Cordysobin, a novel alkaline serine protease with HIV-1 reverse transcriptase inhibitory activity from the medicinal mushroom Cordyceps sobolifera

文献类型: 外文期刊

第一作者: Wang, Shou-Xian

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

作者机构:

关键词: Alkaline serine protease;Fruiting bodies;Mushroom;Cordyceps sobolifera;Purification;H1V-1 reverse transcriptase

期刊名称:JOURNAL OF BIOSCIENCE AND BIOENGINEERING ( 影响因子:2.894; 五年影响因子:2.746 )

ISSN:

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收录情况: SCI

摘要: A novel serine protease, designated as cordysobin, was purified from dried fruiting bodies of the mushroom Cordyceps sobolifera. The isolation procedure utilized ion exchange chromatography on DEAE-cellulose and SP-Sepharose followed by gel filtration on Superdex 75. The protease did not adsorb on DEAE-cellulose but bound to SP-Sepharose. In sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), the protease resolved as a single band with an apparent molecular mass of 31 kDa. Its optimal pH was 10.0, and the optimal temperature was 65°C. The protease displayed a Km value of 0.41 uM and 13.44 μM·min~(-1) using Suc-Leu-Leu-Val-Tyr-MCA as substrate at pH 10.0 and 37°C. Protease activity was enhanced by the Fe~(2+) ion at low concentration range of 1.25-10 mM and was strongly inhibited by Hg~(2+) up to 1.25 mM. The protease was strongly inhibited by chymostatin and phenylmethylsulfonyl fluoride (PMSF), suggesting that it is a serine protease. It manifested significant inhibitory activity toward HIV-1 reverse transcriptase (RT) with an IC_(50) value of 8.2x10~(-3) μM, which is the highest anti-HTV-1 RT activity of reported mushroom proteins.

分类号: Q5

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