Venture from the Interior-Herpesvirus pUL31 Escorts Capsids from Nucleoplasmic Replication Compartments to Sites of Primary Envelopment at the Inner Nuclear Membrane.

Venture from the Interior-Herpesvirus pUL31 Escorts Capsids from Nucleoplasmic Replication Compartments to Sites of Primary Envelopment at the Inner Nuclear Membrane.
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DOI:
10.3390/cells6040046
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发表时间:
2017-11-25
期刊:
影响因子:
6
通讯作者:
Bailer SM
Bailer SM
中科院分区:
生物学2区
文献类型:
--
作者:
Bailer SM

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疱疹病毒衣壳的装配起始于被感染细胞的核质中。大小限制要求新形成的病毒核衣壳通过进化上保守的称为核出口的囊泡运输机制离开细胞核。成熟的衣壳从核质中释放出来,参与一个膜介导的出芽过程,包括在内核膜上的初级出芽和在外核膜上的去出芽。一旦在细胞质中,衣壳接受它们的次级包膜以成熟为感染性病毒体。在疱疹病毒家族中保守的两种病毒蛋白质,整合膜蛋白pUL34和磷蛋白pUL31,形成衣壳从感染的细胞核运输到细胞质所需的核出口复合物。核出口复合物的形成导致膜囊泡的出芽,揭示了其作为最小病毒编码的膜出芽和断裂机制的功能。最近的结构分析揭示了异二聚体核出口复合物的细节,以及它在出芽囊泡内部形成的六边形外壳,以驱动初级萌发。通过这篇综述,我想提出的衣壳护送模型,其中pUL31与衣壳在核质复制室护送到网站的主要表现,从而耦合衣壳成熟和核出口。
Herpesviral capsid assembly is initiated in the nucleoplasm of the infected cell. Size constraints require that newly formed viral nucleocapsids leave the nucleus by an evolutionarily conserved vescular transport mechanism called nuclear egress. Mature capsids released from the nucleoplasm are engaged in a membrane-mediated budding process, composed of primary envelopment at the inner nuclear membrane and de-envelopment at the outer nuclear membrane. Once in the cytoplasm, the capsids receive their secondary envelope for maturation into infectious virions. Two viral proteins conserved throughout the herpesvirus family, the integral membrane protein pUL34 and the phosphoprotein pUL31, form the nuclear egress complex required for capsid transport from the infected nucleus to the cytoplasm. Formation of the nuclear egress complex results in budding of membrane vesicles revealing its function as minimal virus-encoded membrane budding and scission machinery. The recent structural analysis unraveled details of the heterodimeric nuclear egress complex and the hexagonal coat it forms at the inside of budding vesicles to drive primary envelopment. With this review, I would like to present the capsid-escort-model where pUL31 associates with capsids in nucleoplasmic replication compartments for escort to sites of primary envelopment thereby coupling capsid maturation and nuclear egress.
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