Purification and Characterization of a Novel Lectin with Antiphytovirus Activities from the wild Mushroom Paxillus involutus

文献类型： 外文期刊

第一作者： Wang, Shou Xian

作者： Wang, Shou Xian;Zhao, Shuang;Xu, Feng;Zhou, Ying;Geng, Xiao Li;Liu, Yu;Wang, Shou Xian;Wang, He Xiang;Wang, Shou Xian;Wang, He Xiang;Zhang, Guo Qing

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关键词： Antiphytovirus activity;lectin;mushroom;Paxillus involutus;purification

期刊名称：PROTEIN AND PEPTIDE LETTERS （ 影响因子：1.89； 五年影响因子：1.528 ）

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收录情况： SCI

摘要： A novel lectin was isolated from the dried fruiting bodies of the wild mushroom Paxillus involutus. Isolation was conducted by anion exchange chromatography on DEAE-Cellulose, Q-Sepharose and gel filtration on Superdex 75 using a fast protein liquid chromatography (FPLC) system. This lectin had a molecular mass of 28 kDa and was composed of four identical subunits, each with a molecular mass of 7 kDa. N-terminal amino acid sequence of the P. involutus lectin was determined to be CTCAVFLNNTTVKS, which showed a low level of similarity to mushroom lectin sequences reported previously. The biochemical properties of this lectin were determined, and the hemagglutinating activity was inhibited by inulin and O-Nitrophenyl-p-D-galacto-pyranoside. Additionally, Ca~(2+), Zn~(2+), Cd~(2+), Fe~(2+), and Al~(3+) inhibited its hemagglutinating activity, while Cu~(2+) promoted this activity. This lectin exhibited poor thermostability and was sensitive to HC1, but it had a high tolerance to NaOH exposure. In terms of biological properties, this lectin manifested antiphytovirus activity towards tobacco mosaic virus (TMV) with a 70.61% inhibition at a concentration of 200 μg/mL. This lectin was devoid of inhibitory activities toward pathogenic fungi and HIV-1 reverse transcriptase, and antiproliferative activities were observed in tumor cell lines including lung cancer A-549 and human colon cancer HCT-8 cells.

分类号： Q51

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