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The Human parainfluenza virus type 2 Hemagglutinin-neuraminidase (HPIV-2 HN) protein is a multifunctional type II integral membrane glycoprotein essential for the viral life cycle (UniProt: P12564). It mediates the initial attachment of the virus to sialic acid-containing receptors on the surface of host respiratory epithelial cells and subsequently triggers the fusion protein (F) to facilitate viral entry (PubMed: 19100603). Additionally, its neuraminidase (sialidase) activity cleaves sialic acid from host cell receptors and progeny virions, preventing viral self-aggregation and enabling the release of new virus particles from infected cells (PubMed: 15220455). HPIV-2 is a significant cause of upper and lower respiratory tract illnesses, particularly croup and bronchiolitis in infants and young children (CDC). Because of its critical roles in both entry and exit, the HN protein is a primary target for the development of antiviral drugs, such as the sialic acid analog BCX 2798, and is a key focus for vaccine design (PubMed: 11752709).
Inhibition of the neuraminidase active site to prevent viral release and blocking the receptor-binding site to prevent viral attachment to host cells.
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