ArticleJournal of biomedical science2009
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interaction with 3' ends of Japanese encephalitis virus RNA and colocalization with the viral NS5 protein.
Article in Journal of biomedical science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 50 citations in OpenAlex.
- Article
- Glyceraldehyde-3-Phosphate Dehydrogenase Restricted in Cytoplasmic Location by Viral GP5 Facilitates Porcine Reproductive and Respiratory Syndrome Virus Replication via Its Glycolytic Activity.Journal of virology · 2021Article
- Transcriptome-level assessment of the impact of deformed wing virus on honey bee larvae.Scientific reports · 2021Article
- Target Identification Using Homopharma and Network-Based Methods for Predicting Compounds Against Dengue Virus-Infected Cells.Molecules (Basel, Switzerland) · 2020Article
- Universal RNAFrontiers in microbiology · 2020Review
- Review
- Dengue virus nonstructural 3 protein interacts directly with human glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and reduces its glycolytic activity.Scientific reports · 2019Article
- IFIT5 Participates in the Antiviral Mechanisms of Rainbow Trout Red Blood Cells.Frontiers in immunology · 2019Article
- Citrus tristeza virus co-opts glyceraldehyde 3-phosphate dehydrogenase for its infectious cycle by interacting with the viral-encoded protein p23.Plant molecular biology · 2018Article
- Review
- Engineering of soybean mosaic virus as a versatile tool for studying protein-protein interactions in soybean.Scientific reports · 2016Article
- Functions of the 3' and 5' genome RNA regions of members of the genus Flavivirus.Virus research · 2015Review
- Occurrence of a multimeric high-molecular-weight glyceraldehyde-3-phosphate dehydrogenase in human serum.Journal of proteome research · 2015Article
- Japanese encephalitis virus nonstructural protein NS5 interacts with mitochondrial trifunctional protein and impairs fatty acid β-oxidation.PLoS pathogens · 2015Article
- The interface between methyltransferase and polymerase of NS5 is essential for flavivirus replication.PLoS neglected tropical diseases · 2014Article
- Ultrastructural characterization and three-dimensional architecture of replication sites in dengue virus-infected mosquito cells.Journal of virology · 2014Article
- Modulation of neuronal proteome profile in response to Japanese encephalitis virus infection.PloS one · 2014Article
- Proteomics analysis of the DF-1 chicken fibroblasts infected with avian reovirus strain S1133.PloS one · 2014Article
- Review
- Effects of cocktail of four local Malaysian medicinal plants (Phyllanthus spp.) against dengue virus 2.BMC complementary and alternative medicine · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Replication of the Japanese encephalitis virus (JEV) genome depends on host factors for successfully completing their life cycles; to do this, host factors have been recruited and/or relocated to the site of viral replication. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a cellular metabolic protein, was found to colocalize with viral RNA-dependent RNA polymerase (NS5) in JEV-infected cells. Subcellular fractionation further indicated that GAPDH remained relatively constant in the cytosol, while increasing at 12 to 24 hours postinfection (hpi) and decreasing at 36 hpi in the nuclear fraction of infected cells. In contrast, the redistribution patterns of GAPDH were not observed in the uninfected cells. Co-immunoprecipitation of GAPDH and JEV NS5 protein revealed no direct protein-protein interaction; instead, GAPDH binds to the 3' termini of plus- and minus-strand RNAs of JEV by electrophoretic mobility shift assays. Accordingly, GAPDH binds to the minus strand more efficiently than to the plus strand of JEV RNAs. This study highlights the findings that infection of JEV changes subcellular localization of GAPDH suggesting that this metabolic enzyme may play a role in JEV replication.
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