Inhibition of West Nile virus entry by using a recombinant domain III from the envelope glycoprotein.

作者: J. J. H. Chu , R. Rajamanonmani , J. Li , R. Bhuvanakantham , J. Lescar

DOI: 10.1099/VIR.0.80411-0

关键词:

摘要: The envelope glycoprotein located at the outermost surface of flavivirus particle mediates entry virus into host cells. In this study, involvement domain III West Nile (WNV-DIII) protein in binding to cell was investigated. WNV-DIII first expressed as a recombinant and purified after solubilization refolding procedure. refolded displays content β-sheets consistent with known homologous structures other DIII, shown by using circular dichroism analysis. Purified able inhibit WNV Vero cells C6/36 mosquito Recombinant only partially blocked dengue-2 (Den 2) However, Den 2 effectively WNV-DIII. Murine polyclonal serum produced against inhibited infection much lesser extent virus, demonstrated plaque neutralization assays. Together these results provided strong evidence that immunoglobulin-like DIII is responsible for receptor on data also suggest similar attachment molecule(s) or receptor(s) were used

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