A mutant fusion (F) protein of simian virus 5 induces hemagglutinin-neuraminidase-independent syncytium formation despite the internalization of the F protein
A mutant fusion (F) protein of simian virus 5 induces hemagglutinin-neuraminidase-independent syncytium formation despite the internalization of the F protein
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DOI：
10.1016/j.virol.2005.11.014
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发表时间：
2006-03-30
期刊：
影响因子：
3.7
通讯作者：
Ito, Y
中科院分区：
文献类型：
--
作者：
Tsurudome, M;Ito, M;Ito, Y
猴病毒5型毒株W3 A的融合（F）蛋白诱导合胞体形成，与血凝素-神经氨酸酶蛋白的共表达无关。通过用W3 A F对应物脯氨酸替换22位的亮氨酸，这种性质可以转移到WR菌株的F蛋白。所得突变体L22 P具有不同于WR F蛋白的构象。Se-L22 P是L22 P的切割位点突变体，其仅可通过添加外源胰蛋白酶来切割。我们在此表明，细胞表面定位的L22 P以25 min的t（1/2）内化并在细胞中降解，而WR F蛋白则没有。细胞表面定位的Se-L22 P经历了一个显着的构象变化后裂解。有趣的是，它从细胞表面消失的线索，其内在化，同时诱导广泛的合胞体形成。这些结果表明，L22 P在融合诱导过程中可能显示所有的内化信号。(C)2005年爱思唯尔公司All rights reserved.
The fusion (F) protein of simian virus 5 strain W3A induces syncytium formation independently of coexpression of the hemagglutinin-neuraminidase protein. This property call be transferred to the F protein; of strain WR by replacing the leucine at position 22 with the W3A F counterpart, proline. The resulting mutant L22P has a conformation that is distinct from that of the WR F protein. Se-L22P is a cleavage site Mutant of L22P that is cleavable only by addition of exogenous trypsin. We showed here that the cell surface-localized L22P was internalized with a t(1/2) Of 25 min and degraded in the cell, while the WR F protein was not. The cell surface-localized Se-L22P underwent a significant conformational change upon cleavage. Intriguingly, it disappeared from the cell Surface clue to its internalization, while inducing extensive syncytium formation. These results indicate that L22P may display all internalization signal during the course of fusion induction. (C) 2005 Elsevier Inc. All rights reserved.