Human parainfluenza virus type 3 Hemagglutinin-neuraminidase (HPIV3 HN)

Human parainfluenza virus type 3 Hemagglutinin-neuraminidase (HPIV3 HN) is a multifunctional type II transmembrane glycoprotein essential for the viral infection cycle. It mediates the initial attachment of the virus to sialic acid-containing receptors on the surface of host respiratory epithelial cells and works coordinately with the fusion (F) protein to trigger membrane fusion and viral entry (Source: UniProt P08491; PubMed: 15140980). The protein also possesses neuraminidase (sialidase) activity, which cleaves sialic acid from host cell surfaces and progeny virions, preventing viral aggregation and facilitating the release of new virus particles (Source: PubMed: 22438551). Given its central role in both entry and exit, HPIV3 HN is a primary target for neutralizing antibodies and the development of antiviral drugs, such as sialidase inhibitors like BCX 2798 (Source: PubMed: 11742030). It is a major cause of lower respiratory tract infections, including bronchiolitis and pneumonia, particularly in infants, the elderly, and immunocompromised individuals (Source: NIH/NCBI). Therapeutic strategies often focus on inhibiting the enzymatic site or blocking the receptor-binding domain to halt viral spread.

Other names

HN proteinHemagglutinin-neuraminidase glycoproteinHPIV-3 HNSialidaseHPIV3 HN protein

Inhibition of viral neuraminidase activity to prevent progeny release and blocking of sialic acid receptor binding to prevent viral attachment.