{"@type": "dcat:Dataset", "accessLevel": "public", "bureauCode": ["009:25"], "contactPoint": {"@type": "vcard:Contact", "fn": "NIH", "hasEmail": "mailto:info@nih.gov"}, "description": "Hepatitis E virus (HEV) is the causative agent of hepatitis E, an\nacute form of viral hepatitis. The open reading frame 2 (ORF2) of HEV encodes the viral capsid protein, which can self-oligomerize into virus-like particles. To understand the domains within this protein important for capsid biogenesis, we have carried out in vitro analyses of association and folding patterns of wild type and mutant ORF2 proteins. When expressed in vitro or in transfected cells, the ORF2\nprotein assembled as dimers, trimers and higher order forms. While\nN-terminal deletions up to 111 amino acids had no effect, the deletion of amino acids 585\u2013610 led to reduced homo-oligomerization. This deletion also resulted in aberrant folding of the protein, as determined by its sensitivity to trypsin. This study suggests that a C-terminal hydrophobic region encompassing amino acids 585\u2013610 of the ORF2 protein might be critical for capsid biogenesis.", "distribution": [{"@type": "dcat:Distribution", "description": "Visit the original government dataset for complete information, documentation, and data access.", "downloadURL": "https://www.ncbi.nlm.nih.gov/pmc/articles/PMC129057/", "mediaType": "text/html", "title": "Official Government Data Source"}], "identifier": "https://healthdata.gov/api/views/5cnt-rnep", "issued": "2025-07-14", "keyword": ["hepatitis-e-virus", "homo-oligomerization", "nih", "orf2-protein", "viral-capsid-protein"], "landingPage": "https://healthdata.gov/d/5cnt-rnep", "modified": "2025-09-06", "programCode": ["009:033"], "publisher": {"@type": "org:Organization", "name": "National Institutes of Health"}, "theme": ["NIH"], "title": "A C-terminal hydrophobic region is required for homo-oligomerization of the hepatitis E virus capsid (ORF2) protein"}