The recombinant serine protease XAoz1 of Arthrobotrys oligospora exhibits potent nematicidal activity against Caenorhabditis elegans and Haemonchus contortus

文献类型： 外文期刊

第一作者： Wang Junwei

作者： Wang Junwei;Meng Qingling;Qiao Jun;Wang Weisheng;Chen Shuangqing;Zhao Chunguang;Chen Chuangfu;Luo Jianxun

作者机构： Shihezi Univ, Coll Anim Sci & Technol, Key Lab Prevent Vet, Shihezi 832003, Xinjiang, Peoples R China;Chinese Acad Agr Sci, State Key Lab Vet Etiol Biol, Key Lab Vet Parasitol Gansu Prov, Lanzhou Vet Res Inst, Lanzhou, Gansu, Peoples R China

关键词： Arthrobotrys oligospora;Nematicidal activity;Pichia pastoris;Recombinant expression;Serine protease XAoz1

期刊名称：FEMS MICROBIOLOGY LETTERS （ 2020影响因子：2.742； 五年影响因子：2.856 ）

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收录情况： SCI

摘要： The nematophagous fungus Arthrobotrys oligospora is a potential biological agent against parasitic gastrointestinal nematodes. Its subtilisin-like serine proteases play an important role in nematode cuticle breach. In this study, the cDNA of the mature serine protease XAoz1 from A. oligospora XJ-XAo1 was expressed in Pichia pastoris to assess the in vitro nematicidal activity of recombinant XAoz1 (reXAoz1) on Caenorhabditis elegans and Haemonchus contortus. The cDNA sequence of the protease XAoz1 was amplified by reverse transcription polymerase chain reaction (RT-PCR) and inserted into the vector pPIC9K for expression in P. pastoris GS115. Our results show that the reXAoz1 had a molecular mass of 50 kDa after 3 days of 1.5%-methanol induction at 28 °C. The highest specific protease activity was achieved at 12 168 U mg~(-1) protein. The reXAoz1 had the highest hydrolytic activity at pH 6.5-9.5 with an optimal pH at 8.5. Moreover, the purified reXAoz1 displayed a highly toxic and biological activity to immobilize C. elegans and H. contortus by degrading their cuticles and inducing death.

分类号： Q93

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