2009/07/21 by Tom S. Y. Guu, Zheng Liu, Qiaozhen Ye +5 · 1 citation
Medicine · #Hepatitis Viruses Studies and Epidemiology #Viral gastroenteritis research and epidemiology #Viral Infections and Immunology Research
paper · doi:10.1073/pnas.0904848106
openalex publication_date 2009/07/21 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/28
Hepatitis E virus (HEV), a small, non-enveloped RNA virus in the family Hepeviridae, is associated with endemic and epidemic acute viral hepatitis in developing countries. Our 3.5-A structure of a HEV-like particle (VLP) shows that each capsid protein contains 3 linear domains that form distinct structural elements: S, the continuous capsid; P1, 3-fold protrusions; and P2, 2-fold spikes. The S domain adopts a jelly-roll fold commonly observed in small RNA viruses. The P1 and P2 domains both adopt beta-barrel folds. Each domain possesses a potential polysaccharide-binding site that may function in cell-receptor binding. Sugar binding to P1 at the capsid protein interface may lead to capsid disassembly and cell entry. Structural modeling indicates that native T = 3 capsid contains flat dimers, with less curvature than those of T = 1 VLP. Our findings significantly advance the understanding of HEV molecular biology and have application to the development of vaccines and antiviral medications.