Hepatitis E virus capsid protein ORF2 P-domain (HEV ORF2 P-domain)

The Hepatitis E virus (HEV) capsid protein ORF2 P-domain is the outermost structural component of the HEV virion, forming prominent surface spikes essential for viral infectivity (Yamashita et al., 2009, PNAS). It plays a critical role in the viral life cycle by mediating attachment to host cell receptors, including heparan sulfate proteoglycans (HSPGs), which is a necessary step for viral entry into hepatocytes (Gu et al., 2013, Journal of Virology). As the primary site for neutralizing epitopes, the P-domain is the central target for vaccine development and therapeutic antibody design (UniProt P0C0X4). The only licensed HEV vaccine, Hecolin (HEV 239), consists of a recombinant fragment of the P-domain (residues 368–606) that self-assembles into virus-like particles to elicit a protective immune response (Zhu et al., 2010, The Lancet). Targeting this domain aims to prevent viral attachment and subsequent infection, making it a focal point for both preventative and potential therapeutic interventions against hepatitis E.

Other names

ORF2 protrusion domainHEV capsid P-domainHEV ORF2pHEV 239 antigenCapsid protein P-domain

Induction of neutralizing antibodies that block viral attachment to host cell receptors and prevent viral entry; competitive inhibition of receptor binding sites.