Alpha-2,3-linked sialic acid receptor (Sia) (Sia)

The Mumps virus entry receptors are primarily composed of sialic acid residues, with a specific preference for alpha-2,3-linked sialic acids found on host cell surface glycoproteins and glycolipids (Kubota et al., 2016, PNAS). The Mumps virus (MuV) initiates infection through its hemagglutinin-neuraminidase (HN) protein, which recognizes and attaches to these sialic acid moieties (Rother et al., 2018, Journal of Virology). This binding event triggers the viral fusion (F) protein to mediate the merging of the viral envelope with the host cell membrane, allowing the viral genome to enter the cytoplasm. Because sialic acids are ubiquitously expressed, MuV exhibits a broad tissue tropism, leading to systemic symptoms and complications such as parotitis, meningitis, and orchitis (CDC, 2021). Therapeutic strategies targeting this entry pathway include the use of sialidases like DAS181 (Fludase), which enzymatically remove sialic acid from the respiratory epithelium to block viral attachment (Malakhov et al., 2006, Antimicrobial Agents and Chemotherapy). Other research efforts focus on developing small-molecule inhibitors or neutralizing antibodies that specifically disrupt the HN-sialic acid interaction to prevent infection.

Other names

Sialic acidN-acetylneuraminic acidNeu5AcAlpha-2,3-sialylglycanMumps virus receptor

Sialidase-mediated cleavage of terminal sialic acid residues from host cell surface receptors, which prevents the binding of the viral hemagglutinin-neuraminidase (HN) protein and subsequent viral entry.