ArticleScientific reports2024
The N and C-terminal deleted variant of the dengue virus NS1 protein is a potential candidate for dengue vaccine development.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- NS1 of Duck Tembusu Virus Interacts with CCT2: Reduced CCT2 Recovery in LC3C Co-Immunoprecipitation In Vitro and the Proviral Role of CCT2 in DTMUV Infection.Veterinary sciences · 2026Article
- Uncovering the Unique Epitopes: Validation of In-Silico Synthesized Tetravalent Dengue Vaccine (dvac) Through Cloning, Expression, and Immunogenic Analysis.Molecular biotechnology · 2026Article
- Targeting dengue through mucosal vaccination: the potential of NS1 and bacterial spore-based delivery platforms.Frontiers in immunology · 2026Review
- Structural and energetic basis of marine phytochemicals as dengue NS1 protein inhibitors.Scientific reports · 2025Article
- Advancements in dengue vaccines: A historical overview and pro-spects for following next-generation candidates.Journal of microbiology (Seoul, Korea) · 2025Review
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
NS1 is an elusive dengue protein, involved in viral replication, assembly, pathogenesis, and immune evasion. Its levels in blood plasm are positively related to disease severity like thrombocytopenia, hemorrhage, and vascular leakage. Despite its pathogenic roles, NS1 is being used in various vaccine formulations due to its sequence conservancy, ability to produce protective antibodies and low risk for inducing antibody-dependent enhancement. In this study, we have used bioinformatics tools and reported literature to develop an NS1 variant (dNS1). Molecular docking studies were performed to evaluate the receptor-binding ability of the NS1 and dNS1 with TLR4. NS1 and dNS1 (153 to 312 amino acid region) genes were cloned, expressed and protein was purified followed by refolding. Docking studies showed the binding of NS1 and dNS1 with the TLR4 receptor which suggests that N and C-terminal sequences of NS1 are not critical for receptor binding. Antibodies against NS1 and dNS1 were raised in rabbits and binding affinity of anti-dNS1 anti-NS1 sera was evaluated against both NS1 and dNS1. Similar results were observed through western blotting which highlight that N and C-terminal deletion of NS1 does not compromise the immunogenic potential of dNS1 hence, supports its use in future vaccine formulations as a substitute for NS1.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.