Assembly of the Sindbis virus spike protein complex.
Assembly of the Sindbis virus spike protein complex.
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辛德比斯病毒刺突蛋白复合物的组装。
DOI：
10.1006/viro.1996.0229
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Brown,DT
中科院分区：
文献类型：
--
作者：
Mulvey,M;Brown,DT
辛德毕斯病毒糖蛋白E1和E2在病毒包膜内被组织成80个异二聚体的三聚体。使用脉冲追踪协议和化学交联剂，我们已经发现，E1和E2的前体，PE 2，迅速组装成异源二聚体，然后进入异源二聚体的三聚体后易位到内质网。E1在内质网内通过至少三个二硫键构型不同的中间体折叠成其成熟构象。PE 2可以与这些E1折叠中间体中的第二个配对。因此，剩余的E1折叠步骤发生在E1-PE 2多聚体开始形成之后。E1和PE 2之间的四级相互作用可能有助于指导E1的折叠。虽然尚未检测到PE 2折叠中间体，但我们发现PE 2在与E1配对之前与其他PE 2分子和/或未知宿主因子瞬时进入大的非共价复合物或聚集体。
The Sindbis virus glycoproteins E1 and E2 are organized into 80 trimers of heterodimers within the virus envelope. Using pulse–chase protocols and chemical crosslinkers, we have found that E1 and E2 precursor, PE2, rapidly assemble into heterodimers and then into trimers of heterodimers after translocation into the endoplasmic reticulum. E1 folds into its mature conformation within the endoplasmic reticulum via at least three intermediates differing in the configurations of their disulfide bonds. PE2 can pair with the second of these E1 folding intermediates. The remaining E1 folding steps, therefore, occur after E1–PE2 multimers begin to form. Quaternary interactions between E1 and PE2 may help guide the folding of E1. While no PE2 folding intermediates have yet been detected, we have found that PE2 transiently enters into large, noncovalent complexes or aggregates with other PE2 molecules and/or with unknown host factors prior to pairing with E1.