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Sialic acid-containing cell-surface glycoproteins and glycolipids, collectively known as sialoglycans, are essential components of the glycocalyx on vertebrate cells (Varki, 2008, PMID: 18606570). These molecules consist of a diverse array of glycoconjugates where sialic acid residues occupy terminal positions, making them primary points of contact for extracellular interactions (Schauer, 2009, PMID: 19699080). They play critical roles in biological processes such as cell-cell adhesion, signal transduction, and the regulation of the immune system through interactions with Siglec receptors (Pearce & Läubli, 2016, PMID: 26554340). In pathology, aberrant sialylation is a hallmark of cancer, contributing to tumor metastasis and immune evasion by creating a "sialic acid blockade" that inhibits natural killer cells and macrophages (Büll et al., 2014, PMID: 24713433). Furthermore, sialoglycans serve as essential receptors for numerous pathogens, including influenza viruses and certain bacteria, which utilize them for host cell attachment and entry (Varki, 2008, PMID: 18606570). Therapeutic strategies targeting these molecules include neuraminidase inhibitors to prevent viral spread and glyco-immune checkpoint inhibitors, such as sialidase fusion proteins, to enhance anti-tumor immunity (Pearce & Läubli, 2016, PMID: 26554340).
Enzymatic removal of terminal sialic acid residues; inhibition of viral neuraminidase to prevent cleavage of host sialic acid; blockade of Siglec-mediated inhibitory signaling.
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