Amino acids at the exposed C-terminus of the S coat protein of cowpea mosaic virus play different roles in particle formation and viral systemic movement.
Amino acids at the exposed C-terminus of the S coat protein of cowpea mosaic virus play different roles in particle formation and viral systemic movement.
复制标题
豇豆花叶病毒S外壳蛋白暴露的C末端氨基酸在颗粒形成和病毒全身运动中发挥不同的作用。
DOI：
10.1099/jgv.0.001285
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发表时间：
2019
期刊：
影响因子：
--
通讯作者：
Meshcheriakova Y
中科院分区：
文献类型：
--
作者：
Meshcheriakova Y
豇豆花叶病毒的二十面体衣壳由 60 个拷贝的大 (L) 和小 (S) 外壳蛋白亚基形成。 S 外壳蛋白的 24 个氨基酸 C 端肽可以进行蛋白水解切割，而不影响颗粒稳定性或感染性。诱变研究表明，该序列参与颗粒组装、病毒运动、RNA 衣壳化和基因沉默抑制。然而，尚不清楚这些过程如何相关，以及每个过程涉及序列的哪些部分。在这里，我们分析了S蛋白C端区域的突变对空病毒样颗粒组装和感染性病毒全身运动的影响。结果证实了切割位点附近带正电荷的氨基酸对于颗粒组装的重要性，并揭示了 C 端 11 个氨基酸对于病毒有效的全身运动非常重要。
The icosahedral capsid of cowpea mosaic virus is formed by 60 copies of the large (L) and small (S) coat protein subunits. The 24-amino-acid C-terminal peptide of the S coat protein can undergo proteolytic cleavage without affecting particle stability or infectivity. Mutagenic studies have shown that this sequence is involved in particle assembly, virus movement, RNA encapsidation and suppression of gene silencing. However, it is unclear how these processes are related, and which part(s) of the sequence are involved in each process. Here, we have analysed the effect of mutations in the C-terminal region of the S protein on the assembly of empty virus-like particles and on the systemic movement of infectious virus. The results confirmed the importance of positively charged amino acids adjacent to the cleavage site for particle assembly and revealed that the C-terminal 11 amino acids are important for efficient systemic movement of the virus.