A mature and fasogenic form of the Nipah requires proteolytic processing by virus fusion protein cathepsin L
A mature and fasogenic form of the Nipah requires proteolytic processing by virus fusion protein cathepsin L
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DOI：
10.1016/j.virol.2006.01.007
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发表时间：
2006-03-15
期刊：
影响因子：
3.7
通讯作者：
Dutch, RE
中科院分区：
文献类型：
--
作者：
Pager, CT;Craft, WW;Dutch, RE
尼帕病毒融合（F）蛋白经蛋白水解加工成F-1 + F-2亚基。我们在这里证明，组织蛋白酶L参与这一重要的成熟事件。组织蛋白酶抑制剂消融Nipah F的裂解。在表达组织蛋白酶L shRNA的Vero细胞中，Nipah F的蛋白水解加工和融合活性显着降低。此外，尼帕病毒F介导的融合在组织蛋白酶L缺陷细胞中被抑制，但组织蛋白酶L的共表达恢复了融合活性。纯化的组织蛋白酶L和B都能切割免疫纯化的Nipah F蛋白，但只有组织蛋白酶L能产生大小正确的产物。我们的研究结果表明，内体组织蛋白酶可以切割尼帕F，但组织蛋白酶L特异性地将尼帕F转化为成熟的融合形式。(C)2006年爱思唯尔公司All rights reserved.
The Nipah virus fusion (F) protein is proteolytically processed to F-1 + F-2 subunits. We demonstrate here that cathepsin L is involved in this important maturation event. Cathepsin inhibitors ablated cleavage of Nipah F. Proteolytic processing of Nipah F and fusion activity was dramatically reduced in cathepsin L shRNA-expressing Vero cells. Additionally, Nipah virus F-mediated fusion was inhibited in cathepsin L-deficient cells, but coexpression of cathepsin L restored fusion activity. Both purified cathepsin L and B Could cleave immunopurified Nipah F protein, but only cathepsin L produced products of the correct size. Our results suggest that endosomal cathepsins can cleave Nipah F, but that cathepsin L specifically converts Nipah F to a mature and fusogenic form. (C) 2006 Elsevier Inc. All rights reserved.