Role of the cytosolic tails of Rift Valley fever virus envelope glycoproteins in viral morphogenesis
Role of the cytosolic tails of Rift Valley fever virus envelope glycoproteins in viral morphogenesis
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DOI：
10.1016/j.virol.2013.09.023
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发表时间：
2014-01-05
期刊：
影响因子：
3.7
通讯作者：
Bouloy, Michele
中科院分区：
文献类型：
--
作者：
Carnec, Xavier;Ermonval, Myriam;Bouloy, Michele
裂谷热病毒（RVFV）囊膜糖蛋白Gn/Gc的正确折叠、异源二聚体化和运输对病毒颗粒的高尔基体组装和出芽至关重要。Gn和Gc羧基末端分别含有高尔基体靶向和ER-检索信号。我们产生的RVFV样颗粒突变的胞质尾部的Gn或Cc和确定的区域重要的感染性颗粒的释放。通过反向遗传学创建重组突变病毒，进一步研究了这些区域中特定氨基酸的作用。在高尔基体靶向基序之外的残基，即二赖氨酸K29-K30基序和Gn胞质结构域的N43、R44和146残基，对于高尔基体定位和RNP包装似乎是重要的。关于Cc尾，双赖氨酸基序中K2或K3的替换对Gn运输产生了剧烈的影响，并诱导了重要的细胞器重新分布和细胞重塑，极大地影响了颗粒的形成和释放。(C)2013 Elsevier Inc. All rights reserved.
The correct folding, heterodimerization and trafficking of Gn/Gc envelope glycoproteins of Rift Valley fever virus, RVFV (Bunyaviridae and Phlebovirus genus) are essential for Golgi assembly and budding of viral particles. The Gn and Gc carboxy-terminus contain a Golgi targeting and an ER-retrieval signal, respectively. We generated RVFV-like particles with mutations in the cytosolic tails of Gn or Cc and identified regions important for release of infectious particles. The role of specific amino-acids in these regions was further investigated by creating recombinant mutant viruses by reverse-genetics. Residues outside the suspected Golgi targeting motif, i.e. the di-lysine K29-K30 motif and the N43, R44 and 146 residues of the Gn cytosolic domain, appeared important for Golgi localization and RNP packaging. Concerning the Cc tail, replacement of K2 or K3 in the di-lysine motif, had a drastic impact on Gn trafficking and induced an important organelle redistribution and cell remodeling, greatly affecting particle formation and release. (C) 2013 Elsevier Inc. All rights reserved.