Plant Virology Research Center, College of Agriculture, Shiraz University, Shiraz, Iran.
Microb Pathog. 2020 Mar;140:103929. doi: 10.1016/j.micpath.2019.103929. Epub 2019 Dec 14.
An antiviral protein, designated Opuntin B, was purified from Prickly Pear (Opuntia ficus-indica (L.) Miller) Cladode by heat treatment of the extract, protein precipitation by ammonium sulfate treatment followed by ion-exchange chromatography. Assessment of enzymatic activity of the purified protein showed that it degrades total plant genomic RNA, while causing electrophoretic mobility shifting of Cucumber mosaic virus (CMV) RNAs. However, heat-denatured viral RNA became sensitive to degradation upon treatment with antiviral protein. Opuntin B had no DNase activity on native and heat-denatured apricot genomic DNA, and on PCR-amplified coat protein gene of CMV. Using CMV as prey protein and Opuntin B as bait protein, no interaction was found between the antiviral protein and viral coat protein in far western dot blot analysis.
一种抗病毒蛋白，命名为 Opuntin B，通过对提取物进行热处理、用硫酸铵处理进行蛋白质沉淀，然后进行离子交换层析，从仙人掌（Opuntia ficus-indica (L.) Miller）的茎中纯化出来。对纯化蛋白的酶活性评估表明，它降解总植物基因组 RNA，同时导致黄瓜花叶病毒 (CMV) RNA 的电泳迁移率发生变化。然而，经热处理失活的病毒 RNA 在经过抗病毒蛋白处理后变得易于降解。Opuntin B 对天然和热处理的杏基因组 DNA 以及对 CMV 的衣壳蛋白基因的 PCR 扩增产物均无 DNA 酶活性。在 far western dot blot 分析中，使用 CMV 作为 prey 蛋白和 Opuntin B 作为 bait 蛋白，未发现抗病毒蛋白与病毒衣壳蛋白之间存在相互作用。
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