ArticleVirology journal2016
Recombinant Dengue virus protein NS2B alters membrane permeability in different membrane models.
Article in Virology journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 183 citations in OpenAlex.
- Zika virus recruits karyopherin α6 for efficient replication via NS2B.Journal of virology · 2026Article
- The Impacts of Dengue Virus Infection on Mitochondrial Functions and Dynamics.International journal of molecular sciences · 2025Review
- Super-resolution optical microscopy reveals accumulation of photoactivable dengue protein (Dendra2-NS2B) in the endoplasmic reticulum.Scientific reports · 2025Article
- Review
- Review
- Seeking heterocyclic scaffolds as antivirals against dengue virus.European journal of medicinal chemistry · 2022Review
- Review
- Review
- Drugs to limit Zika virus infection and implication for maternal-fetal health.Frontiers in virology (Lausanne, Switzerland) · 2022Article
- Functions of Viroporins in the Viral Life Cycle and Their Regulation of Host Cell Responses.Frontiers in immunology · 2022Review
- Review
- Article
- Compartmentalized replication organelle of flavivirus at the ER and the factors involved.Cellular and molecular life sciences : CMLS · 2021Review
- Review
- Dengue Virus Serotype 2 Intrahost Diversity in Patients with Different Clinical Outcomes.Viruses · 2021Article
- Anti-flavivirus Properties of Lipid-Lowering Drugs.Frontiers in physiology · 2021Review
- Dengue Virus Envelope Protein Domain III Induces Nlrp3 Inflammasome-Dependent NETosis-Mediated Inflammation in Mice.Frontiers in immunology · 2021Article
- Heterocyclic Inhibitors of Viroporins in the Design of Antiviral Compounds.Chemistry of heterocyclic compounds · 2020Article
- Inflammasome Fuels Dengue Severity.Frontiers in cellular and infection microbiology · 2020Review
- Dengue Virus Serotype 2 and Its Non-Structural Proteins 2A and 2B Activate NLRP3 Inflammasome.Frontiers in immunology · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundOne of the main phenomena occurring in cellular membranes during virus infection is a change in membrane permeability. It has been observed that numerous viral proteins can oligomerize and form structures known as viroporins that alter the permeability of membranes. Previous findings have identified such proteins in cells infected with Japanese encephalitis virus (JEV), a member of the same family that Dengue virus (DENV) belongs to (Flaviviridae). In the present work, we investigated whether the small hydrophobic DENV protein NS2B serves a viroporin function.
methodsWe cloned the DENV NS2B sequence and expressed it in a bacterial expression system. Subsequently, we evaluated the effect of DENV NS2B on membranes when NS2B was overexpressed, measured bacterial growth restriction, and evaluated changes of permeability to hygromycin. The NS2B protein was purified by affinity chromatography, and crosslinking assays were performed to determine the presence of oligomers. Hemolysis assays and transmission electron microscopy were performed to identify structures involved in permeability changes.
resultsThe DENV-2 NS2B protein showed similitude with the JEV viroporin. The DENV-2 NS2B protein possessed the ability to change the membrane permeability in bacteria, to restrict bacterial cell growth, and to enable membrane permeability to hygromycin B. The NS2B protein formed trimers that could participate in cell lysis and generate organized structures on eukaryotes membranes.
conclusionsOur data suggest that the DENV-2 NS2B viral protein is capable of oligomerizing and organizing to form pore-like structures in different lipid environments, thereby modifying the permeability of cell membranes.
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