ArticleScientific reports2019
Dengue virus nonstructural 3 protein interacts directly with human glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and reduces its glycolytic activity.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 50 citations in OpenAlex.
- Maltase 1 regulates DENV2 infection and life history in Aedes aegypti.Insect science · 2026Article
- An investigation of fucoidan as a potential inhibitor against DENV/NS3 proteases through molecular dynamics simulations and DFT studies.Journal of molecular modeling · 2025Article
- Investigating how dengue virus-induced metabolic changes affect the host immune response and how to develop Immunomodulatory strategies.Virology journal · 2025Review
- Identification of Potential Inhibitors Targeting Non-Structural Proteins NS3 and NS5 of Dengue Virus Using Docking and Deep Learning Approaches.Pharmaceuticals (Basel, Switzerland) · 2025Article
- A comprehensive overview on the crosstalk between microRNAs and viral pathogenesis and infection.Medicinal research reviews · 2025Review
- Current status of the development of dengue vaccines.Vaccine: X · 2025Review
- Alteration of mitochondrial function in arthropods during arboviruses infection: a review of the literature.Frontiers in physiology · 2025Review
- Molecular docking analysis of zidovudine triphosphate with conserved residues from NS3 protein.Bioinformation · 2025Article
- The Inhibition of NS2B/NS3 Protease: A New Therapeutic Opportunity to Treat Dengue and Zika Virus Infection.International journal of molecular sciences · 2024Review
- Glycolysis is reduced in dengue virus 2 infected liver cells.Scientific reports · 2024Article
- Review
- Article
- Lactate facilitates classical swine fever virus replication by enhancing cholesterol biosynthesis.iScience · 2022Article
- Seeking heterocyclic scaffolds as antivirals against dengue virus.European journal of medicinal chemistry · 2022Review
- Identification of Aedes aegypti salivary gland proteins interacting with human immune receptor proteins.PLoS neglected tropical diseases · 2022Article
- Yeast Two-Hybrid System for Mapping Novel Dengue Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Review
- 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
- Structure and Dynamics of Zika Virus Protease and Its Insights into Inhibitor Design.Biomedicines · 2021Review
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dengue is an important mosquito-borne disease and a global public health problem. The disease is caused by dengue virus (DENV), which is a member of the Flaviviridae family and contains a positive single-stranded RNA genome that encodes a single precursor polyprotein that is further cleaved into structural and non-structural proteins. Among these proteins, the non-structural 3 (NS3) protein is very important because it forms a non-covalent complex with the NS2B cofactor, thereby forming the functional viral protease. NS3 also contains a C-terminal ATPase/helicase domain that is essential for RNA replication. Here, we identified 47 NS3-interacting partners using the yeast two-hybrid system. Among those partners, we highlight several proteins involved in host energy metabolism, such as apolipoprotein H, aldolase B, cytochrome C oxidase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). GAPDH directly binds full-length NS3 and its isolated helicase and protease domains. Moreover, we observed an intense colocalization between the GAPDH and NS3 proteins in DENV2-infected Huh7.5.1 cells, in NS3-transfected BHK-21 cells and in hepatic tissue from a fatal dengue case. Taken together, these results suggest that the human GAPDH-DENV NS3 interaction is involved in hepatic metabolic alterations, which may contribute to the appearance of steatosis in dengue-infected patients. The interaction between GAPDH and full-length NS3 or its helicase domain in vitro as well as in NS3-transfected cells resulted in decreased GAPDH glycolytic activity. Reduced GAPDH glycolytic activity may lead to the accumulation of metabolic intermediates, shifting metabolism to alternative, non-glycolytic pathways. This report is the first to identify the interaction of the DENV2 NS3 protein with the GAPDH protein and to demonstrate that this interaction may play an important role in the molecular mechanism that triggers hepatic alterations.
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