期刊
ANTIVIRAL RESEARCH
卷 80, 期 1, 页码 11-22出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.antiviral.2008.05.004
关键词
flaviviruses; dengue virus; West Nile virus; envelope glycoprotein; antiviral therapy
资金
- NIH/NIAID Regional Center of Excellence for Bio-defense and Emerging Infectious Dieseases Research (RCE) program
- Region V 'Great Lakes' RCE [1-U54-Al-057153]
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [U54AI057153] Funding Source: NIH RePORTER
With the emergence and rapid spread of West Nile virus in the United States since 1999, and the 50-100 million infections per year caused by dengue virus globally, the threat of flaviviruses as re-emerging human pathogens has become a reality. To support the efforts that are currently being pursued to develop effective vaccines against these Viruses, researchers are also actively Pursuing the development of small molecule compounds that target various aspects of the virus life cycle. Recent advances in the structural characterization of the flaviviruses have provided a strong foundation towards these efforts. These studies have provided the pseudo-atomic structures of virions from several members of the genus as well as atomic resolution structures of several viral proteins. Most importantly, these studies have highlighted specific structural rearrangements that occur within the virion that are necessary for the virus to complete its life cycle. These rearrangements occur when the virus must transition from immature, to mature, to fusion-active states and rely heavily on the conformational flexibility of the envelope (E) Protein that forms the outer glycoprotein shell of the virus. Analysis of these conformational changes can suggest promising targets for structure-based antiviral design. For instance, by targeting the flexibility of the E protein, it might be possible to inhibit required rearrangements of this Protein and trap the virus in a specific state. This would interfere with a productive flaviviral infection. This review presents a Structural perspective of the flavivirus life cycle and focuses on the role of the E protein as an opportune target for structure-based antiviral drug design. Published by Elsevier B.V.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据