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Human cell-surface sialic acid-containing receptors are a broad class of glycoproteins and glycolipids that present terminal sialic acid residues, most commonly N-acetylneuraminic acid (Neu5Ac). These molecules are essential components of the glycocalyx and play pivotal roles in cell-cell recognition, immune system modulation, and signal transduction. They are particularly significant in virology as the primary attachment receptors for numerous pathogens, including influenza viruses, parainfluenza viruses, and certain adenoviruses. The specific glycosidic linkage of the sialic acid, such as α2,3 or α2,6, is a key determinant of viral tropism and host susceptibility. In therapeutic development, these receptors are targeted by agents like DAS181 (Fludase), a recombinant sialidase that enzymatically removes the sialic acid to prevent viral entry. Additionally, the aberrant hypersialylation of these receptors in malignant cells contributes to cancer progression and immune evasion, making them targets for novel diagnostic and therapeutic strategies. While targeting these host factors offers a high barrier to viral resistance, challenges include the potential for immunogenicity and the disruption of normal physiological signaling.
Enzymatic removal of terminal sialic acid residues from the host cell surface to block viral attachment and entry.
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