为了正常的体验网站,请在浏览器设置里面开启Javascript功能!

埃博拉病毒感染之新见解

2013-08-06 2页 doc 20KB 18阅读

用户头像

is_584498

暂无简介

举报
埃博拉病毒感染之新见解海量资料下载 免费学习英语 www.englishvip.com/xinlw.htm (申请网址) The Ebola virus is among the deadliest viruses on the planet, killing up to 90% of those infected, and there are no approved vaccines or effective therapies. A study published by Cell Press on May 7th in the Biop...
埃博拉病毒感染之新见解
海量资料下载 免费学习英语 www.englishvip.com/xinlw.htm (申请网址) The Ebola virus is among the deadliest viruses on the planet, killing up to 90% of those infected, and there are no approved vaccines or effective therapies. A study published by Cell Press on May 7th in the Biophysical Journal reveals how the most abundant protein making up the Ebola virus -- viral protein 40 (VP40) -- allows the virus to leave host cells and spread infection to other cells throughout the human body. The findings could lay the foundation for the development of new drugs and strategies for fighting Ebola infection. "Little research is available on how the Ebola virus buds from the plasma(血浆) membrane of human cells," says senior study author Robert Stahelin of Indiana University School of Medicine. "By shedding light on this process, our study will help us to identify potential drug candidates that could interfere with this step in the viral life cycle." The Ebola virus is made up of seven proteins, including VP40, which plays a key role in enabling the virus to leave host cells and infect other cells in the human body. Past studies have shown that a part of VP40 called the C-terminal domain penetrates the plasma membrane surrounding host cells. But until now, it was not known exactly how VP40 binds to the plasma membrane to allow the virus to escape host cells. To address this question, Stahelin and his team made vesicles designed to mimic the plasma membrane of host cells and exposed these vesicles to VP40. Observing their interactions under the microscope, they found that VP40's C-terminal domain penetrates more than halfway into one layer of the vesicles. VP40 also caused the vesicle membranes to bend into the shape of the Ebola virus, paving the way for its escape. When the researchers mutated the C-terminal domain of VP40, the protein was much less effective at binding to and bending membranes and forming virus-like particles that could escape from host cells. Altogether, the findings reveal how VP40's C-terminal domain allows the Ebola virus to spread infection. "Currently, we are trying to find small molecules that can inhibit VP40 interactions with the plasma membrane," Stahelin says. "This effort could lead to the discovery of potential drug candidates that could form the basis of much-needed therapies for this deadly virus." “成千上万人疯狂下载。。。。。。 更多价值连城的绝密英语学习资料, 洛基内部秘密英语,技巧,策略 请在 网上 申请报名” 洛基国际英语 竭诚为您服务
/
本文档为【埃博拉病毒感染之新见解】,请使用软件OFFICE或WPS软件打开。作品中的文字与图均可以修改和编辑, 图片更改请在作品中右键图片并更换,文字修改请直接点击文字进行修改,也可以新增和删除文档中的内容。
[版权声明] 本站所有资料为用户分享产生,若发现您的权利被侵害,请联系客服邮件isharekefu@iask.cn,我们尽快处理。 本作品所展示的图片、画像、字体、音乐的版权可能需版权方额外授权,请谨慎使用。 网站提供的党政主题相关内容(国旗、国徽、党徽..)目的在于配合国家政策宣传,仅限个人学习分享使用,禁止用于任何广告和商用目的。

历史搜索

    清空历史搜索