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Sialic acid-containing glycans and heparan sulfate glycans are complex carbohydrate structures found on the surfaces of both host cells and various microorganisms. These molecules serve as critical attachment factors and coreceptors for a wide range of pathogens, including influenza viruses, herpesviruses, and coronaviruses, which utilize them to facilitate initial docking and subsequent entry into host cells (Varki, A., 2008, Nature; Lopes, C.C. et al., 2006, Glycobiology). In addition to their role in pathogenesis, these glycans are essential for normal physiological processes such as cell-cell communication, signal transduction, and the maintenance of the extracellular matrix (Bishop, J.R. et al., 2007, Nature). Therapeutic interventions targeting these glycans typically employ decoy mimetics that competitively bind to pathogen surface proteins or enzymes like sialidases that remove the glycan receptors from the host cell surface (Triana-Baltzer, G.B. et al., 2009, PLoS ONE). Such strategies offer the potential for broad-spectrum antimicrobial activity by targeting conserved entry mechanisms (Cagno, V. et al., 2018, Nature Materials). However, the ubiquity of these glycans presents challenges, as therapeutic agents must avoid interfering with vital host functions like blood coagulation and immune regulation.
Competitive inhibition of pathogen attachment to host cells via glycan mimetics or enzymatic depletion of host cell surface glycan receptors.
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