Alphavirus budding is dependent on the interaction between the nucleocapsid and hydrophobic amino acids on the cytoplasmic domain of the E2 envelope glycoprotein.
Alphavirus budding is dependent on the interaction between the nucleocapsid and hydrophobic amino acids on the cytoplasmic domain of the E2 envelope glycoprotein.
复制标题
甲病毒出芽依赖于核衣壳和 E2 包膜糖蛋白胞质结构域上的疏水性氨基酸之间的相互作用。
DOI：
10.1006/viro.1997.8480
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
Kuhn,RJ
中科院分区：
文献类型：
--
作者：
Owen,KE;Kuhn,RJ
核衣壳核心和糖蛋白刺突之间的相互作用是甲病毒出芽过程的关键组成部分。先前提出的分子模型表明这种相互作用是通过糖蛋白 E2 的胞质结构域与核衣壳蛋白表面上发现的疏水口袋的结合介导的[S.李，K.E. 欧文，H.-K。 Choi、H. Lee、G. Lu、G. Wengler、D. T. Brown、M. G. Rossmann 和 R. J. Kuhn (1996)Structure4, 531–541； U. Skoging、M. Vihinen、L. Nilsson 和 P. Liljeström (1996)Structure4, 519–529]。预计 E2 细胞质结构域中的两个疏水氨基酸对于蛋白质之间的接触非常重要。其中一个残基 Y400（辛德比斯病毒编号）先前已通过突变研究表明对于塞姆利基森林病毒 [H.赵、B. Lindqvist、H. Garoff、C. H. von Bonsdorf 和 P. Liljeström (1994)EMBO J.13, 4204–4211]。第二个残基 L402 的作用尚未得到研究。通过在该残基上创建一组氨基酸替换，然后对获救的突变病毒进行表型分析，我们现在表明 L402 对于辛德比斯病毒的产生至关重要。该氨基酸的取代会抑制出芽，数据表明 L402 在糖蛋白和核衣壳核心之间的相互作用中发挥重要作用。这些数据支持该模型，并表明所提出的分子相互作用对于甲病毒从细胞中出芽很重要。
The interaction between the nucleocapsid core and the glycoprotein spikes is a critical component in the budding process of alphaviruses. A molecular model was previously proposed which suggested that this interaction was mediated by the binding of the cytoplasmic domain of glycoprotein E2 into a hydrophobic pocket found on the surface of the nucleocapsid protein [S. Lee, K. E. Owen, H.-K. Choi, H. Lee, G. Lu, G. Wengler, D. T. Brown, M. G. Rossmann, and R. J. Kuhn (1996)Structure4, 531–541; U. Skoging, M. Vihinen, L. Nilsson, and P. Liljeström (1996)Structure4, 519–529]. Two hydrophobic amino acids in the cytoplasmic domain of E2 were predicted to be important in the contact between the proteins. One of the residues, Y400 (Sindbis virus numbering), had previously been shown by mutational studies to be important in the budding of Semliki Forest virus [H. Zhao, B. Lindqvist, H. Garoff, C. H. von Bonsdorf, and P. Liljeström (1994)EMBO J.13, 4204–4211]. The role of the second residue, L402, had not been examined. By creating a panel of amino acid substitutions at this residue, followed by phenotypic analysis of rescued mutant viruses, we now show that L402 is critical for the production of Sindbis virus. Substitutions at this amino acid inhibit budding, and the data suggest that L402 plays an important role in the interaction between the glycoprotein and the nucleocapsid core. These data support the model and suggest that the proposed molecular interactions are important for the budding of alphaviruses from the cell.