The DOI matches its Crossref record; 56 of the 56 references it cites were found in a registry or an index.
Structure of the hepatitis E virus-like particle suggests mechanisms for virus assembly and receptor binding
Open accessAbstract
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-Å 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 β-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.
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Cited by
Kamar, N., Dalton, H. R., Abravanel, F., & Izopet, J. (2014) · Clinical Microbiology Reviews · doi:10.1128/cmr.00057-13 · Cited by 675
Metadata
- Authors
- Guu, T. S. Y., Liu, Z., Ye, Q., Mata, D. A., Li, K., Yin, C., Zhang, J., & Tao, Y. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2009-08-04
- Volume
- 106
- Issue
- 31
- Pages
- 12992-12997
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2106555961
- Cited by
- 255
- References
- 56
- FWCI
- 8.64
- Type
- journal article
- Language
- en
- Open access
- green
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