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Peptide inhibitors of dengue virus and West Nile virus infectivity
- Source :
- Virology Journal, Vol 2, Iss 1, p 49 (2005)
- Publication Year :
- 2005
- Publisher :
- BMC, 2005.
-
Abstract
- Abstract Viral fusion proteins mediate cell entry by undergoing a series of conformational changes that result in virion-target cell membrane fusion. Class I viral fusion proteins, such as those encoded by influenza virus and human immunodeficiency virus (HIV), contain two prominent alpha helices. Peptides that mimic portions of these alpha helices inhibit structural rearrangements of the fusion proteins and prevent viral infection. The envelope glycoprotein (E) of flaviviruses, such as West Nile virus (WNV) and dengue virus (DENV), are class II viral fusion proteins comprised predominantly of beta sheets. We used a physio-chemical algorithm, the Wimley-White interfacial hydrophobicity scale (WWIHS) 1 in combination with known structural data to identify potential peptide inhibitors of WNV and DENV infectivity that target the viral E protein. Viral inhibition assays confirm that several of these peptides specifically interfere with target virus entry with 50% inhibitory concentration (IC50) in the 10 μM range. Inhibitory peptides similar in sequence to domains with a significant WWIHS scores, including domain II (IIb), and the stem domain, were detected. DN59, a peptide corresponding to the stem domain of DENV, inhibited infection by DENV (>99% inhibition of plaque formation at a concentrations of 99% inhibition at
- Subjects :
- Infectious and parasitic diseases
RC109-216
Subjects
Details
- Language :
- English
- ISSN :
- 1743422X and 98692690
- Volume :
- 2
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Virology Journal
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.f98692690eab4d9d85996f17b6eb85d7
- Document Type :
- article
- Full Text :
- https://doi.org/10.1186/1743-422X-2-49