Isolation and characterization of a serine protease from the nematophagous fungus, Lecanicillium psalliotae, displaying nematicidal activity.
Lecanicillium psalliotae produced an extracellular protease (Ver112) which was purified to apparent homogeneity giving a single band on SDS-PAGE with a molecular mass of 32 kDa. The optimum activity of Ver112 was at pH 10 and 70 degrees C (over 5 min). The purified protease degraded a broad range of substrates including casein, gelatin, and nematode cuticle with 81% of a nematode (Panagrellus redivivus) being degraded after treating with Ver112 for 12 h. The protease was highly sensitive to PMSF (1 mM) indicating it to be a serine protease. The N-terminal amino acid residues of Ver112 shared a high degree of similarity with other cuticle-degrading proteases from nematophagous fungi which suggests a role in nematode infection.
Yang
Jinkui
J
Laboratory for Conservation and Utilization of Bio-resources, Yunnan University, 650091, Kunming, P. R. China.
Huang
Xiaowei
X
Tian
Baoyu
B
Wang
Miao
M
Niu
Qiuhong
Q
Zhang
Keqin
K
D000595:Amino Acid Sequence; D000818:Animals; D000969:Antinematodal Agents / Q000494:pharmacology; D001203:Ascomycota / Q000378:metabolism*; D002364:Caseins / Q000737:chemistry; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000737:chemistry; D005780:Gelatin / Q000737:chemistry; D005800:Genes, Fungal; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D008969:Molecular Sequence Data; D009348:Nematoda; D010447:Peptide Hydrolases / Q000737:chemistry / Q000302:isolation & purification*; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry*; D013696:Temperature; D013997:Time Factors; D014105:Tosyl Compounds / Q000737:chemistry
D000969:Antinematodal Agents; D002364:Caseins; D005656:Fungal Proteins; D014105:Tosyl Compounds; C003614:4-toluenesulfonyl fluoride; D005780:Gelatin; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases