles in cell-cell recognition, adhesion, and signaling, acting as receptors for hormones, ligands, and pathogens, while also providing structural protection and lubrication to epithelial tissues. In immune responses, they facilitate antigen presentation and pathogen entrapment, with mucins exemplifying protective barrier functions against microbial invasion. Dysregulation of their glycosylation contributes to disease pathology, such as enhanced cancer metastasis via altered branching or viral exploitation for host cell entry in infections like influenza and HIV. Although individual surface glycoproteins (e.g., selectins, integrins) are pursued as therapeutic targets, the broad class lacks specific small-molecule drugs due to its diversity and ubiquitous roles. This category encompasses diverse families rather than a singular target, complicating direct pharmacologic intervention, though glycan-modulating enzymes or antibodies against specific subtypes show preclinical promise in oncology and antivirals.
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