Purification and Characterization of a New Ribosome Inactivating Protein from Cinchonaglycoside C-treated Tobacco Leaves |
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| Authors: | Yanmei Li Yantao Jia Zhongkai Zhang Xiaoying Chen Hongping He Rongxiang Fang Xiaojiang Hao |
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| Institution: | ( State Key Laboratory of Photochemistry and Plant Resources in West China, Kunming Institute of Botany, the Chinese Academy of Sciences, Kunming 650204, China;;State Key Laboratory of Plant Genomics, Institute of Microbiology, the Chinese Academy of Sciences, Beijing 100080, China;;Laboratory of Plant Virology, Yunnan Academy of Agricultural Science, Kunming 650223, China;;The Graduate School of the Chinese Academy of Sciences, Beijing 100049, China;) |
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| Abstract: | A new ribosome-inactivating protein (RIP) with a molecular weight of 31 kDa induced by Cinchonaglycoside C (1) designated CIP31, was isolated from tobacco leaves. Analysis of this protein sequence indicated that it belongs to the RIP family and it was distinct from the other plant RIPs reported previously at its N-terminal amino acid sequence. CIP31 can directly impair synthesis of coat protein (CP) of tobacco mosaic virus (TMV), which resulted in inhibition of TMV long distance movement and multiplication in tobacco plants at concentrations of ng/mL. Furthermore, no toxicity was shown to the growth and fertility of the plants. CIP31 was synthesized only in the presence of Cinchonaglycoside C (1) and was independent of the salicylic acid (SA) signal pathway. We provided evidence for the SA-independent biological induction of resistance. |
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| Keywords: | antiviral protein Cinchonaglycoside C(1) coat protein medical plant ribosome inactivating protein salicylic acid tobacco mosaic virus |
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