Viral attachment to host cell surface glycoconjugates

Viral attachment to host cell surface glycoconjugates is a critical initial step in the infection cycle of many viruses, where viral surface proteins bind to specific carbohydrate moieties on the host cell membrane (Maginnis, 2018). These glycoconjugates, which include heparan sulfate proteoglycans (HSPGs), sialic acids, and various glycoproteins or glycolipids, serve as primary attachment factors or co-receptors that concentrate viruses on the cell surface and facilitate subsequent interaction with high-affinity entry receptors (Stencel-Baerenwald et al., 2014). For instance, influenza viruses utilize hemagglutinin to bind sialic acids, while viruses like herpes simplex virus (HSV) and SARS-CoV-2 often utilize HSPGs for initial docking (Koehler et al., 2020). Targeting this interaction involves the use of glycan mimetics, lectins, or enzymes that modify the host glycome to prevent viral adsorption (Cagno et al., 2019). While broad-spectrum potential exists, therapeutic challenges include the high diversity of glycan structures and the potential for interfering with essential physiological processes mediated by these same glycoconjugates, such as blood coagulation or growth factor signaling (Stencel-Baerenwald et al., 2014).

Other names

Viral adsorption to host glycansGlycan-mediated viral entryHeparan sulfate-mediated viral attachmentSialic acid-mediated viral bindingViral docking to cell surface glycoconjugates

Competitive inhibition of viral attachment to host cell surface glycoconjugates by mimicking host glycans or enzymatically depleting host receptors.