Archives of Microbiology (2007) 188, 167-174
Jinkui Yang, Juan Li, Lianming Liang, Baoyu Tian, Ying Zhang, Chunmei Cheng and Ke-Qin Zhang (2007)
Cloning and characterization of an extracellular serine protease from the nematode-trapping fungus Arthrobotrys conoides
Archives of Microbiology 188 (2), 167-174
Abstract: An extracellular serine protease (Ac1) with a molecular mass of 35 kDa was purified from the nematode-trapping fungus Arthrobotrys conoides. The optimum activity of Ac1 is at pH 7.0 and 53.2°C (over 20 min). Ac1 can degrade a broad range of substrates including casein, gelatin, bovine serum albumin, collagen, and nematode cuticles. Moreover, the enzyme can immobilize the free-living nematode Panagrellus redivivus and the pine wood nematode Bursaphelenchus xylophilus, indicating Ac1 may be involved in infection against nematodes. The encoding gene of Ac1 contains one intron of 60-bp and two exons encoding a polypeptide of 411 amino acid residues. The deduced polypeptide sequence of Ac1 showed a high degree of similarity to two previously reported serine proteases PII and Mlx from other nematode-trapping fungi (81% aa sequence identity). However, three proteases Ac1, Aoz1 and Mlx showed optimum temperatures at 53.2, 45 and 65°C, respectively. Compared to PII, Ac1 appears to have a significantly higher activity against gelatin, bovine serum albumin, and non-denatured collagen. Moreover, our bioassay experiments showed that Ac1 is more effective at immobilizing P. redivivus than B. xylophilus.
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Research topic(s) for pests/diseases/weeds:
biocontrol - natural enemies
Research topic(s) for beneficials or antagonists:
molecular biology - genes
Pest and/or beneficial records:
Beneficial | Pest/Disease/Weed | Crop/Product | Country | Quarant.
|
---|---|---|---|---|
Bursaphelenchus xylophilus | ||||
Arthrobotrys conoides (antagonist) | Bursaphelenchus xylophilus |