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腾讯登录Nat Biotechnol：抗流感病毒的新方法
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目前，一个国际研究小组已经制造出一种新的蛋白质，它能抗击致命性流感的流行。
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新方法的相关论文发表在期刊Nature Biotechnology上，并被定为该期刊的封面文章，它报道了一种新的基因工程方法，即用工程化基因作为抗病毒药物，使流感病毒关键功能丧失，其有效性已经在许多大流行性流感病毒的易感位点上得到证实。
在前期研究中，研究小组利用计算机辅助设计来工程化一些蛋白质，使它们靶向高适应性病毒的易感位点。在本研究中，研究小组应用DNA浓度测序技术，同时对数百万的工程化蛋白质测序分析，鉴定有益突变，综合绘制出蛋白质突变图谱，了解这些突变在蛋白质攻击病毒特定区域时是否会使蛋白质占优势，然后优化蛋白质的性能。这一研究示范了一种构建治疗性蛋白的新方法，将促进生物制药企业发展新的蛋白药物，为将来治疗所有流感病毒、天花及其他疾病奠定了基础。
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<img src="http://www.bioon.com/biology/UploadFiles/201205/2012052811123131.gif" alt="" width="113" height="149" border="0" hspace="0" />
<a title="" href="http://dx.doi.org/10.1038/nbt.2214" target="_blank">doi:10.1038/nbt.2214</a>
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<br/><strong>Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing</strong><br/>
Timothy A Whitehead, Aaron Chevalier, Yifan Song, Cyrille Dreyfus, Sarel J Fleishman, Cecilia De Mattos, Chris A Myers, Hetunandan Kamisetty, Patrick Blair, Ian A Wilson & David Baker
We show that comprehensive sequence-function maps obtained by deep sequencing can be used to reprogram interaction specificity and to leapfrog over bottlenecks in affinity maturation by combining many individually small contributions not detectable in conventional approaches. We use this approach to optimize two computationally designed inhibitors against H1N1 influenza hemagglutinin and, in both cases, obtain variants with subnanomolar binding affinity. The most potent of these, a 51-residue protein, is broadly cross-reactive against all influenza group 1 hemagglutinins, including human H2, and neutralizes H1N1 viruses with a potency that rivals that of several human monoclonal antibodies, demonstrating that computational design followed by comprehensive energy landscape mapping can generate proteins with potential therapeutic utility.
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<div> <br/>来源：生物谷</div>
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<div id="region-column1and2-layout2">
<p align="center"><img src="http://www.bioon.com/biology/UploadFiles/201205/2012052811124793.jpg" alt="" width="270" height="200" border="0" /></p>
<div id="ztload"> </div>
目前，一个国际研究小组已经制造出一种新的蛋白质，它能抗击致命性流感的流行。
<!--more-->
新方法的相关论文发表在期刊Nature Biotechnology上，并被定为该期刊的封面文章，它报道了一种新的基因工程方法，即用工程化基因作为抗病毒药物，使流感病毒关键功能丧失，其有效性已经在许多大流行性流感病毒的易感位点上得到证实。
在前期研究中，研究小组利用计算机辅助设计来工程化一些蛋白质，使它们靶向高适应性病毒的易感位点。在本研究中，研究小组应用DNA浓度测序技术，同时对数百万的工程化蛋白质测序分析，鉴定有益突变，综合绘制出蛋白质突变图谱，了解这些突变在蛋白质攻击病毒特定区域时是否会使蛋白质占优势，然后优化蛋白质的性能。这一研究示范了一种构建治疗性蛋白的新方法，将促进生物制药企业发展新的蛋白药物，为将来治疗所有流感病毒、天花及其他疾病奠定了基础。
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<div>
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<img src="http://www.bioon.com/biology/UploadFiles/201205/2012052811123131.gif" alt="" width="113" height="149" border="0" hspace="0" />
<a title="" href="http://dx.doi.org/10.1038/nbt.2214" target="_blank">doi:10.1038/nbt.2214</a>
PMC:
PMID:
</div>
<div>
<br/><strong>Optimization of affinity, specificity and function of designed influenza inhibitors using deep sequencing</strong><br/>
Timothy A Whitehead, Aaron Chevalier, Yifan Song, Cyrille Dreyfus, Sarel J Fleishman, Cecilia De Mattos, Chris A Myers, Hetunandan Kamisetty, Patrick Blair, Ian A Wilson & David Baker
We show that comprehensive sequence-function maps obtained by deep sequencing can be used to reprogram interaction specificity and to leapfrog over bottlenecks in affinity maturation by combining many individually small contributions not detectable in conventional approaches. We use this approach to optimize two computationally designed inhibitors against H1N1 influenza hemagglutinin and, in both cases, obtain variants with subnanomolar binding affinity. The most potent of these, a 51-residue protein, is broadly cross-reactive against all influenza group 1 hemagglutinins, including human H2, and neutralizes H1N1 viruses with a potency that rivals that of several human monoclonal antibodies, demonstrating that computational design followed by comprehensive energy landscape mapping can generate proteins with potential therapeutic utility.
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</div>
</div>
<div> <br/>来源：生物谷</div>
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