Sialylated cell-surface glycans bearing α2,3-linked sialic acid (α2,3-Sia)

Sialylated cell-surface glycans bearing α2,3-linked sialic acid are terminal carbohydrate structures where N-acetylneuraminic acid is linked to the third carbon of a galactose residue. These glycans serve as essential receptors for various pathogens, most notably avian influenza viruses like H5N1, which preferentially bind to α2,3-linkages found in the avian gut and human lower respiratory tract (Source: PubMed PMID: 21835002). In human physiology, these structures are involved in critical processes such as cell-cell recognition and the modulation of immune responses. In the context of oncology, the upregulation of α2,3-sialyltransferases leads to an abundance of these glycans, which is often correlated with increased tumor cell invasiveness and metastasis (Source: PubMed PMID: 25635353). Therapeutic strategies targeting these glycans include the use of recombinant sialidases, such as DAS181, which enzymatically cleave the sialic acid to prevent viral entry (Source: NIH/ClinicalTrials.gov). Additionally, neuraminidase inhibitors like oseltamivir indirectly interact with this system by preventing the virus from detaching from these glycans during the budding process. Understanding the distribution and density of these α2,3-linked structures is vital for predicting the pandemic potential of emerging influenza strains.

Other names

Neu5Acα2-3GalAlpha-2,3-sialic acidAvian influenza receptorα2,3-linked sialylglycanα2,3-linked N-acetylneuraminic acid

Enzymatic removal of terminal sialic acid residues from the host cell surface to prevent viral attachment, or inhibition of viral neuraminidase to prevent the release of new virions from sialic acid-containing receptors.