ArticleJournal of virology2016
Inhibition of the Membrane Attack Complex by Dengue Virus NS1 through Interaction with Vitronectin and Terminal Complement Proteins.
Article in Journal of virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 95 citations in OpenAlex.
- Dengue NS1 as a Driver of Immune-Mediated Pathogenesis.Tropical medicine and infectious disease · 2026Review
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- Plasmonic sensors for dengue virus detection: technological advances, challenges, future directions.Mikrochimica acta · 2026Review
- SARS-CoV-2 nucleocapsid protein forms complexes with soluble complement regulatory proteins that can bind to the virion.Scientific reports · 2026Article
- Pathogenicity and virulence of Powassan virus.Virulence · 2025Review
- Review
- Dengue Virus and the Host Immune System: A Battle of Immune Modulation, Response and Evasion.Pathogens (Basel, Switzerland) · 2025Review
- Dengue virus NS1 protein does not activate TLR4 and has a modest effect on endothelial monolayer integrity compared to TNF.PLoS pathogens · 2025Article
- The grand escape - how pathogens outsmart the human complement system.Immunobiology · 2025Review
- Review
- Review
- A non-structural protein 1 substitution of dengue virus enhances viral replication by interfering with the antiviral signaling pathway.Journal of biomedical science · 2025Article
- Article
- The complement system: A key player in the host response to infections.European journal of immunology · 2024Review
- The Complement System as a Part of Immunometabolic Post-Exercise Response in Adipose and Muscle Tissue.International journal of molecular sciences · 2024Review
- The N and C-terminal deleted variant of the dengue virus NS1 protein is a potential candidate for dengue vaccine development.Scientific reports · 2024Article
- Development of a quantitative NS1 antigen enzyme-linked immunosorbent assay (ELISA) for Zika virus detection using a novel virus-specific mAb.Scientific reports · 2024Article
- Plasmid-encoded toxin ofFrontiers in cellular and infection microbiology · 2024Article
- Article
- Metabolomic and Proteomic Profiling of Porcine Intestinal Epithelial Cells Infected with Porcine Epidemic Diarrhea Virus.International journal of molecular sciences · 2023Article
2 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dengue virus (DENV) infects millions of people worldwide and is a major public health problem. DENV nonstructural protein 1 (NS1) is a conserved glycoprotein that associates with membranes and is also secreted into the plasma in DENV-infected patients. The present study describes a novel mechanism by which NS1 inhibits the terminal complement pathway. We first identified the terminal complement regulator vitronectin (VN) as a novel DENV2 NS1 binding partner by using a yeast two-hybrid system. This interaction was further assessed by enzyme-linked immunosorbent assay (ELISA) and surface plasmon resonance (SPR) assay. The NS1-VN complex was also detected in plasmas from DENV-infected patients, suggesting that this interaction occurs during DENV infection. We also demonstrated that the DENV2 NS1 protein, either by itself or by interacting with VN, hinders the formation of the membrane attack complex (MAC) and C9 polymerization. Finally, we showed that DENV2, West Nile virus (WNV), and Zika virus (ZIKV) NS1 proteins produced in mammalian cells inhibited C9 polymerization. Taken together, our results points to a role for NS1 as a terminal pathway inhibitor of the complement system. IMPORTANCE: Dengue is the most important arthropod-borne viral disease nowadays and is caused by dengue virus (DENV). The flavivirus NS1 glycoprotein has been characterized functionally as a complement evasion protein that can attenuate the activation of the classical, lectin, and alternative pathways. The present study describes a novel mechanism by which DENV NS1 inhibits the terminal complement pathway. We identified the terminal complement regulator vitronectin (VN) as a novel DENV NS1 binding partner, and the NS1-VN complex was detected in plasmas from DENV-infected patients, suggesting that this interaction occurs during DENV infection. We also demonstrated that the NS1-VN complex inhibited membrane attack complex (MAC) formation, thus interfering with the complement terminal pathway. Interestingly, NS1 itself also inhibited MAC activity, suggesting a direct role of this protein in the inhibition process. Our findings imply a role for NS1 as a terminal pathway inhibitor of the complement system.
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