A conformational change in the adeno-associated virus type 2 capsid leads to the exposure of hidden VP1N termini
A conformational change in the adeno-associated virus type 2 capsid leads to the exposure of hidden VP1N termini
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DOI：
10.1128/jvi.79.9.5296-5303.2005
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发表时间：
2005-05-01
影响因子：
5.4
通讯作者：
Kleinschmidt, JA
中科院分区：
文献类型：
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作者：
Kronenberg, S;Böttcher, B;Kleinschmidt, JA
细小病毒的复杂感染过程至今尚未完全了解。磷脂酶a结构域在衣壳蛋白VP1独特的N端起着重要作用。基于腺相关病毒2型野生型衣壳与缺乏VP1或VP2衣壳的结构差异，我们通过电子冷冻显微镜发现VP1和VP2的N端参与了空颗粒和满颗粒衣壳内球粒的形成。在有限的热冲击下，VP1和可能的VP2暴露在满衣壳的外部，而不是空衣壳，这与衣壳内表面的球体消失有关。利用分子模型，我们讨论了全局组织的vp1唯一N端通过衣壳外五重对称轴通道释放的限制。
The complex infection process of parvoviruses is not well understood so far. An important role has been attributed to a phospholipase A, domain which is located within the unique N terminus of the capsid protein VP1. Based on the structural difference between adeno-associated virus type 2 wild-type capsids and capsids lacking VP1 or VP2, we show via electron cryomicroscopy that the N termini of VP1 and VP2 are involved in forming globules inside the capsids of empty and full particles. Upon limited heat shock, VP1 and possibly VP2 become exposed on the outsides of full but not empty capsids, which is correlated with the disappearance of the globules in the inner surfaces of the capsids. Using molecular modeling, we discuss the constraints on the release of the globularly organized VP1-unique N termini through the channels at the fivefold symmetry axes outside of the capsid.