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Crystal Structure of the Japanese Encephalitis Virus Capsid Protein

1
Molecular Biophysics Group, Institute of Integrative Biology, Faculty of Health and Life Sciences, University of Liverpool, L69 7ZB Liverpool, UK
2
Health Protection Research Unit on Emerging and Zoonotic Infections, Institute of Infection and Global Health, University of Liverpool, L69 7BE Liverpool, UK
3
Walton Centre NHS Foundation Trust, L9 7LJ Liverpool, UK
*
Author to whom correspondence should be addressed.
Current address: Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794, USA.
Viruses 2019, 11(7), 623; https://doi.org/10.3390/v11070623
Received: 3 June 2019 / Revised: 1 July 2019 / Accepted: 4 July 2019 / Published: 6 July 2019
(This article belongs to the Special Issue Neuroinvasive Viral Infections)
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Abstract

Japanese encephalitis (JE) is inflammation and swelling of the brain caused by the JE virus (JEV), a mosquito-borne member of the Flavivirus family. There are around 68,000 JE cases worldwide each year, many of which result in permanent brain damage and death. There is no specific treatment for JE. Here we present the crystal structure of the JEV capsid protein, a potential drug target, at 1.98 Å, and compare it to other flavivirus capsid proteins. The JEV capsid has a helical secondary structure (α helixes 1–4) and a similar protein fold to the dengue virus (DENV), the West Nile virus (WNV), and the Zika virus (ZIKV) capsid proteins. It forms a homodimer by antiparallel pairing with another subunit (‘) through α-helix 1-1’, 2-2’, and 4-4’ interactions. This dimeric form is believed to be the building block of the nucleocapsid. The flexibility of the N-terminal α helix-1 allows the formation of closed and open conformations with possible functional importance. The basic C-terminal pairing of α4-4’ forms a coiled-coil-like structure, indicating possible nucleic acid binding functionality. However, a comparison with other nucleic acid interacting domains indicates that homodimerization would preclude binding. This is the first JEV capsid protein to be described and is an addition to the structural biology of the Flavivirus. View Full-Text
Keywords: flavivirus; core protein; x-ray crystallography; homodimer flavivirus; core protein; x-ray crystallography; homodimer
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Poonsiri, T.; Wright, G.S.A.; Solomon, T.; Antonyuk, S.V. Crystal Structure of the Japanese Encephalitis Virus Capsid Protein. Viruses 2019, 11, 623.

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