A Single Herpesvirus Protein Can Mediate Vesicle Formation in the Nuclear Envelope
A Single Herpesvirus Protein Can Mediate Vesicle Formation in the Nuclear Envelope
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DOI：
10.1074/jbc.m114.627521
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发表时间：
2015-03-13
影响因子：
4.8
通讯作者：
Antonin, Wolfram
中科院分区：
文献类型：
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作者：
Lorenz, Michael;Vollmer, Benjamin;Antonin, Wolfram
疱疹病毒在细胞核中组装衣壳，并通过非常规囊泡介导的运输通过核膜排出。衣壳在内核膜上出芽进入核膜腔。产生的腔内囊泡与外核膜融合，将衣壳运送到细胞质。囊泡的形成需要两种病毒蛋白，尾锚定pUL34和其可溶性相互作用物pUL31。细胞蛋白质是否参与尚不清楚。使用巨大的单层囊泡，我们表明，pUL31和pUL34是足够的膜出芽和断裂。pUL 31的膜束缚可以绕过pUL 34的功能，这表明pUL 34是pUL 31膜募集所需的，但不是膜重塑所需的。pUL31可以通过在膜的内表面上寡聚而使膜向内变形，以形成收缩成囊泡的芽。因此，单个病毒蛋白可以介导膜出芽和脱落所需的所有事件。
Herpesviruses assemble capsids in the nucleus and egress by unconventional vesicle-mediated trafficking through the nuclear envelope. Capsids bud at the inner nuclear membrane into the nuclear envelope lumen. The resulting intralumenal vesicles fuse with the outer nuclear membrane, delivering the capsids to the cytoplasm. Two viral proteins are required for vesicle formation, the tail-anchored pUL34 and its soluble interactor, pUL31. Whether cellular proteins are involved is unclear. Using giant unilamellar vesicles, we show that pUL31 and pUL34 are sufficient for membrane budding and scission. pUL34 function can be bypassed by membrane tethering of pUL31, demonstrating that pUL34 is required for pUL31 membrane recruitment but not for membrane remodeling. pUL31 can inwardly deform membranes by oligomerizing on their inner surface to form buds that constrict to vesicles. Therefore, a single viral protein can mediate all events necessary for membrane budding and abscission.