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Host galactose-containing glycans are a diverse class of carbohydrate structures, typically terminating in or containing galactose residues, found on the surface of host cell glycoproteins and glycolipids (Cummings et al., 2017). These glycans serve as essential ligands for a variety of endogenous proteins, most notably galectins, which "read" the glycan code to regulate biological processes such as cell-cell adhesion, apoptosis, and immune cell activation (Liu & Rabinovich, 2005). In the context of human health, these glycans are frequently exploited by pathogens; for instance, many bacteria and viruses utilize host galactose residues as primary or secondary receptors for attachment and subsequent cellular entry (Imberty & Varrot, 2008). Furthermore, alterations in the density and branching of these glycans are a hallmark of cancer progression, where they facilitate tumor cell migration and help the tumor evade immune detection (Pinho & Reis, 2015). Therapeutic interventions targeting this system often involve small molecules or glycan mimetics designed to block the interaction between these host glycans and their binding partners. For example, galectin inhibitors are currently being investigated in clinical trials for the treatment of liver fibrosis, non-alcoholic steatohepatitis (NASH), and various solid tumors (Blanchard et al., 2014). These drugs work by competitively binding to the carbohydrate-recognition domains of galectins, preventing them from cross-linking host glycans and triggering pathological signaling pathways.
Competitive inhibition of the interaction between host galactose-containing glycans and their binding partners, such as galectins or microbial adhesins.
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