The N-Terminal Region of the Readthrough Domain Is Closely Related to Aphid Vector Specificity of Soybean dwarf virus.
The N-Terminal Region of the Readthrough Domain Is Closely Related to Aphid Vector Specificity of Soybean dwarf virus.
复制标题
通读结构域的 N 末端区域与大豆矮化病毒的蚜虫载体特异性密切相关。
DOI：
10.1094/phyto.2003.93.12.1560
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发表时间：
2003
期刊：
影响因子：
3.2
通讯作者：
S. Hidaka
中科院分区：
文献类型：
--
作者：
Hidetaka Terauchi;K. Honda;N. Yamagishi;S. Kanematsu;K. Ishiguro;S. Hidaka
摘要 据推测，大豆矮化病毒（SbDV）开放阅读框5编码的通读结构域（RTD）的N端一半与介体特异性有关。为进一步研究这一假说，对17个SbDV分离物进行了蚜虫传播性测试，并对这些分离物的外壳蛋白（CP）以及RTD编码的其他蛋白的推导氨基酸序列进行了比较。分离物被区分为4个株系：YS株系，导致大豆黄化，可由茄无网蚜传播；DS株系，导致矮化，可由茄无网蚜传播；YP株系，导致黄化，可由豌豆蚜传播；DP株系，导致矮化，可由豌豆蚜传播。系统发育分析表明，CP和RTD序列C端一半的系统发育树包含相同症状类型的分离物簇，而RTD的N端一半的系统发育树包含相同蚜虫介体类型的分离物簇。这些结果与我们先前关于4个SbDV分离物完整核苷酸序列的数据一致，并有力地表明RTD氨基酸序列的N端一半与SbDV的蚜虫传播特异性之间存在密切关系。
ABSTRACT It has been speculated that the N-terminal half of the readthrough domain (RTD) encoded by open reading frame 5 of Soybean dwarf virus (SbDV) is related to the vector specificity. To further investigate this hypothesis, transmissibility via aphids was tested on 17 SbDV isolates and comparisons of the deduced amino acid sequences of the coat protein (CP) and other proteins encoded by the RTD were made between these isolates. Isolates were distinguished into four strains: YS, causing yellowing in soybean and transmittable by Aulacorthum solani; DS, causing dwarfing and transmittable by A. solani; YP, causing yellowing and transmittable by Acyrthosiphon pisum; and DP, causing dwarfing and transmittable by A. pisum. Phylogenetic analysis showed that the trees for the CP and the C-terminal half of the RTD sequences contained clusters of isolates of the same symptom type, whereas the tree for the N-terminal half of the RTD contained clusters of isolates of the same aphid vector type. These results agreed with our previous data of the complete nucleotide sequences of four SbDV isolates, and strongly indicated a close relationship between the N-terminal half of the RTD amino acid sequences and aphid transmission specificity of SbDV.