ArticleJournal of virology2011
The helical domains of the stem region of dengue virus envelope protein are involved in both virus assembly and entry.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 58 citations in OpenAlex.
- ZDHHC11-mediated palmitoylation of viral envelope protein restricts dengue virus replication: implication for the development of universal anti-flavivirus therapeutic strategies.Virology journal · 2026Article
- Development of New Live-Attenuated Vaccine Candidates Lacking Antibody-Dependent Enhancement (ADE) Against Dengue.Vaccines · 2025Review
- Genomic hotspots in the DENV-2 serotype (E, NS4B, and NS5 genes) are associated with dengue disease severity in the endemic region of India.PLoS neglected tropical diseases · 2025Article
- Dual EMCV-IRES-integrated dengue virus can express an exogenous gene and cellular Mdm2 integration suppresses the dengue viral replication.Frontiers in microbiology · 2025Article
- Broad-spectrum activity against mosquito-borne flaviviruses achieved by a targeted protein degradation mechanism.Nature communications · 2024Article
- Exploring the Targets of Dengue Virus and Designs of Potential Inhibitors.Combinatorial chemistry & high throughput screening · 2024Article
- Flavivirus genome recoding by codon optimisation confers genetically stable in vivo attenuation in both mice and mosquitoes.PLoS pathogens · 2023Article
- Structure-first identification of RNA elements that regulate dengue virus genome architecture and replication.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Sites of vulnerability in HCV E1E2 identified by comprehensive functional screening.Cell reports · 2022Article
- Article
- The key amino acids of E protein involved in early flavivirus infection: viral entry.Virology journal · 2021Review
- Substantial Attenuation of Virulence of Tembusu Virus Strain PS Is Determined by an Arginine at Residue 304 of the Envelope Protein.Journal of virology · 2021Article
- Comparison of Neutralizing Dengue Virus B Cell Epitopes and Protective T Cell Epitopes With Those in Three Main Dengue Virus Vaccines.Frontiers in immunology · 2021Article
- Substitutions at Loop Regions of TMUV E Protein Domain III Differentially Impair Viral Entry and Assembly.Frontiers in microbiology · 2021Article
- Animal models of congenital zika syndrome provide mechanistic insight into viral pathogenesis during pregnancy.PLoS neglected tropical diseases · 2020Review
- A cocrystal structure of dengue capsid protein in complex of inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Using Next Generation Sequencing to Study the Genetic Diversity of Candidate Live Attenuated Zika Vaccines.Vaccines · 2020Article
- Synthetic nucleic acid antibody prophylaxis confers rapid and durable protective immunity against Zika virus challenge.Human vaccines & immunotherapeutics · 2020Article
- Inflammasome Fuels Dengue Severity.Frontiers in cellular and infection microbiology · 2020Review
- The Neutralizing Antibody Response Elicited by Tembusu Virus Is Affected Dramatically by a Single Mutation in the Stem Region of the Envelope Protein.Frontiers in microbiology · 2020Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
The envelope (E) of dengue virus (DENV) is a determinant of tropism and virulence. At the C terminus of E protein, there is a stem region containing two amphipathic α-helical domains (EH1 and EH2) and a stretch of conserved sequences in between. The crystal structure of E protein at the postfusion state suggested the involvement of the stem during the fusion; however, the critical domains or residues involved remain unknown. Site-directed mutagenesis was carried out to replace each of the stem residues at the hydrophobic face with an alanine or proline in a DENV serotype 4 (DENV4) precursor membrane (prM)/E expression construct. Most of the 15 proline mutations at either EH1 or EH2 severely affected the assembly of virus-like particles (VLPs). Radioimmunoprecipitation and membrane flotation assays revealed that EH1 mutations primarily affect prM-E heterodimerization and EH2 mutations affect the membrane binding of the stem. Introducing four proline mutations at either EH1 or EH2 into a DENV2 replicon packaging system greatly affects assembly and entry. Moreover, introducing these mutations into a DENV2 infectious clone confirmed the impairment in assembly and infectivity. Sequencing analysis of adaptive mutations in passage 5 viruses revealed a change to a leucine or wild-type residue at the original site, suggesting the importance of maintaining the helical structure. Collectively, these findings suggest that the EH1 and EH2 domains are involved in both assembly and entry steps of the DENV replication cycle; this feature, together with the high degree of sequence conservation, suggests that the stem region is a potential target of antiviral strategies.
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