ArticleViruses2019
Crystal Structure of the Japanese Encephalitis Virus Capsid Protein.
Article in Viruses, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Beyond the Capsid: How Can Post-Translational Modifications Modulate the Multifunctionality of the Orthoflavivirus Capsid Protein?Molecules (Basel, Switzerland) · 2026Review
- Article
- A Bovine Cell Line Resistant to Japanese Encephalitis Virus Entry but Permissive to Post-Entry Replication.Viruses · 2026Article
- Annexin A2 facilitates Japanese encephalitis virus replication by regulating endocytosis and intracellular transport in PK15 cells.Frontiers in microbiology · 2026Article
- An Updated Review of Potential Drug Targets for Japanese Encephalitis.Central nervous system agents in medicinal chemistry · 2026Review
- The alarming spread of Japanese encephalitis: A growing public health concern.Open veterinary journal · 2025Review
- Article
- Zika virus capsid protein closed structure modulates binding to host lipid systems.Protein science : a publication of the Protein Society · 2024Article
- Characterization of a Small Plaque Variant Derived from Genotype V Japanese Encephalitis Virus Clinical Isolate K15P38.Journal of microbiology and biotechnology · 2024Article
- Importin-7-dependent nuclear translocation of the Flavivirus core protein is required for infectious virus production.PLoS pathogens · 2024Article
- Computational Exploration of Potential Pharmacological Inhibitors Targeting the Envelope Protein of the Kyasanur Forest Disease Virus.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Japanese encephlu emergence in Australia: the potential population at risk.Annals of medicine and surgery (2012) · 2024Review
- The Dynamic Landscape of Capsid Proteins and Viral RNA Interactions in Flavivirus Genome Packaging and Virus Assembly.Pathogens (Basel, Switzerland) · 2024Review
- Review
- Identification of a critical role for ZIKV capsid α3 in virus assembly and its genetic interaction with M protein.PLoS neglected tropical diseases · 2024Article
- Mice as an Animal Model for Japanese Encephalitis Virus Research: Mouse Susceptibility, Infection Route, and Viral Pathogenesis.Pathogens (Basel, Switzerland) · 2023Review
- Review
- Simultaneous membrane and RNA binding by tick-borne encephalitis virus capsid protein.PLoS pathogens · 2023Article
- Molecular Mechanism and Role of Japanese Encephalitis Virus Infection in Central Nervous System-Mediated Diseases.Viruses · 2022Review
- Antiviral drug research for Japanese encephalitis: an updated review.Pharmacological reports : PR · 2022Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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.
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