The recombinant serine protease XAoz1 of Arthrobotrys oligospora exhibits potent nematicidal activity against Caenorhabditis elegans and Haemonchus contortus. Issue 1 (13th May 2013)

• Record Type: Journal Article
• Authors: Junwei, Wang; Qingling, Meng; Jun, Qiao; Weisheng, Wang; Shuangqing, Chen; Jianxun, Luo; Chunguang, Zhao; Chuangfu, Chen
• Is Part Of: FEMS microbiology letters. Volume 344:Issue 1(2013:Jul.)
• Page Start: 53
• Page End: 59
• Publication Date: 2013-05-13
• Subjects: Microbiology -- Periodicals; 579
• DOI: 10.1111/1574-6968.12154
• Languages: English
• ISSNs: 0378-1097

Abstract

<abstract abstract-type="main" xml:lang="en" id="fml12154-abs-0001"> <title>Abstract</title> <p>The nematophagous fungus <italic>Arthrobotrys oligospora</italic> 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 <italic>A. oligospora </italic>XJ‐XAo1 was expressed in <italic>Pichia pastoris</italic> to assess the <italic>in vitro</italic> nematicidal activity of recombinant XAoz1 (reXAoz1) on <italic>Caenorhabditis elegans</italic> and <italic>Haemonchus contortus</italic>. 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 <italic>P.pastoris </italic>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 <italic>C. elegans</italic> and <italic>H. contortus</italic> by degrading their cuticles and inducing death.</p> </abstract>