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西尼罗河病毒可被次氯酸修饰的人血清白蛋白中和,该白蛋白与病毒包膜蛋白E的结构域III结合。

West Nile virus is neutralized by HOCl-modified human serum albumin that binds to domain III of the viral envelope protein E.

作者信息

Vossmann Markus, Kirst Martin, Ludolfs Diana, Schreiber Michael

机构信息

Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard Nocht Str. 74, 20359 Hamburg, Germany.

出版信息

Virology. 2008 Apr 10;373(2):322-8. doi: 10.1016/j.virol.2007.12.008. Epub 2008 Jan 14.

DOI:10.1016/j.virol.2007.12.008
PMID:18191981
Abstract

The outbreaks of West Nile virus (WNV), an emerging flavivirus recently implicated in outbreaks of fatal encephalitis, necessitate the development of effective anti-WNV drugs. In this study, it is demonstrated that human serum albumin is transformed into a WNV antiviral substance by hypochlorite (HOCl) modification. The HOCl-modified albumin efficiently neutralized WNV in vitro (EC50=300 nM) and showed binding to a recombinant protein, representing the domain III of the WNV external envelope E glycoprotein.

摘要

西尼罗河病毒(WNV)是一种新出现的黄病毒,最近与致命性脑炎的爆发有关,其爆发使得开发有效的抗WNV药物成为必要。在本研究中,证明了人血清白蛋白通过次氯酸盐(HOCl)修饰转化为一种WNV抗病毒物质。HOCl修饰的白蛋白在体外能有效中和WNV(EC50=300 nM),并显示出与一种重组蛋白结合,该重组蛋白代表WNV外膜E糖蛋白的结构域III。

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West Nile virus is neutralized by HOCl-modified human serum albumin that binds to domain III of the viral envelope protein E.西尼罗河病毒可被次氯酸修饰的人血清白蛋白中和,该白蛋白与病毒包膜蛋白E的结构域III结合。
Virology. 2008 Apr 10;373(2):322-8. doi: 10.1016/j.virol.2007.12.008. Epub 2008 Jan 14.
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