ArticleVirus genes2007
Computational analysis and identification of amino acid sites in dengue E proteins relevant to development of diagnostics and vaccines.
Article in Virus genes, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 39 citations in OpenAlex.
- Machine learning, network pharmacology, and molecular dynamics reveal potent cyclopeptide inhibitors against dengue virus proteins.Molecular diversity · 2025Article
- Seropositivity among Blood Samples Drawn from Suspected Dengue Cases at a Tertiary Care Centre of Nepal: A Descriptive Cross-sectional Study.JNMA; journal of the Nepal Medical Association · 2022Article
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- Protein- and Peptide-Based Virus Inactivators: Inactivating Viruses Before Their Entry Into Cells.Frontiers in microbiology · 2020Review
- Dynamics and binding interactions of peptide inhibitors of dengue virus entry.Journal of biological physics · 2019Article
- Peptides as Therapeutic Agents for Dengue Virus.International journal of medical sciences · 2017Review
- Computational analysis of perturbations in the post-fusion Dengue virus envelope protein highlights known epitopes and conserved residues in the Zika virus.F1000Research · 2016Article
- Synthetic B-Cell Epitopes Eliciting Cross-Neutralizing Antibodies: Strategies for Future Dengue Vaccine.PloS one · 2016Article
- Structure-function analysis of hepatitis C virus envelope glycoproteins E1 and E2.Journal of biomolecular structure & dynamics · 2015Article
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- Sulfated polysaccharide, curdlan sulfate, efficiently prevents entry/fusion and restricts antibody-dependent enhancement of dengue virus infection in vitro: a possible candidate for clinical application.PLoS neglected tropical diseases · 2013Article
- Inhibition of dengue virus entry into target cells using synthetic antiviral peptides.International journal of medical sciences · 2013Article
- Analysis of epitopes on dengue virus envelope protein recognized by monoclonal antibodies and polyclonal human sera by a high throughput assay.PLoS neglected tropical diseases · 2012Article
- Sequence signatures in envelope protein may determine whether flaviviruses produce hemorrhagic or encephalitic syndromes.Virus genes · 2009Article
- Antibodies to envelope glycoprotein of dengue virus during the natural course of infection are predominantly cross-reactive and recognize epitopes containing highly conserved residues at the fusion loop of domain II.Journal of virology · 2008Article
- Evolutionarily conserved protein sequences of influenza a viruses, avian and human, as vaccine targets.PloS one · 2007Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
We have identified 72 completely conserved amino acid residues in the E protein of major groups of the Flavivirus genus by computational analyses. In the dengue species we have identified 12 highly conserved sequence regions, 186 negatively selected sites, and many dengue serotype-specific negatively selected sites. The flavivirus-conserved sites included residues involved in forming six disulfide bonds crucial for the structural integrity of the protein, the fusion motif involved in viral infectivity, and the interface residues of the oligomers. The structural analysis of the E protein showed 19 surface-exposed non-conserved residues, 128 dimer or trimer interface residues, and regions, which undergo major conformational change during trimerization. Eleven consensus T(h)-cell epitopes common to all four dengue serotypes were predicted. Most of these corresponded to dengue-conserved regions or negatively selected sites. Of special interest are six singular sites (N(37), Q(211), D(215), P(217), H(244), K(246)) in dengue E protein that are conserved, are part of the predicted consensus T(h)-cell epitopes and are exposed in the dimer or trimer. We propose these sites and corresponding epitopic regions as potential candidates for prioritization by experimental biologists for development of diagnostics and vaccines that may be difficult to circumvent by natural or man-made alteration of dengue virus.
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