ArticleScientific reports2016
Genome-wide analyses reveal a highly conserved Dengue virus envelope peptide which is critical for virus viability and antigenic in humans.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- Neutralizing antibody correlates of sequence specific dengue disease in a tetravalent dengue vaccine efficacy trial in Asia.Vaccine · 2022Trial
- Localized Inflammation in Dengue Vaccine-Induced Skin Rash Is Not Associated with Continuous Presence of Dengue Virus Genome.The Journal of investigative dermatology · 2025Article
- In Silico Evaluation of Potential Hit Molecules Against Multiple Serotypes of Dengue Virus Envelope Glycoprotein.Molecules (Basel, Switzerland) · 2025Article
- Three highly variable genome regions of the four dengue virus serotypes can accurately recapitulate the CDS phylogeny.MethodsX · 2022Article
- Identification of Dengue Virus Serotype 3 Specific Antigenic Sites Targeted by Neutralizing Human Antibodies.Cell host & microbe · 2020Article
- Identification of highly conserved, serotype-specific dengue virus sequences: implications for vaccine design.BMC genomics · 2019Article
- Designing antibody against highly conserved region of dengue envelope protein by in silico screening of scFv mutant library.PloS one · 2019Article
- Genetic Variation between Dengue Virus Type 4 Strains Impacts Human Antibody Binding and Neutralization.Cell reports · 2018Article
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 2 countries.
Funding
Abstract
Targeting regions of proteins that show a high degree of structural conservation has been proposed as a method of developing immunotherapies and vaccines that may bypass the wide genetic variability of RNA viruses. Despite several attempts, a vaccine that protects evenly against the four circulating Dengue virus (DV) serotypes remains elusive. To find critical conserved amino acids in dengue viruses, 120 complete genomes of each serotype were selected at random and used to calculate conservation scores for nucleotide and amino acid sequences. The identified peptide sequences were analysed for their structural conservation and localisation using crystallographic data. The longest, surface exposed, highly conserved peptide of Envelope protein was found to correspond to amino acid residues 250 to 270. Mutation of this peptide in DV1 was lethal, since no replication of the mutant virus was detected in human cells. Antibodies against this peptide were detected in DV naturally infected patients indicating its potential antigenicity. Hence, this study has identified a highly conserved, critical peptide in DV that is a target of antibodies in infected humans.
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