Experimental Therapeutics Centre, Agency for Science, Technology and Research (A∗STAR), Singapore 138669, Singapore.
Biochem Biophys Res Commun. 2012 Jul 13;423(4):799-804. doi: 10.1016/j.bbrc.2012.06.043. Epub 2012 Jun 16.
West Nile Virus (WNV) protease is a two-component protease, important for the maturation of virus by cleaving the viral ploypeptide into functional proteins. WNV protease contains a Nonstructural (NS) protein 3 possessing the protease active sites and is regulated by a cofactor region containing approximately 40 amino acids from an integral membrane protein, NS2B. Although NS2B was demonstrated to be important for the location of the protease on the membrane, there was no direct evidence to show the interaction between protease (NS3) and membrane. Herein, we investigated the interaction between WNV protease and dodecylphosphocoline (DPC) micelles using NMR spectroscopy. The results showed that amino acids (31-33) from NS3 were important for the interaction with detergent micelles, which was similar to the finding in the study of protease from Dengue virus. This region may serve as an anchoring site to stabilized NS3 protease domain on the membrane.
西尼罗河病毒（WNV）蛋白酶是一种由两个亚基组成的蛋白酶，对于通过切割病毒多聚蛋白成功能性蛋白来成熟病毒非常重要。WNV 蛋白酶包含非结构（NS）蛋白 3，其具有蛋白酶活性位点，并受包含大约 40 个氨基酸的辅助因子区域调节，该区域来自整合膜蛋白 NS2B。尽管已经证明 NS2B 对于蛋白酶在膜上的定位很重要，但没有直接证据表明蛋白酶（NS3）和膜之间的相互作用。在此，我们使用 NMR 光谱法研究了 WNV 蛋白酶和十二烷基磷酸胆碱（DPC）胶束之间的相互作用。结果表明，NS3 中的氨基酸（31-33）对于与去污剂胶束的相互作用很重要，这与登革热病毒蛋白酶研究的发现相似。该区域可能作为一个锚定点，将 NS3 蛋白酶结构域稳定在膜上。
