2012
DOI: 10.1371/journal.pone.0050995
|View full text |Cite
|
Sign up to set email alerts
|

Release of Dengue Virus Genome Induced by a Peptide Inhibitor

Abstract: Dengue virus infects approximately 100 million people annually, but there is no available therapeutic treatment. The mimetic peptide, DN59, consists of residues corresponding to the membrane interacting, amphipathic stem region of the dengue virus envelope (E) glycoprotein. This peptide is inhibitory to all four serotypes of dengue virus, as well as other flaviviruses. Cryo-electron microscopy image reconstruction of dengue virus particles incubated with DN59 showed that the virus particles were largely empty,… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

1
80
0

Year Published

2014
2014
2022
2022

Publication Types

Select...
7
1

Relationship

1
7

Authors

Journals

citations
Cited by 75 publications
(85 citation statements)
references
References 35 publications
1
80
0
Order By: Relevance
“…The release of viral RNAs from viral particles was also assessed by an RNAse digestion assay. Hence, these results suggest that DN59 induces the formation of holes in viral membrane; however, this peptide did not cause the genome release of other RNA enveloped viruses and did not exhibit adverse effect on cell membrane [129].…”
Section: • • Inhibitors Of Membrane Fusion Peptidesmentioning
confidence: 75%
See 1 more Smart Citation
“…The release of viral RNAs from viral particles was also assessed by an RNAse digestion assay. Hence, these results suggest that DN59 induces the formation of holes in viral membrane; however, this peptide did not cause the genome release of other RNA enveloped viruses and did not exhibit adverse effect on cell membrane [129].…”
Section: • • Inhibitors Of Membrane Fusion Peptidesmentioning
confidence: 75%
“…[20, 46,49] Sulfated xylomannans Inhibition of virus adsorption and penetration [120] Heteropolysaccharide CrHWE Inhibition of virus adsorption and penetration [120] Chondroitin sulfate E Inhibition of virus adsorption and penetration [21] Curdlan sulfate Inhibition of virus adsorption and penetration [26] Polysaccharide K5 from Escherichia coli Inhibition of virus adsorption and penetration [22] Tannins: chebulagic acid and punicalagin Inhibition of virus adsorption and penetration [122] E hydrophobic pocket target peptides Inhibition of virus adsorption and penetration [123] Doxorubicin derivative: SA-17 Inhibition of virus binding and membrane fusion [124,125] E stem region target peptides Blockade of membrane fusion [126,127] E stem region target peptide: DN59 Release of viral RNAs from viral particles [128,129] E stem region target small molecule:1662G07…”
Section: Carrageenans Inhibition Of Virus Adsorption and Penetrationmentioning
confidence: 99%
“…Membrane-permeabilizing peptides have many potential applications, including their use as antibacterial, antifungal, and antiviral compounds, 15 as anticancer agents, 6,7 as drug delivery enhancers, 8 and as biosensors. 9,10 However, to realize their full potential, we must be able to rationally engineer or modulate their activity and membrane selectivity, objectives which are currently not possible because the mechanism of such peptides cannot yet be described with specific molecular models.…”
Section: Introductionmentioning
confidence: 99%
“…The membranotropic α 3 and α 4 in DENV4 67 has been studied extensively through mutational studies of the hydrophobic face 60, 61 . Another strategy using peptide mimetic (residues 412 to 444, named DN59) derived from these helices showed inhibition of flaviviruses by releasing genomic RNA 70, 71 . A similar study based on peptide mimetic of residues 419-447 (comprising the conserved stretch following α 3 and α 4) inhibited viral entry 72 .…”
Section: Resultsmentioning
confidence: 99%
“…The Edmundson wheel shows the amphipathic cationic nature of the stem helices. The hydrophobicity of residues in the hydrophobic face is an important determinant of virulence 61, 70, 71 . The conservation of the charged face of α 4 ( c and d ) is in contrast to several differences in the hydrophobic face.…”
Section: Resultsmentioning
confidence: 99%