Sialic acid-bearing surface receptor (SA-receptor)

Sialic acid-bearing surface receptors are a diverse group of glycoproteins and glycolipids characterized by terminal sialic acid residues, which serve as the primary attachment points for various pathogens, including the Newcastle Disease Virus (NDV) [PMID: 11160744]. In the context of NDV, the viral hemagglutinin-neuraminidase (HN) protein recognizes and binds to these sialic acid moieties, while the fusion (F) protein facilitates the merging of the viral envelope with the host cell membrane [PMID: 15220444]. These receptors are frequently overexpressed on the surface of many cancer cells, a phenomenon known as hypersialylation, which contributes to the selective oncolytic properties of NDV [PMID: 22431868]. By targeting these receptors, NDV can preferentially infect, replicate within, and eventually lyse tumor cells while sparing most normal human cells [PMID: 17560176]. Beyond their role in viral entry, sialic acid receptors are involved in critical biological processes such as cell-cell adhesion, signal transduction, and immune system regulation [PMID: 12676068]. Therapeutic strategies leveraging these receptors often involve oncolytic virotherapy or the development of sialic acid-mimetic drugs to interfere with pathological interactions [PMID: 25403444].

Other names

Sialic acid receptorSialoglycanN-acetylneuraminic acid-containing receptorSialoglycoproteinSialoglycolipid

The Newcastle Disease Virus (NDV) hemagglutinin-neuraminidase (HN) protein binds to terminal sialic acid residues (specifically alpha-2,3 and alpha-2,6 linkages) on host cell surface glycoproteins and glycolipids [PMID: 11160744]. This binding event triggers a conformational change in the associated fusion (F) protein, which then inserts its fusion peptide into the host cell membrane, mediating membrane fusion and viral entry [PMID: 15220444]. In tumor cells, the high density of these receptors facilitates efficient viral attachment and subsequent oncolysis [PMID: 22431868].